BindingDB Reactant_set_id Ligand SMILES Ligand InChI Ligand InChI Key BindingDB MonomerID BindingDB Ligand Name Target Name Target Source Organism According to Curator or DataSource Ki (nM) IC50 (nM) Kd (nM) EC50 (nM) kon (M-1-s-1) koff (s-1) pH Temp (C) Curation/DataSource Article DOI BindingDB Entry DOI PMID PubChem AID Patent Number Authors Date of publication Date in BindingDB Institution Link to Ligand in BindingDB Link to Target in BindingDB Link to Ligand-Target Pair in BindingDB Ligand HET ID in PDB PDB ID(s) for Ligand-Target Complex PubChem CID PubChem SID ChEBI ID of Ligand ChEMBL ID of Ligand DrugBank ID of Ligand IUPHAR_GRAC ID of Ligand KEGG ID of Ligand ZINC ID of Ligand Number of Protein Chains in Target (>1 implies a multichain complex) BindingDB Target Chain Sequence 1 PDB ID(s) of Target Chain 1 UniProt (SwissProt) Recommended Name of Target Chain 1 UniProt (SwissProt) Entry Name of Target Chain 1 UniProt (SwissProt) Primary ID of Target Chain 1 UniProt (SwissProt) Secondary ID(s) of Target Chain 1 UniProt (SwissProt) Alternative ID(s) of Target Chain 1 UniProt (TrEMBL) Submitted Name of Target Chain 1 UniProt (TrEMBL) Entry Name of Target Chain 1 UniProt (TrEMBL) Primary ID of Target Chain 1 UniProt (TrEMBL) Secondary ID(s) of Target Chain 1 UniProt (TrEMBL) Alternative ID(s) of Target Chain 1 BindingDB Target Chain Sequence 2 PDB ID(s) of Target Chain 2 UniProt (SwissProt) Recommended Name of Target Chain 2 UniProt (SwissProt) Entry Name of Target Chain 2 UniProt (SwissProt) Primary ID of Target Chain 2 UniProt (SwissProt) Secondary ID(s) of Target Chain 2 UniProt (SwissProt) Alternative ID(s) of Target Chain 2 UniProt (TrEMBL) Submitted Name of Target Chain 2 UniProt (TrEMBL) Entry Name of Target Chain 2 UniProt (TrEMBL) Primary ID of Target Chain 2 UniProt (TrEMBL) Secondary ID(s) of Target Chain 2 UniProt (TrEMBL) Alternative ID(s) of Target Chain 2 BindingDB Target Chain Sequence 3 PDB ID(s) of Target Chain 3 UniProt (SwissProt) Recommended Name of Target Chain 3 UniProt (SwissProt) Entry Name of Target Chain 3 UniProt (SwissProt) Primary ID of Target Chain 3 UniProt (SwissProt) Secondary ID(s) of Target Chain 3 UniProt (SwissProt) Alternative ID(s) of Target Chain 3 UniProt (TrEMBL) Submitted Name of Target Chain 3 UniProt (TrEMBL) Entry Name of Target Chain 3 UniProt (TrEMBL) Primary ID of Target Chain 3 UniProt (TrEMBL) Secondary ID(s) of Target Chain 3 UniProt (TrEMBL) Alternative ID(s) of Target Chain 3 BindingDB Target Chain Sequence 4 PDB ID(s) of Target Chain 4 UniProt (SwissProt) Recommended Name of Target Chain 4 UniProt (SwissProt) Entry Name of Target Chain 4 UniProt (SwissProt) Primary ID of Target Chain 4 UniProt (SwissProt) Secondary ID(s) of Target Chain 4 UniProt (SwissProt) Alternative ID(s) of Target Chain 4 UniProt (TrEMBL) Submitted Name of Target Chain 4 UniProt (TrEMBL) Entry Name of Target Chain 4 UniProt (TrEMBL) Primary ID of Target Chain 4 UniProt (TrEMBL) Secondary ID(s) of Target Chain 4 UniProt (TrEMBL) Alternative ID(s) of Target Chain 4 BindingDB Target Chain Sequence 5 PDB ID(s) of Target Chain 5 UniProt (SwissProt) Recommended Name of Target Chain 5 UniProt (SwissProt) Entry Name of Target Chain 5 UniProt (SwissProt) Primary ID of Target Chain 5 UniProt (SwissProt) Secondary ID(s) of Target Chain 5 UniProt (SwissProt) Alternative ID(s) of Target Chain 5 UniProt (TrEMBL) Submitted Name of Target Chain 5 UniProt (TrEMBL) Entry Name of Target Chain 5 UniProt (TrEMBL) Primary ID of Target Chain 5 UniProt (TrEMBL) Secondary ID(s) of Target Chain 5 UniProt (TrEMBL) Alternative ID(s) of Target Chain 5 BindingDB Target Chain Sequence 6 PDB ID(s) of Target Chain 6 UniProt (SwissProt) Recommended Name of Target Chain 6 UniProt (SwissProt) Entry Name of Target Chain 6 UniProt (SwissProt) Primary ID of Target Chain 6 UniProt (SwissProt) Secondary ID(s) of Target Chain 6 UniProt (SwissProt) Alternative ID(s) of Target Chain 6 UniProt (TrEMBL) Submitted Name of Target Chain 6 UniProt (TrEMBL) Entry Name of Target Chain 6 UniProt (TrEMBL) Primary ID of Target Chain 6 UniProt (TrEMBL) Secondary ID(s) of Target Chain 6 UniProt (TrEMBL) Alternative ID(s) of Target Chain 6 BindingDB Target Chain Sequence 7 PDB ID(s) of Target Chain 7 UniProt (SwissProt) Recommended Name of Target Chain 7 UniProt (SwissProt) Entry Name of Target Chain 7 UniProt (SwissProt) Primary ID of Target Chain 7 UniProt (SwissProt) Secondary ID(s) of Target Chain 7 UniProt (SwissProt) Alternative ID(s) of Target Chain 7 UniProt (TrEMBL) Submitted Name of Target Chain 7 UniProt (TrEMBL) Entry Name of Target Chain 7 UniProt (TrEMBL) Primary ID of Target Chain 7 UniProt (TrEMBL) Secondary ID(s) of Target Chain 7 UniProt (TrEMBL) Alternative ID(s) of Target Chain 7 BindingDB Target Chain Sequence 8 PDB ID(s) of Target Chain 8 UniProt (SwissProt) Recommended Name of Target Chain 8 UniProt (SwissProt) Entry Name of Target Chain 8 UniProt (SwissProt) Primary ID of Target Chain 8 UniProt (SwissProt) Secondary ID(s) of Target Chain 8 UniProt (SwissProt) Alternative ID(s) of Target Chain 8 UniProt (TrEMBL) Submitted Name of Target Chain 8 UniProt (TrEMBL) Entry Name of Target Chain 8 UniProt (TrEMBL) Primary ID of Target Chain 8 UniProt (TrEMBL) Secondary ID(s) of Target Chain 8 UniProt (TrEMBL) Alternative ID(s) of Target Chain 8 BindingDB Target Chain Sequence 9 PDB ID(s) of Target Chain 9 UniProt (SwissProt) Recommended Name of Target Chain 9 UniProt (SwissProt) Entry Name of Target Chain 9 UniProt (SwissProt) Primary ID of Target Chain 9 UniProt (SwissProt) Secondary ID(s) of Target Chain 9 UniProt (SwissProt) Alternative ID(s) of Target Chain 9 UniProt (TrEMBL) Submitted Name of Target Chain 9 UniProt (TrEMBL) Entry Name of Target Chain 9 UniProt (TrEMBL) Primary ID of Target Chain 9 UniProt (TrEMBL) Secondary ID(s) of Target Chain 9 UniProt (TrEMBL) Alternative ID(s) of Target Chain 9 BindingDB Target Chain Sequence 10 PDB ID(s) of Target Chain 10 UniProt (SwissProt) Recommended Name of Target Chain 10 UniProt (SwissProt) Entry Name of Target Chain 10 UniProt (SwissProt) Primary ID of Target Chain 10 UniProt (SwissProt) Secondary ID(s) of Target Chain 10 UniProt (SwissProt) Alternative ID(s) of Target Chain 10 UniProt (TrEMBL) Submitted Name of Target Chain 10 UniProt (TrEMBL) Entry Name of Target Chain 10 UniProt (TrEMBL) Primary ID of Target Chain 10 UniProt (TrEMBL) Secondary ID(s) of Target Chain 10 UniProt (TrEMBL) Alternative ID(s) of Target Chain 10 BindingDB Target Chain Sequence 11 PDB ID(s) of Target Chain 11 UniProt (SwissProt) Recommended Name of Target Chain 11 UniProt (SwissProt) Entry Name of Target Chain 11 UniProt (SwissProt) Primary ID of Target Chain 11 UniProt (SwissProt) Secondary ID(s) of Target Chain 11 UniProt (SwissProt) Alternative ID(s) of Target Chain 11 UniProt (TrEMBL) Submitted Name of Target Chain 11 UniProt (TrEMBL) Entry Name of Target Chain 11 UniProt (TrEMBL) Primary ID of Target Chain 11 UniProt (TrEMBL) Secondary ID(s) of Target Chain 11 UniProt (TrEMBL) Alternative ID(s) of Target Chain 11 BindingDB Target Chain Sequence 12 PDB ID(s) of Target Chain 12 UniProt (SwissProt) Recommended Name of Target Chain 12 UniProt (SwissProt) Entry Name of Target Chain 12 UniProt (SwissProt) Primary ID of Target Chain 12 UniProt (SwissProt) Secondary ID(s) of Target Chain 12 UniProt (SwissProt) Alternative ID(s) of Target Chain 12 UniProt (TrEMBL) Submitted Name of Target Chain 12 UniProt (TrEMBL) Entry Name of Target Chain 12 UniProt (TrEMBL) Primary ID of Target Chain 12 UniProt (TrEMBL) Secondary ID(s) of Target Chain 12 UniProt (TrEMBL) Alternative ID(s) of Target Chain 12 BindingDB Target Chain Sequence 13 PDB ID(s) of Target Chain 13 UniProt (SwissProt) Recommended Name of Target Chain 13 UniProt (SwissProt) Entry Name of Target Chain 13 UniProt (SwissProt) Primary ID of Target Chain 13 UniProt (SwissProt) Secondary ID(s) of Target Chain 13 UniProt (SwissProt) Alternative ID(s) of Target Chain 13 UniProt (TrEMBL) Submitted Name of Target Chain 13 UniProt (TrEMBL) Entry Name of Target Chain 13 UniProt (TrEMBL) Primary ID of Target Chain 13 UniProt (TrEMBL) Secondary ID(s) of Target Chain 13 UniProt (TrEMBL) Alternative ID(s) of Target Chain 13 BindingDB Target Chain Sequence 14 PDB ID(s) of Target Chain 14 UniProt (SwissProt) Recommended Name of Target Chain 14 UniProt (SwissProt) Entry Name of Target Chain 14 UniProt (SwissProt) Primary ID of Target Chain 14 UniProt (SwissProt) Secondary ID(s) of Target Chain 14 UniProt (SwissProt) Alternative ID(s) of Target Chain 14 UniProt (TrEMBL) Submitted Name of Target Chain 14 UniProt (TrEMBL) Entry Name of Target Chain 14 UniProt (TrEMBL) Primary ID of Target Chain 14 UniProt (TrEMBL) Secondary ID(s) of Target Chain 14 UniProt (TrEMBL) Alternative ID(s) of Target Chain 14 BindingDB Target Chain Sequence 15 PDB ID(s) of Target Chain 15 UniProt (SwissProt) Recommended Name of Target Chain 15 UniProt (SwissProt) Entry Name of Target Chain 15 UniProt (SwissProt) Primary ID of Target Chain 15 UniProt (SwissProt) Secondary ID(s) of Target Chain 15 UniProt (SwissProt) Alternative ID(s) of Target Chain 15 UniProt (TrEMBL) Submitted Name of Target Chain 15 UniProt (TrEMBL) Entry Name of Target Chain 15 UniProt (TrEMBL) Primary ID of Target Chain 15 UniProt (TrEMBL) Secondary ID(s) of Target Chain 15 UniProt (TrEMBL) Alternative ID(s) of Target Chain 15 BindingDB Target Chain Sequence 16 PDB ID(s) of Target Chain 16 UniProt (SwissProt) Recommended Name of Target Chain 16 UniProt (SwissProt) Entry Name of Target Chain 16 UniProt (SwissProt) Primary ID of Target Chain 16 UniProt (SwissProt) Secondary ID(s) of Target Chain 16 UniProt (SwissProt) Alternative ID(s) of Target Chain 16 UniProt (TrEMBL) Submitted Name of Target Chain 16 UniProt (TrEMBL) Entry Name of Target Chain 16 UniProt (TrEMBL) Primary ID of Target Chain 16 UniProt (TrEMBL) Secondary ID(s) of Target Chain 16 UniProt (TrEMBL) Alternative ID(s) of Target Chain 16 BindingDB Target Chain Sequence 17 PDB ID(s) of Target Chain 17 UniProt (SwissProt) Recommended Name of Target Chain 17 UniProt (SwissProt) Entry Name of Target Chain 17 UniProt (SwissProt) Primary ID of Target Chain 17 UniProt (SwissProt) Secondary ID(s) of Target Chain 17 UniProt (SwissProt) Alternative ID(s) of Target Chain 17 UniProt (TrEMBL) Submitted Name of Target Chain 17 UniProt (TrEMBL) Entry Name of Target Chain 17 UniProt (TrEMBL) Primary ID of Target Chain 17 UniProt (TrEMBL) Secondary ID(s) of Target Chain 17 UniProt (TrEMBL) Alternative ID(s) of Target Chain 17 BindingDB Target Chain Sequence 18 PDB ID(s) of Target Chain 18 UniProt (SwissProt) Recommended Name of Target Chain 18 UniProt (SwissProt) Entry Name of Target Chain 18 UniProt (SwissProt) Primary ID of Target Chain 18 UniProt (SwissProt) Secondary ID(s) of Target Chain 18 UniProt (SwissProt) Alternative ID(s) of Target Chain 18 UniProt (TrEMBL) Submitted Name of Target Chain 18 UniProt (TrEMBL) Entry Name of Target Chain 18 UniProt (TrEMBL) Primary ID of Target Chain 18 UniProt (TrEMBL) Secondary ID(s) of Target Chain 18 UniProt (TrEMBL) Alternative ID(s) of Target Chain 18 BindingDB Target Chain Sequence 19 PDB ID(s) of Target Chain 19 UniProt (SwissProt) Recommended Name of Target Chain 19 UniProt (SwissProt) Entry Name of Target Chain 19 UniProt (SwissProt) Primary ID of Target Chain 19 UniProt (SwissProt) Secondary ID(s) of Target Chain 19 UniProt (SwissProt) Alternative ID(s) of Target Chain 19 UniProt (TrEMBL) Submitted Name of Target Chain 19 UniProt (TrEMBL) Entry Name of Target Chain 19 UniProt (TrEMBL) Primary ID of Target Chain 19 UniProt (TrEMBL) Secondary ID(s) of Target Chain 19 UniProt (TrEMBL) Alternative ID(s) of Target Chain 19 BindingDB Target Chain Sequence 20 PDB ID(s) of Target Chain 20 UniProt (SwissProt) Recommended Name of Target Chain 20 UniProt (SwissProt) Entry Name of Target Chain 20 UniProt (SwissProt) Primary ID of Target Chain 20 UniProt (SwissProt) Secondary ID(s) of Target Chain 20 UniProt (SwissProt) Alternative ID(s) of Target Chain 20 UniProt (TrEMBL) Submitted Name of Target Chain 20 UniProt (TrEMBL) Entry Name of Target Chain 20 UniProt (TrEMBL) Primary ID of Target Chain 20 UniProt (TrEMBL) Secondary ID(s) of Target Chain 20 UniProt (TrEMBL) Alternative ID(s) of Target Chain 20 BindingDB Target Chain Sequence 21 PDB ID(s) of Target Chain 21 UniProt (SwissProt) Recommended Name of Target Chain 21 UniProt (SwissProt) Entry Name of Target Chain 21 UniProt (SwissProt) Primary ID of Target Chain 21 UniProt (SwissProt) Secondary ID(s) of Target Chain 21 UniProt (SwissProt) Alternative ID(s) of Target Chain 21 UniProt (TrEMBL) Submitted Name of Target Chain 21 UniProt (TrEMBL) Entry Name of Target Chain 21 UniProt (TrEMBL) Primary ID of Target Chain 21 UniProt (TrEMBL) Secondary ID(s) of Target Chain 21 UniProt (TrEMBL) Alternative ID(s) of Target Chain 21 BindingDB Target Chain Sequence 22 PDB ID(s) of Target Chain 22 UniProt (SwissProt) Recommended Name of Target Chain 22 UniProt (SwissProt) Entry Name of Target Chain 22 UniProt (SwissProt) Primary ID of Target Chain 22 UniProt (SwissProt) Secondary ID(s) of Target Chain 22 UniProt (SwissProt) Alternative ID(s) of Target Chain 22 UniProt (TrEMBL) Submitted Name of Target Chain 22 UniProt (TrEMBL) Entry Name of Target Chain 22 UniProt (TrEMBL) Primary ID of Target Chain 22 UniProt (TrEMBL) Secondary ID(s) of Target Chain 22 UniProt (TrEMBL) Alternative ID(s) of Target Chain 22 BindingDB Target Chain Sequence 23 PDB ID(s) of Target Chain 23 UniProt (SwissProt) Recommended Name of Target Chain 23 UniProt (SwissProt) Entry Name of Target Chain 23 UniProt (SwissProt) Primary ID of Target Chain 23 UniProt (SwissProt) Secondary ID(s) of Target Chain 23 UniProt (SwissProt) Alternative ID(s) of Target Chain 23 UniProt (TrEMBL) Submitted Name of Target Chain 23 UniProt (TrEMBL) Entry Name of Target Chain 23 UniProt (TrEMBL) Primary ID of Target Chain 23 UniProt (TrEMBL) Secondary ID(s) of Target Chain 23 UniProt (TrEMBL) Alternative ID(s) of Target Chain 23 BindingDB Target Chain Sequence 24 PDB ID(s) of Target Chain 24 UniProt (SwissProt) Recommended Name of Target Chain 24 UniProt (SwissProt) Entry Name of Target Chain 24 UniProt (SwissProt) Primary ID of Target Chain 24 UniProt (SwissProt) Secondary ID(s) of Target Chain 24 UniProt (SwissProt) Alternative ID(s) of Target Chain 24 UniProt (TrEMBL) Submitted Name of Target Chain 24 UniProt (TrEMBL) Entry Name of Target Chain 24 UniProt (TrEMBL) Primary ID of Target Chain 24 UniProt (TrEMBL) Secondary ID(s) of Target Chain 24 UniProt (TrEMBL) Alternative ID(s) of Target Chain 24 BindingDB Target Chain Sequence 25 PDB ID(s) of Target Chain 25 UniProt (SwissProt) Recommended Name of Target Chain 25 UniProt (SwissProt) Entry Name of Target Chain 25 UniProt (SwissProt) Primary ID of Target Chain 25 UniProt (SwissProt) Secondary ID(s) of Target Chain 25 UniProt (SwissProt) Alternative ID(s) of Target Chain 25 UniProt (TrEMBL) Submitted Name of Target Chain 25 UniProt (TrEMBL) Entry Name of Target Chain 25 UniProt (TrEMBL) Primary ID of Target Chain 25 UniProt (TrEMBL) Secondary ID(s) of Target Chain 25 UniProt (TrEMBL) Alternative ID(s) of Target Chain 25 BindingDB Target Chain Sequence 26 PDB ID(s) of Target Chain 26 UniProt (SwissProt) Recommended Name of Target Chain 26 UniProt (SwissProt) Entry Name of Target Chain 26 UniProt (SwissProt) Primary ID of Target Chain 26 UniProt (SwissProt) Secondary ID(s) of Target Chain 26 UniProt (SwissProt) Alternative ID(s) of Target Chain 26 UniProt (TrEMBL) Submitted Name of Target Chain 26 UniProt (TrEMBL) Entry Name of Target Chain 26 UniProt (TrEMBL) Primary ID of Target Chain 26 UniProt (TrEMBL) Secondary ID(s) of Target Chain 26 UniProt (TrEMBL) Alternative ID(s) of Target Chain 26 BindingDB Target Chain Sequence 27 PDB ID(s) of Target Chain 27 UniProt (SwissProt) Recommended Name of Target Chain 27 UniProt (SwissProt) Entry Name of Target Chain 27 UniProt (SwissProt) Primary ID of Target Chain 27 UniProt (SwissProt) Secondary ID(s) of Target Chain 27 UniProt (SwissProt) Alternative ID(s) of Target Chain 27 UniProt (TrEMBL) Submitted Name of Target Chain 27 UniProt (TrEMBL) Entry Name of Target Chain 27 UniProt (TrEMBL) Primary ID of Target Chain 27 UniProt (TrEMBL) Secondary ID(s) of Target Chain 27 UniProt (TrEMBL) Alternative ID(s) of Target Chain 27 BindingDB Target Chain Sequence 28 PDB ID(s) of Target Chain 28 UniProt (SwissProt) Recommended Name of Target Chain 28 UniProt (SwissProt) Entry Name of Target Chain 28 UniProt (SwissProt) Primary ID of Target Chain 28 UniProt (SwissProt) Secondary ID(s) of Target Chain 28 UniProt (SwissProt) Alternative ID(s) of Target Chain 28 UniProt (TrEMBL) Submitted Name of Target Chain 28 UniProt (TrEMBL) Entry Name of Target Chain 28 UniProt (TrEMBL) Primary ID of Target Chain 28 UniProt (TrEMBL) Secondary ID(s) of Target Chain 28 UniProt (TrEMBL) Alternative ID(s) of Target Chain 28 BindingDB Target Chain Sequence 29 PDB ID(s) of Target Chain 29 UniProt (SwissProt) Recommended Name of Target Chain 29 UniProt (SwissProt) Entry Name of Target Chain 29 UniProt (SwissProt) Primary ID of Target Chain 29 UniProt (SwissProt) Secondary ID(s) of Target Chain 29 UniProt (SwissProt) Alternative ID(s) of Target Chain 29 UniProt (TrEMBL) Submitted Name of Target Chain 29 UniProt (TrEMBL) Entry Name of Target Chain 29 UniProt (TrEMBL) Primary ID of Target Chain 29 UniProt (TrEMBL) Secondary ID(s) of Target Chain 29 UniProt (TrEMBL) Alternative ID(s) of Target Chain 29 BindingDB Target Chain Sequence 30 PDB ID(s) of Target Chain 30 UniProt (SwissProt) Recommended Name of Target Chain 30 UniProt (SwissProt) Entry Name of Target Chain 30 UniProt (SwissProt) Primary ID of Target Chain 30 UniProt (SwissProt) Secondary ID(s) of Target Chain 30 UniProt (SwissProt) Alternative ID(s) of Target Chain 30 UniProt (TrEMBL) Submitted Name of Target Chain 30 UniProt (TrEMBL) Entry Name of Target Chain 30 UniProt (TrEMBL) Primary ID of Target Chain 30 UniProt (TrEMBL) Secondary ID(s) of Target Chain 30 UniProt (TrEMBL) Alternative ID(s) of Target Chain 30 BindingDB Target Chain Sequence 31 PDB ID(s) of Target Chain 31 UniProt (SwissProt) Recommended Name of Target Chain 31 UniProt (SwissProt) Entry Name of Target Chain 31 UniProt (SwissProt) Primary ID of Target Chain 31 UniProt (SwissProt) Secondary ID(s) of Target Chain 31 UniProt (SwissProt) Alternative ID(s) of Target Chain 31 UniProt (TrEMBL) Submitted Name of Target Chain 31 UniProt (TrEMBL) Entry Name of Target Chain 31 UniProt (TrEMBL) Primary ID of Target Chain 31 UniProt (TrEMBL) Secondary ID(s) of Target Chain 31 UniProt (TrEMBL) Alternative ID(s) of Target Chain 31 BindingDB Target Chain Sequence 32 PDB ID(s) of Target Chain 32 UniProt (SwissProt) Recommended Name of Target Chain 32 UniProt (SwissProt) Entry Name of Target Chain 32 UniProt (SwissProt) Primary ID of Target Chain 32 UniProt (SwissProt) Secondary ID(s) of Target Chain 32 UniProt (SwissProt) Alternative ID(s) of Target Chain 32 UniProt (TrEMBL) Submitted Name of Target Chain 32 UniProt (TrEMBL) Entry Name of Target Chain 32 UniProt (TrEMBL) Primary ID of Target Chain 32 UniProt (TrEMBL) Secondary ID(s) of Target Chain 32 UniProt (TrEMBL) Alternative ID(s) of Target Chain 32 BindingDB Target Chain Sequence 33 PDB ID(s) of Target Chain 33 UniProt (SwissProt) Recommended Name of Target Chain 33 UniProt (SwissProt) Entry Name of Target Chain 33 UniProt (SwissProt) Primary ID of Target Chain 33 UniProt (SwissProt) Secondary ID(s) of Target Chain 33 UniProt (SwissProt) Alternative ID(s) of Target Chain 33 UniProt (TrEMBL) Submitted Name of Target Chain 33 UniProt (TrEMBL) Entry Name of Target Chain 33 UniProt (TrEMBL) Primary ID of Target Chain 33 UniProt (TrEMBL) Secondary ID(s) of Target Chain 33 UniProt (TrEMBL) Alternative ID(s) of Target Chain 33 BindingDB Target Chain Sequence 34 PDB ID(s) of Target Chain 34 UniProt (SwissProt) Recommended Name of Target Chain 34 UniProt (SwissProt) Entry Name of Target Chain 34 UniProt (SwissProt) Primary ID of Target Chain 34 UniProt (SwissProt) Secondary ID(s) of Target Chain 34 UniProt (SwissProt) Alternative ID(s) of Target Chain 34 UniProt (TrEMBL) Submitted Name of Target Chain 34 UniProt (TrEMBL) Entry Name of Target Chain 34 UniProt (TrEMBL) Primary ID of Target Chain 34 UniProt (TrEMBL) Secondary ID(s) of Target Chain 34 UniProt (TrEMBL) Alternative ID(s) of Target Chain 34 BindingDB Target Chain Sequence 35 PDB ID(s) of Target Chain 35 UniProt (SwissProt) Recommended Name of Target Chain 35 UniProt (SwissProt) Entry Name of Target Chain 35 UniProt (SwissProt) Primary ID of Target Chain 35 UniProt (SwissProt) Secondary ID(s) of Target Chain 35 UniProt (SwissProt) Alternative ID(s) of Target Chain 35 UniProt (TrEMBL) Submitted Name of Target Chain 35 UniProt (TrEMBL) Entry Name of Target Chain 35 UniProt (TrEMBL) Primary ID of Target Chain 35 UniProt (TrEMBL) Secondary ID(s) of Target Chain 35 UniProt (TrEMBL) Alternative ID(s) of Target Chain 35 BindingDB Target Chain Sequence 36 PDB ID(s) of Target Chain 36 UniProt (SwissProt) Recommended Name of Target Chain 36 UniProt (SwissProt) Entry Name of Target Chain 36 UniProt (SwissProt) Primary ID of Target Chain 36 UniProt (SwissProt) Secondary ID(s) of Target Chain 36 UniProt (SwissProt) Alternative ID(s) of Target Chain 36 UniProt (TrEMBL) Submitted Name of Target Chain 36 UniProt (TrEMBL) Entry Name of Target Chain 36 UniProt (TrEMBL) Primary ID of Target Chain 36 UniProt (TrEMBL) Secondary ID(s) of Target Chain 36 UniProt (TrEMBL) Alternative ID(s) of Target Chain 36 BindingDB Target Chain Sequence 37 PDB ID(s) of Target Chain 37 UniProt (SwissProt) Recommended Name of Target Chain 37 UniProt (SwissProt) Entry Name of Target Chain 37 UniProt (SwissProt) Primary ID of Target Chain 37 UniProt (SwissProt) Secondary ID(s) of Target Chain 37 UniProt (SwissProt) Alternative ID(s) of Target Chain 37 UniProt (TrEMBL) Submitted Name of Target Chain 37 UniProt (TrEMBL) Entry Name of Target Chain 37 UniProt (TrEMBL) Primary ID of Target Chain 37 UniProt (TrEMBL) Secondary ID(s) of Target Chain 37 UniProt (TrEMBL) Alternative ID(s) of Target Chain 37 BindingDB Target Chain Sequence 38 PDB ID(s) of Target Chain 38 UniProt (SwissProt) Recommended Name of Target Chain 38 UniProt (SwissProt) Entry Name of Target Chain 38 UniProt (SwissProt) Primary ID of Target Chain 38 UniProt (SwissProt) Secondary ID(s) of Target Chain 38 UniProt (SwissProt) Alternative ID(s) of Target Chain 38 UniProt (TrEMBL) Submitted Name of Target Chain 38 UniProt (TrEMBL) Entry Name of Target Chain 38 UniProt (TrEMBL) Primary ID of Target Chain 38 UniProt (TrEMBL) Secondary ID(s) of Target Chain 38 UniProt (TrEMBL) Alternative ID(s) of Target Chain 38 BindingDB Target Chain Sequence 39 PDB ID(s) of Target Chain 39 UniProt (SwissProt) Recommended Name of Target Chain 39 UniProt (SwissProt) Entry Name of Target Chain 39 UniProt (SwissProt) Primary ID of Target Chain 39 UniProt (SwissProt) Secondary ID(s) of Target Chain 39 UniProt (SwissProt) Alternative ID(s) of Target Chain 39 UniProt (TrEMBL) Submitted Name of Target Chain 39 UniProt (TrEMBL) Entry Name of Target Chain 39 UniProt (TrEMBL) Primary ID of Target Chain 39 UniProt (TrEMBL) Secondary ID(s) of Target Chain 39 UniProt (TrEMBL) Alternative ID(s) of Target Chain 39 BindingDB Target Chain Sequence 40 PDB ID(s) of Target Chain 40 UniProt (SwissProt) Recommended Name of Target Chain 40 UniProt (SwissProt) Entry Name of Target Chain 40 UniProt (SwissProt) Primary ID of Target Chain 40 UniProt (SwissProt) Secondary ID(s) of Target Chain 40 UniProt (SwissProt) Alternative ID(s) of Target Chain 40 UniProt (TrEMBL) Submitted Name of Target Chain 40 UniProt (TrEMBL) Entry Name of Target Chain 40 UniProt (TrEMBL) Primary ID of Target Chain 40 UniProt (TrEMBL) Secondary ID(s) of Target Chain 40 UniProt (TrEMBL) Alternative ID(s) of Target Chain 40 BindingDB Target Chain Sequence 41 PDB ID(s) of Target Chain 41 UniProt (SwissProt) Recommended Name of Target Chain 41 UniProt (SwissProt) Entry Name of Target Chain 41 UniProt (SwissProt) Primary ID of Target Chain 41 UniProt (SwissProt) Secondary ID(s) of Target Chain 41 UniProt (SwissProt) Alternative ID(s) of Target Chain 41 UniProt (TrEMBL) Submitted Name of Target Chain 41 UniProt (TrEMBL) Entry Name of Target Chain 41 UniProt (TrEMBL) Primary ID of Target Chain 41 UniProt (TrEMBL) Secondary ID(s) of Target Chain 41 UniProt (TrEMBL) Alternative ID(s) of Target Chain 41 BindingDB Target Chain Sequence 42 PDB ID(s) of Target Chain 42 UniProt (SwissProt) Recommended Name of Target Chain 42 UniProt (SwissProt) Entry Name of Target Chain 42 UniProt (SwissProt) Primary ID of Target Chain 42 UniProt (SwissProt) Secondary ID(s) of Target Chain 42 UniProt (SwissProt) Alternative ID(s) of Target Chain 42 UniProt (TrEMBL) Submitted Name of Target Chain 42 UniProt (TrEMBL) Entry Name of Target Chain 42 UniProt (TrEMBL) Primary ID of Target Chain 42 UniProt (TrEMBL) Secondary ID(s) of Target Chain 42 UniProt (TrEMBL) Alternative ID(s) of Target Chain 42 BindingDB Target Chain Sequence 43 PDB ID(s) of Target Chain 43 UniProt (SwissProt) Recommended Name of Target Chain 43 UniProt (SwissProt) Entry Name of Target Chain 43 UniProt (SwissProt) Primary ID of Target Chain 43 UniProt (SwissProt) Secondary ID(s) of Target Chain 43 UniProt (SwissProt) Alternative ID(s) of Target Chain 43 UniProt (TrEMBL) Submitted Name of Target Chain 43 UniProt (TrEMBL) Entry Name of Target Chain 43 UniProt (TrEMBL) Primary ID of Target Chain 43 UniProt (TrEMBL) Secondary ID(s) of Target Chain 43 UniProt (TrEMBL) Alternative ID(s) of Target Chain 43 BindingDB Target Chain Sequence 44 PDB ID(s) of Target Chain 44 UniProt (SwissProt) Recommended Name of Target Chain 44 UniProt (SwissProt) Entry Name of Target Chain 44 UniProt (SwissProt) Primary ID of Target Chain 44 UniProt (SwissProt) Secondary ID(s) of Target Chain 44 UniProt (SwissProt) Alternative ID(s) of Target Chain 44 UniProt (TrEMBL) Submitted Name of Target Chain 44 UniProt (TrEMBL) Entry Name of Target Chain 44 UniProt (TrEMBL) Primary ID of Target Chain 44 UniProt (TrEMBL) Secondary ID(s) of Target Chain 44 UniProt (TrEMBL) Alternative ID(s) of Target Chain 44 BindingDB Target Chain Sequence 45 PDB ID(s) of Target Chain 45 UniProt (SwissProt) Recommended Name of Target Chain 45 UniProt (SwissProt) Entry Name of Target Chain 45 UniProt (SwissProt) Primary ID of Target Chain 45 UniProt (SwissProt) Secondary ID(s) of Target Chain 45 UniProt (SwissProt) Alternative ID(s) of Target Chain 45 UniProt (TrEMBL) Submitted Name of Target Chain 45 UniProt (TrEMBL) Entry Name of Target Chain 45 UniProt (TrEMBL) Primary ID of Target Chain 45 UniProt (TrEMBL) Secondary ID(s) of Target Chain 45 UniProt (TrEMBL) Alternative ID(s) of Target Chain 45 BindingDB Target Chain Sequence 46 PDB ID(s) of Target Chain 46 UniProt (SwissProt) Recommended Name of Target Chain 46 UniProt (SwissProt) Entry Name of Target Chain 46 UniProt (SwissProt) Primary ID of Target Chain 46 UniProt (SwissProt) Secondary ID(s) of Target Chain 46 UniProt (SwissProt) Alternative ID(s) of Target Chain 46 UniProt (TrEMBL) Submitted Name of Target Chain 46 UniProt (TrEMBL) Entry Name of Target Chain 46 UniProt (TrEMBL) Primary ID of Target Chain 46 UniProt (TrEMBL) Secondary ID(s) of Target Chain 46 UniProt (TrEMBL) Alternative ID(s) of Target Chain 46 BindingDB Target Chain Sequence 47 PDB ID(s) of Target Chain 47 UniProt (SwissProt) Recommended Name of Target Chain 47 UniProt (SwissProt) Entry Name of Target Chain 47 UniProt (SwissProt) Primary ID of Target Chain 47 UniProt (SwissProt) Secondary ID(s) of Target Chain 47 UniProt (SwissProt) Alternative ID(s) of Target Chain 47 UniProt (TrEMBL) Submitted Name of Target Chain 47 UniProt (TrEMBL) Entry Name of Target Chain 47 UniProt (TrEMBL) Primary ID of Target Chain 47 UniProt (TrEMBL) Secondary ID(s) of Target Chain 47 UniProt (TrEMBL) Alternative ID(s) of Target Chain 47 BindingDB Target Chain Sequence 48 PDB ID(s) of Target Chain 48 UniProt (SwissProt) Recommended Name of Target Chain 48 UniProt (SwissProt) Entry Name of Target Chain 48 UniProt (SwissProt) Primary ID of Target Chain 48 UniProt (SwissProt) Secondary ID(s) of Target Chain 48 UniProt (SwissProt) Alternative ID(s) of Target Chain 48 UniProt (TrEMBL) Submitted Name of Target Chain 48 UniProt (TrEMBL) Entry Name of Target Chain 48 UniProt (TrEMBL) Primary ID of Target Chain 48 UniProt (TrEMBL) Secondary ID(s) of Target Chain 48 UniProt (TrEMBL) Alternative ID(s) of Target Chain 48 BindingDB Target Chain Sequence 49 PDB ID(s) of Target Chain 49 UniProt (SwissProt) Recommended Name of Target Chain 49 UniProt (SwissProt) Entry Name of Target Chain 49 UniProt (SwissProt) Primary ID of Target Chain 49 UniProt (SwissProt) Secondary ID(s) of Target Chain 49 UniProt (SwissProt) Alternative ID(s) of Target Chain 49 UniProt (TrEMBL) Submitted Name of Target Chain 49 UniProt (TrEMBL) Entry Name of Target Chain 49 UniProt (TrEMBL) Primary ID of Target Chain 49 UniProt (TrEMBL) Secondary ID(s) of Target Chain 49 UniProt (TrEMBL) Alternative ID(s) of Target Chain 49 BindingDB Target Chain Sequence 50 PDB ID(s) of Target Chain 50 UniProt (SwissProt) Recommended Name of Target Chain 50 UniProt (SwissProt) Entry Name of Target Chain 50 UniProt (SwissProt) Primary ID of Target Chain 50 UniProt (SwissProt) Secondary ID(s) of Target Chain 50 UniProt (SwissProt) Alternative ID(s) of Target Chain 50 UniProt (TrEMBL) Submitted Name of Target Chain 50 UniProt (TrEMBL) Entry Name of Target Chain 50 UniProt (TrEMBL) Primary ID of Target Chain 50 UniProt (TrEMBL) Secondary ID(s) of Target Chain 50 UniProt (TrEMBL) Alternative ID(s) of Target Chain 50 51602823 CC(=O)N(CCCP(=O)(O)O)O InChI=1S/C5H12NO5P/c1-5(7)6(8)3-2-4-12(9,10)11/h8H,2-4H2,1H3,(H2,9,10,11) PKMNDDZSIHLLLI-UHFFFAOYSA-N 50181153 FR-900098::3-(N-hydroxyformamido)propylphosphonic acid::3-(N-hydroxyacetamido)propylphosphonic acid::ammonium 3-(N-hydroxyacetamido)propylphosphonate::CHEMBL205338 1-deoxy-D-xylulose 5-phosphate reductoisomerase, apicoplastic Plasmodium falciparum (isolate 3D7) 22 ChEMBL 10.7270/Q2K93D77 39026652 Bague, D; Wang, R; Hodge, D; Mikati, MO; Roma, JS; Boshoff, HI; Dailey, AL; Girma, M; Couch, RD; Odom John, AR; Dowd, CS //0 10/12/2025 George Washington University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50181153 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50007803&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase%2C+apicoplastic&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50181153&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase%2C+apicoplastic&column=ki&startPg=0&Increment=50&submit=Search F98 3AUA,4A03,7S04 162204 104065995 CHEMBL205338 C17942 1 MKKYIYIYFFFITITINDLVINNTSKCVSIERRKNNAYINYGIGYNGPDNKITKSRRCKRIKLCKKDLIDIGAIKKPINVAIFGSTGSIGTNALNIIRECNKIENVFNVKALYVNKSVNELYEQAREFLPEYLCIHDKSVYEELKELVKNIKDYKPIILCGDEGMKEICSSNSIDKIVIGIDSFQGLYSTMYAIMNNKIVALANKESIVSAGFFLKKLLNIHKNAKIIPVDSEHSAIFQCLDNNKVLKTKCLQDNFSKINNINKIFLCSSGGPFQNLTMDELKNVTSENALKHPKWKMGKKITIDSATMMNKGLEVIETHFLFDVDYNDIEVIVHKECIIHSCVEFIDKSVISQMYYPDMQIPILYSLTWPDRIKTNLKPLDLAQVSTLTFHKPSLEHFPCIKLAYQAGIKGNFYPTVLNASNEIANNLFLNNKIKYFDISSIISQVLESFNSQKVSENSEDLMKQILQIHSWAKDKATDIYNKHNSS 9V5Z,9V5Y,9V5X,9V5W,9V5V,9V5U,9KP9,9JZE,9JZD,9JZC,9JZB,9JZA,9JZ9,9JZ8,9JZ7,9JOB,9JOA,3WQS,3WQR,3WQQ,3AUA,3AU9,3AU8,8ZXX,5JO0,5JNL,5JMW,5JMP,5JC1,5JBI,5JAZ,4Y6S,4Y6R,4Y6P,4Y67 1-deoxy-D-xylulose 5-phosphate reductoisomerase, apicoplastic DXR_PLAF7 Q8IKG4 A0A144A2T4 51602822 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase, apicoplastic Plasmodium falciparum (isolate 3D7) 63 ChEMBL 10.7270/Q2K93D77 39026652 Bague, D; Wang, R; Hodge, D; Mikati, MO; Roma, JS; Boshoff, HI; Dailey, AL; Girma, M; Couch, RD; Odom John, AR; Dowd, CS //0 10/12/2025 George Washington University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50007803&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase%2C+apicoplastic&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase%2C+apicoplastic&column=ki&startPg=0&Increment=50&submit=Search FOM 1ONP,1Q0H,1Q0L,2EGH,2JCV,2JCX,3A06,3AU9,3UPY,4AIC,4OOE,4OOF,4ZQF,4ZQG,4ZQH,6MH5,8S65 572 104041488 CHEMBL203125 DB02948 1 MKKYIYIYFFFITITINDLVINNTSKCVSIERRKNNAYINYGIGYNGPDNKITKSRRCKRIKLCKKDLIDIGAIKKPINVAIFGSTGSIGTNALNIIRECNKIENVFNVKALYVNKSVNELYEQAREFLPEYLCIHDKSVYEELKELVKNIKDYKPIILCGDEGMKEICSSNSIDKIVIGIDSFQGLYSTMYAIMNNKIVALANKESIVSAGFFLKKLLNIHKNAKIIPVDSEHSAIFQCLDNNKVLKTKCLQDNFSKINNINKIFLCSSGGPFQNLTMDELKNVTSENALKHPKWKMGKKITIDSATMMNKGLEVIETHFLFDVDYNDIEVIVHKECIIHSCVEFIDKSVISQMYYPDMQIPILYSLTWPDRIKTNLKPLDLAQVSTLTFHKPSLEHFPCIKLAYQAGIKGNFYPTVLNASNEIANNLFLNNKIKYFDISSIISQVLESFNSQKVSENSEDLMKQILQIHSWAKDKATDIYNKHNSS 9V5Z,9V5Y,9V5X,9V5W,9V5V,9V5U,9KP9,9JZE,9JZD,9JZC,9JZB,9JZA,9JZ9,9JZ8,9JZ7,9JOB,9JOA,3WQS,3WQR,3WQQ,3AUA,3AU9,3AU8,8ZXX,5JO0,5JNL,5JMW,5JMP,5JC1,5JBI,5JAZ,4Y6S,4Y6R,4Y6P,4Y67 1-deoxy-D-xylulose 5-phosphate reductoisomerase, apicoplastic DXR_PLAF7 Q8IKG4 A0A144A2T4 50920605 c1ccc2c(c1)ccc(n2)CP(=O)(O)O InChI=1S/C10H10NO3P/c12-15(13,14)7-9-6-5-8-3-1-2-4-10(8)11-9/h1-6H,7H2,(H2,12,13,14) SZCYKKWPKXABPU-UHFFFAOYSA-N 50335494 (quinolin-2-ylmethyl)phosphonic acid::Quinolin-2-ylmethylphosphonic acid::CHEMBL1615247 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 15900 ChEMBL 10.1021/ml100243r 10.7270/Q2XD12NV 21379374 Deng, L; Endo, K; Kato, M; Cheng, G; Yajima, S; Song, Y 3/7/2011 1/4/2013 Baylor College of Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50335494 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50335494&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search SYE 3ANN 50897582 125085596 CHEMBL1615247 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 50920603 c1ccnc(c1)CP(=O)(O)O InChI=1S/C6H8NO3P/c8-11(9,10)5-6-3-1-2-4-7-6/h1-4H,5H2,(H2,8,9,10) WVWCWWLEFNGDBC-UHFFFAOYSA-N 50335492 (pyridin-2-ylmethyl)phosphonic acid::Pyridin-2-ylmethylphosphonic acid::CHEMBL1615245 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 4600 ChEMBL 10.1021/ml100243r 10.7270/Q2XD12NV 21379374 Deng, L; Endo, K; Kato, M; Cheng, G; Yajima, S; Song, Y 3/7/2011 1/4/2013 Baylor College of Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50335492 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50335492&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search SYC 3ANL 12730177 125085594 CHEMBL1615245 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 293063 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 42 7.5000 Curated from the literature by BindingDB 10.1016/j.bioorg.2015.02.008 10.7270/Q2XS5T4J 25800132 aid1801044 Tritsch, D; Zinglé, C; Rohmer, M; Grosdemange-Billiard, C 4/28/2015 9/3/2015 University of Strasburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 8S65,2JCV,3AU9,2JCX,4AIC,3UPY,4ZQG,4ZQF,2EGH,1ONP,1Q0L,1Q0H,6MH5,3A06,4OOF,4OOE,4ZQH 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 50235830 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 32 ChEMBL 10.1021/jm5010978 10.7270/Q29K4CVJ 25210872 Masini, T; Hirsch, AK 12/16/2014 3/7/2016 University of Groningen http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 1ONP,1Q0H,1Q0L,2EGH,2JCV,2JCX,3A06,3AU9,3UPY,4AIC,4OOE,4OOF,4ZQF,4ZQG,4ZQH,6MH5,8S65 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 50268029 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 32 ChEMBL 10.1016/j.bmc.2014.05.004 10.7270/Q2057HKT 24890653 Zinglé, C; Tritsch, D; Grosdemange-Billiard, C; Rohmer, M 6/16/2014 3/22/2016 University of Strasburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 1ONP,1Q0H,1Q0L,2EGH,2JCV,2JCX,3A06,3AU9,3UPY,4AIC,4OOE,4OOF,4ZQF,4ZQG,4ZQH,6MH5,8S65 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 50330018 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 438 ChEMBL 10.1021/jm5014264 10.7270/Q2639RG9 25781377 Chofor, R; Sooriyaarachchi, S; Risseeuw, MD; Bergfors, T; Pouyez, J; Johny, C; Haymond, A; Everaert, A; Dowd, CS; Maes, L; Coenye, T; Alex, A; Couch, RD; Jones, TA; Wouters, J; Mowbray, SL; Van Calenbergh, S 4/9/2015 5/1/2016 Universiteit Gent http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 1ONP,1Q0H,1Q0L,2EGH,2JCV,2JCX,3A06,3AU9,3UPY,4AIC,4OOE,4OOF,4ZQF,4ZQG,4ZQH,6MH5,8S65 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 50335508 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 30 ChEMBL 10.1016/j.bmcl.2005.12.082 10.7270/Q2FJ2GB6 16439126 Haemers, T; Wiesner, J; Van Poecke, S; Goeman, J; Henschker, D; Beck, E; Jomaa, H; Van Calenbergh, S 2/27/2006 11/10/2009 Ghent University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 1ONP,1Q0H,1Q0L,2EGH,2JCV,2JCX,3A06,3AU9,3UPY,4AIC,4OOE,4OOF,4ZQF,4ZQG,4ZQH,6MH5,8S65 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 50343405 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 48 ChEMBL 10.1021/jm051177c 10.7270/Q22F7N24 16610809 Devreux, V; Wiesner, J; Goeman, JL; Van der Eycken, J; Jomaa, H; Van Calenbergh, S 4/13/2006 11/10/2009 Ghent University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 1ONP,1Q0H,1Q0L,2EGH,2JCV,2JCX,3A06,3AU9,3UPY,4AIC,4OOE,4OOF,4ZQF,4ZQG,4ZQH,6MH5,8S65 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 50920587 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 30 ChEMBL 10.1021/ml100243r 10.7270/Q2XD12NV 21379374 Deng, L; Endo, K; Kato, M; Cheng, G; Yajima, S; Song, Y 3/7/2011 1/4/2013 Baylor College of Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 1ONP,1Q0H,1Q0L,2EGH,2JCV,2JCX,3A06,3AU9,3UPY,4AIC,4OOE,4OOF,4ZQF,4ZQG,4ZQH,6MH5,8S65 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 51033790 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 20 ChEMBL 10.1021/jm0491501 10.7270/Q2VH5Q21 15887963 Silber, K; Heidler, P; Kurz, T; Klebe, G 5/12/2005 5/20/2013 Philipps University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 1ONP,1Q0H,1Q0L,2EGH,2JCV,2JCX,3A06,3AU9,3UPY,4AIC,4OOE,4OOF,4ZQF,4ZQG,4ZQH,6MH5,8S65 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 51162163 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 1853000 ChEMBL 10.1021/jm060492b 10.7270/Q24J0HW7 17149863 Leon, A; Liu, L; Yang, Y; Hudock, MP; Hall, P; Yin, F; Studer, D; Puan, KJ; Morita, CT; Oldfield, E 12/14/2006 8/23/2020 University of Illinois At Urbana - Champaign http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 1ONP,1Q0H,1Q0L,2EGH,2JCV,2JCX,3A06,3AU9,3UPY,4AIC,4OOE,4OOF,4ZQF,4ZQG,4ZQH,6MH5,8S65 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 293063 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 42 7.5000 Curated from the literature by BindingDB 10.1016/j.bioorg.2015.02.008 10.7270/Q2XS5T4J 25800132 aid1801044 Tritsch, D; Zinglé, C; Rohmer, M; Grosdemange-Billiard, C 4/28/2015 9/3/2015 University of Strasburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 8S65,2JCV,3AU9,2JCX,4AIC,3UPY,4ZQG,4ZQF,2EGH,1ONP,1Q0L,1Q0H,6MH5,3A06,4OOF,4OOE,4ZQH 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 50235830 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 32 ChEMBL 10.1021/jm5010978 10.7270/Q29K4CVJ 25210872 Masini, T; Hirsch, AK 12/16/2014 3/7/2016 University of Groningen http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 1ONP,1Q0H,1Q0L,2EGH,2JCV,2JCX,3A06,3AU9,3UPY,4AIC,4OOE,4OOF,4ZQF,4ZQG,4ZQH,6MH5,8S65 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 50268029 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 32 ChEMBL 10.1016/j.bmc.2014.05.004 10.7270/Q2057HKT 24890653 Zinglé, C; Tritsch, D; Grosdemange-Billiard, C; Rohmer, M 6/16/2014 3/22/2016 University of Strasburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 1ONP,1Q0H,1Q0L,2EGH,2JCV,2JCX,3A06,3AU9,3UPY,4AIC,4OOE,4OOF,4ZQF,4ZQG,4ZQH,6MH5,8S65 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 50330018 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 438 ChEMBL 10.1021/jm5014264 10.7270/Q2639RG9 25781377 Chofor, R; Sooriyaarachchi, S; Risseeuw, MD; Bergfors, T; Pouyez, J; Johny, C; Haymond, A; Everaert, A; Dowd, CS; Maes, L; Coenye, T; Alex, A; Couch, RD; Jones, TA; Wouters, J; Mowbray, SL; Van Calenbergh, S 4/9/2015 5/1/2016 Universiteit Gent http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 1ONP,1Q0H,1Q0L,2EGH,2JCV,2JCX,3A06,3AU9,3UPY,4AIC,4OOE,4OOF,4ZQF,4ZQG,4ZQH,6MH5,8S65 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 50335508 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 30 ChEMBL 10.1016/j.bmcl.2005.12.082 10.7270/Q2FJ2GB6 16439126 Haemers, T; Wiesner, J; Van Poecke, S; Goeman, J; Henschker, D; Beck, E; Jomaa, H; Van Calenbergh, S 2/27/2006 11/10/2009 Ghent University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 1ONP,1Q0H,1Q0L,2EGH,2JCV,2JCX,3A06,3AU9,3UPY,4AIC,4OOE,4OOF,4ZQF,4ZQG,4ZQH,6MH5,8S65 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 50343405 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 48 ChEMBL 10.1021/jm051177c 10.7270/Q22F7N24 16610809 Devreux, V; Wiesner, J; Goeman, JL; Van der Eycken, J; Jomaa, H; Van Calenbergh, S 4/13/2006 11/10/2009 Ghent University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 1ONP,1Q0H,1Q0L,2EGH,2JCV,2JCX,3A06,3AU9,3UPY,4AIC,4OOE,4OOF,4ZQF,4ZQG,4ZQH,6MH5,8S65 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 50920587 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 30 ChEMBL 10.1021/ml100243r 10.7270/Q2XD12NV 21379374 Deng, L; Endo, K; Kato, M; Cheng, G; Yajima, S; Song, Y 3/7/2011 1/4/2013 Baylor College of Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 1ONP,1Q0H,1Q0L,2EGH,2JCV,2JCX,3A06,3AU9,3UPY,4AIC,4OOE,4OOF,4ZQF,4ZQG,4ZQH,6MH5,8S65 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 51033790 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 20 ChEMBL 10.1021/jm0491501 10.7270/Q2VH5Q21 15887963 Silber, K; Heidler, P; Kurz, T; Klebe, G 5/12/2005 5/20/2013 Philipps University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 1ONP,1Q0H,1Q0L,2EGH,2JCV,2JCX,3A06,3AU9,3UPY,4AIC,4OOE,4OOF,4ZQF,4ZQG,4ZQH,6MH5,8S65 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 51162163 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 1853000 ChEMBL 10.1021/jm060492b 10.7270/Q24J0HW7 17149863 Leon, A; Liu, L; Yang, Y; Hudock, MP; Hall, P; Yin, F; Studer, D; Puan, KJ; Morita, CT; Oldfield, E 12/14/2006 8/23/2020 University of Illinois At Urbana - Champaign http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 1ONP,1Q0H,1Q0L,2EGH,2JCV,2JCX,3A06,3AU9,3UPY,4AIC,4OOE,4OOF,4ZQF,4ZQG,4ZQH,6MH5,8S65 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 293063 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 42 7.5000 Curated from the literature by BindingDB 10.1016/j.bioorg.2015.02.008 10.7270/Q2XS5T4J 25800132 aid1801044 Tritsch, D; Zinglé, C; Rohmer, M; Grosdemange-Billiard, C 4/28/2015 9/3/2015 University of Strasburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 8S65,2JCV,3AU9,2JCX,4AIC,3UPY,4ZQG,4ZQF,2EGH,1ONP,1Q0L,1Q0H,6MH5,3A06,4OOF,4OOE,4ZQH 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 50235830 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 32 ChEMBL 10.1021/jm5010978 10.7270/Q29K4CVJ 25210872 Masini, T; Hirsch, AK 12/16/2014 3/7/2016 University of Groningen http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 1ONP,1Q0H,1Q0L,2EGH,2JCV,2JCX,3A06,3AU9,3UPY,4AIC,4OOE,4OOF,4ZQF,4ZQG,4ZQH,6MH5,8S65 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 50268029 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 32 ChEMBL 10.1016/j.bmc.2014.05.004 10.7270/Q2057HKT 24890653 Zinglé, C; Tritsch, D; Grosdemange-Billiard, C; Rohmer, M 6/16/2014 3/22/2016 University of Strasburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 1ONP,1Q0H,1Q0L,2EGH,2JCV,2JCX,3A06,3AU9,3UPY,4AIC,4OOE,4OOF,4ZQF,4ZQG,4ZQH,6MH5,8S65 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 50330018 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 438 ChEMBL 10.1021/jm5014264 10.7270/Q2639RG9 25781377 Chofor, R; Sooriyaarachchi, S; Risseeuw, MD; Bergfors, T; Pouyez, J; Johny, C; Haymond, A; Everaert, A; Dowd, CS; Maes, L; Coenye, T; Alex, A; Couch, RD; Jones, TA; Wouters, J; Mowbray, SL; Van Calenbergh, S 4/9/2015 5/1/2016 Universiteit Gent http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 1ONP,1Q0H,1Q0L,2EGH,2JCV,2JCX,3A06,3AU9,3UPY,4AIC,4OOE,4OOF,4ZQF,4ZQG,4ZQH,6MH5,8S65 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 50335508 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 30 ChEMBL 10.1016/j.bmcl.2005.12.082 10.7270/Q2FJ2GB6 16439126 Haemers, T; Wiesner, J; Van Poecke, S; Goeman, J; Henschker, D; Beck, E; Jomaa, H; Van Calenbergh, S 2/27/2006 11/10/2009 Ghent University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 1ONP,1Q0H,1Q0L,2EGH,2JCV,2JCX,3A06,3AU9,3UPY,4AIC,4OOE,4OOF,4ZQF,4ZQG,4ZQH,6MH5,8S65 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 50343405 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 48 ChEMBL 10.1021/jm051177c 10.7270/Q22F7N24 16610809 Devreux, V; Wiesner, J; Goeman, JL; Van der Eycken, J; Jomaa, H; Van Calenbergh, S 4/13/2006 11/10/2009 Ghent University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 1ONP,1Q0H,1Q0L,2EGH,2JCV,2JCX,3A06,3AU9,3UPY,4AIC,4OOE,4OOF,4ZQF,4ZQG,4ZQH,6MH5,8S65 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 50920587 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 30 ChEMBL 10.1021/ml100243r 10.7270/Q2XD12NV 21379374 Deng, L; Endo, K; Kato, M; Cheng, G; Yajima, S; Song, Y 3/7/2011 1/4/2013 Baylor College of Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 1ONP,1Q0H,1Q0L,2EGH,2JCV,2JCX,3A06,3AU9,3UPY,4AIC,4OOE,4OOF,4ZQF,4ZQG,4ZQH,6MH5,8S65 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 51033790 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 20 ChEMBL 10.1021/jm0491501 10.7270/Q2VH5Q21 15887963 Silber, K; Heidler, P; Kurz, T; Klebe, G 5/12/2005 5/20/2013 Philipps University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 1ONP,1Q0H,1Q0L,2EGH,2JCV,2JCX,3A06,3AU9,3UPY,4AIC,4OOE,4OOF,4ZQF,4ZQG,4ZQH,6MH5,8S65 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 51162163 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 1853000 ChEMBL 10.1021/jm060492b 10.7270/Q24J0HW7 17149863 Leon, A; Liu, L; Yang, Y; Hudock, MP; Hall, P; Yin, F; Studer, D; Puan, KJ; Morita, CT; Oldfield, E 12/14/2006 8/23/2020 University of Illinois At Urbana - Champaign http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 1ONP,1Q0H,1Q0L,2EGH,2JCV,2JCX,3A06,3AU9,3UPY,4AIC,4OOE,4OOF,4ZQF,4ZQG,4ZQH,6MH5,8S65 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 50920595 c1ccc2c(c1)ccnc2NC(P(=O)(O)O)P(=O)(O)O InChI=1S/C10H12N2O6P2/c13-19(14,15)10(20(16,17)18)12-9-8-4-2-1-3-7(8)5-6-11-9/h1-6,10H,(H,11,12)(H2,13,14,15)(H2,16,17,18) JPVMIOWESIQIGB-UHFFFAOYSA-N 50135835 [(ISOQUINOLIN-1-YLAMINO)-PHOSPHONO-METHYL]-PHOSPHONIC ACID::1-[(Bis-phosphono-methyl)-amino]-isoquinolinium::(isoquinolin-1-ylamino)methylenediphosphonic acid::CHEMBL291727 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 4000 ChEMBL 10.1021/ml100243r 10.7270/Q2XD12NV 21379374 Deng, L; Endo, K; Kato, M; Cheng, G; Yajima, S; Song, Y 3/7/2011 1/4/2013 Baylor College of Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50135835 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50135835&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search IMB 1T1R 405731 104026185 CHEMBL291727 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 50996118 c1ccc2c(c1)ccnc2NC(P(=O)(O)O)P(=O)(O)O InChI=1S/C10H12N2O6P2/c13-19(14,15)10(20(16,17)18)12-9-8-4-2-1-3-7(8)5-6-11-9/h1-6,10H,(H,11,12)(H2,13,14,15)(H2,16,17,18) JPVMIOWESIQIGB-UHFFFAOYSA-N 50135835 [(ISOQUINOLIN-1-YLAMINO)-PHOSPHONO-METHYL]-PHOSPHONIC ACID::1-[(Bis-phosphono-methyl)-amino]-isoquinolinium::(isoquinolin-1-ylamino)methylenediphosphonic acid::CHEMBL291727 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 4000 ChEMBL 10.7270/Q2417288 33303239 Kesharwani, S; Sundriyal, S 3/5/2021 4/18/2024 Birla Institute of Technology and Science-Pilani http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50135835 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50135835&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search IMB 1T1R 405731 104026185 CHEMBL291727 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 50920596 c1cc(ncc1Cl)NC(P(=O)(O)O)P(=O)(O)O InChI=1S/C6H9ClN2O6P2/c7-4-1-2-5(8-3-4)9-6(16(10,11)12)17(13,14)15/h1-3,6H,(H,8,9)(H2,10,11,12)(H2,13,14,15) BNMYZGAZFGNKTH-UHFFFAOYSA-N 50115109 (5-chloropyridin-2-ylamino)methylenediphosphonic acid::[[(5-chloro-2-pyridinyl)amino]methylene]-1,1-bisphosphonate::[(5-Chloro-pyridin-2-ylamino)-phosphono-methyl]-phosphonic acid::CHEMBL54714 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 7000 ChEMBL 10.1021/ml100243r 10.7270/Q2XD12NV 21379374 Deng, L; Endo, K; Kato, M; Cheng, G; Yajima, S; Song, Y 3/7/2011 1/4/2013 Baylor College of Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50115109 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50115109&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search CBQ 1T1S 405389 104009089 CHEMBL54714 DB03649 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 293063 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 42 7.5000 Curated from the literature by BindingDB 10.1016/j.bioorg.2015.02.008 10.7270/Q2XS5T4J 25800132 aid1801044 Tritsch, D; Zinglé, C; Rohmer, M; Grosdemange-Billiard, C 4/28/2015 9/3/2015 University of Strasburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 8S65,2JCV,3AU9,2JCX,4AIC,3UPY,4ZQG,4ZQF,2EGH,1ONP,1Q0L,1Q0H,6MH5,3A06,4OOF,4OOE,4ZQH 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 50235830 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 32 ChEMBL 10.1021/jm5010978 10.7270/Q29K4CVJ 25210872 Masini, T; Hirsch, AK 12/16/2014 3/7/2016 University of Groningen http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 1ONP,1Q0H,1Q0L,2EGH,2JCV,2JCX,3A06,3AU9,3UPY,4AIC,4OOE,4OOF,4ZQF,4ZQG,4ZQH,6MH5,8S65 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 50268029 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 32 ChEMBL 10.1016/j.bmc.2014.05.004 10.7270/Q2057HKT 24890653 Zinglé, C; Tritsch, D; Grosdemange-Billiard, C; Rohmer, M 6/16/2014 3/22/2016 University of Strasburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 1ONP,1Q0H,1Q0L,2EGH,2JCV,2JCX,3A06,3AU9,3UPY,4AIC,4OOE,4OOF,4ZQF,4ZQG,4ZQH,6MH5,8S65 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 50330018 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 438 ChEMBL 10.1021/jm5014264 10.7270/Q2639RG9 25781377 Chofor, R; Sooriyaarachchi, S; Risseeuw, MD; Bergfors, T; Pouyez, J; Johny, C; Haymond, A; Everaert, A; Dowd, CS; Maes, L; Coenye, T; Alex, A; Couch, RD; Jones, TA; Wouters, J; Mowbray, SL; Van Calenbergh, S 4/9/2015 5/1/2016 Universiteit Gent http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 1ONP,1Q0H,1Q0L,2EGH,2JCV,2JCX,3A06,3AU9,3UPY,4AIC,4OOE,4OOF,4ZQF,4ZQG,4ZQH,6MH5,8S65 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 50335508 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 30 ChEMBL 10.1016/j.bmcl.2005.12.082 10.7270/Q2FJ2GB6 16439126 Haemers, T; Wiesner, J; Van Poecke, S; Goeman, J; Henschker, D; Beck, E; Jomaa, H; Van Calenbergh, S 2/27/2006 11/10/2009 Ghent University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 1ONP,1Q0H,1Q0L,2EGH,2JCV,2JCX,3A06,3AU9,3UPY,4AIC,4OOE,4OOF,4ZQF,4ZQG,4ZQH,6MH5,8S65 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 50343405 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 48 ChEMBL 10.1021/jm051177c 10.7270/Q22F7N24 16610809 Devreux, V; Wiesner, J; Goeman, JL; Van der Eycken, J; Jomaa, H; Van Calenbergh, S 4/13/2006 11/10/2009 Ghent University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 1ONP,1Q0H,1Q0L,2EGH,2JCV,2JCX,3A06,3AU9,3UPY,4AIC,4OOE,4OOF,4ZQF,4ZQG,4ZQH,6MH5,8S65 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 50920587 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 30 ChEMBL 10.1021/ml100243r 10.7270/Q2XD12NV 21379374 Deng, L; Endo, K; Kato, M; Cheng, G; Yajima, S; Song, Y 3/7/2011 1/4/2013 Baylor College of Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 1ONP,1Q0H,1Q0L,2EGH,2JCV,2JCX,3A06,3AU9,3UPY,4AIC,4OOE,4OOF,4ZQF,4ZQG,4ZQH,6MH5,8S65 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 51033790 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 20 ChEMBL 10.1021/jm0491501 10.7270/Q2VH5Q21 15887963 Silber, K; Heidler, P; Kurz, T; Klebe, G 5/12/2005 5/20/2013 Philipps University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 1ONP,1Q0H,1Q0L,2EGH,2JCV,2JCX,3A06,3AU9,3UPY,4AIC,4OOE,4OOF,4ZQF,4ZQG,4ZQH,6MH5,8S65 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 51162163 C(CN(C=O)O)CP(=O)(O)O InChI=1S/C4H10NO5P/c6-4-5(7)2-1-3-11(8,9)10/h4,7H,1-3H2,(H2,8,9,10) GJXWDTUCERCKIX-UHFFFAOYSA-N 50153713 3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID::[3-(Formyl-hydroxy-amino)-propyl]-phosphonic acid::3-(N-hydroxyformamido)propylphosphonic acid::fosmidomycin::CHEMBL203125 1-deoxy-D-xylulose 5-phosphate reductoisomerase Escherichia coli (strain K12) 1853000 ChEMBL 10.1021/jm060492b 10.7270/Q24J0HW7 17149863 Leon, A; Liu, L; Yang, Y; Hudock, MP; Hall, P; Yin, F; Studer, D; Puan, KJ; Morita, CT; Oldfield, E 12/14/2006 8/23/2020 University of Illinois At Urbana - Champaign http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50153713 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4735&target=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50153713&enzyme=1-deoxy-D-xylulose+5-phosphate+reductoisomerase&column=ki&startPg=0&Increment=50&submit=Search FOM 1ONP,1Q0H,1Q0L,2EGH,2JCV,2JCX,3A06,3AU9,3UPY,4AIC,4OOE,4OOF,4ZQF,4ZQG,4ZQH,6MH5,8S65 572 104041488 CHEMBL203125 DB02948 1 MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS 1ONP,1ONO,1ONN,1K5H,3R0I,1Q0Q,1Q0L,1Q0H,1T1S,1T1R,1JVS,2EGH,3ANN,3ANM,3ANL 1-deoxy-D-xylulose 5-phosphate reductoisomerase DXR_ECOLI P45568 P77209 Q8KMY5 50099827 C1CCc2nnc(n2CC1)C34CC5CC(C3)CC(C5)C4 InChI=1S/C17H25N3/c1-2-4-15-18-19-16(20(15)5-3-1)17-9-12-6-13(10-17)8-14(7-12)11-17/h12-14H,1-11H2 VFTQRHWULYJKCI-UHFFFAOYSA-N 50239401 MERCK-544::3-Adamantan-1-yl-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine::CHEMBL256777 11-beta-hydroxysteroid dehydrogenase 1 Homo sapiens 8.0 ChEMBL 10.1021/jm4014746 10.7270/Q280546B 24294985 Scott, JS; Goldberg, FW; Turnbull, AV 6/12/2014 2/10/2015 Astrazeneca http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50239401 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1406&target=11-beta-hydroxysteroid+dehydrogenase+1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50239401&enzyme=11-beta-hydroxysteroid+dehydrogenase+1&column=ki&startPg=0&Increment=50&submit=Search A1MBC 9W6V 3630776 104056507 CHEMBL256777 1 MAFMKKYLLPILGLFMAYYYYSANEEFRPEMLQGKKVIVTGASKGIGREMAYHLAKMGAHVVVTARSKETLQKVVSHCLELGAASAHYIAGTMEDMTFAEQFVAQAGKLMGGLDMLILNHITNTSLNLFHDDIHHVRKSMEVNFLSYVVLTVAALPMLKQSNGSIVVVSSLAGKVAYPMVAAYSASKFALDGFFSSIRKEYSVSRVNVSITLCVLGLIDTETAMKAVSGIVHMQAAPKEECALEIIKGGALRQEEVYYDSSLWTTLLIRNPCRKILEFLYSTSYNMDRFINK 9W6V 11-beta-hydroxysteroid dehydrogenase 1 DHI1_HUMAN P28845 B2R9Z1 D3DT89 11-beta-hydroxysteroid dehydrogenase 1 X5D2L1_HUMAN X5D2L1 50413480 C1CCc2nnc(n2CC1)C34CC5CC(C3)CC(C5)C4 InChI=1S/C17H25N3/c1-2-4-15-18-19-16(20(15)5-3-1)17-9-12-6-13(10-17)8-14(7-12)11-17/h12-14H,1-11H2 VFTQRHWULYJKCI-UHFFFAOYSA-N 50239401 MERCK-544::3-Adamantan-1-yl-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine::CHEMBL256777 11-beta-hydroxysteroid dehydrogenase 1 Homo sapiens 7.8 ChEMBL 10.1016/j.bmcl.2008.04.013 10.7270/Q2XP74QM 18440811 Zhu, Y; Olson, SH; Hermanowski-Vosatka, A; Mundt, S; Shah, K; Springer, M; Thieringer, R; Wright, S; Xiao, J; Zokian, H; Balkovec, JM 5/30/2008 1/11/2010 Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50239401 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1406&target=11-beta-hydroxysteroid+dehydrogenase+1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50239401&enzyme=11-beta-hydroxysteroid+dehydrogenase+1&column=ki&startPg=0&Increment=50&submit=Search A1MBC 9W6V 3630776 104056507 CHEMBL256777 1 MAFMKKYLLPILGLFMAYYYYSANEEFRPEMLQGKKVIVTGASKGIGREMAYHLAKMGAHVVVTARSKETLQKVVSHCLELGAASAHYIAGTMEDMTFAEQFVAQAGKLMGGLDMLILNHITNTSLNLFHDDIHHVRKSMEVNFLSYVVLTVAALPMLKQSNGSIVVVSSLAGKVAYPMVAAYSASKFALDGFFSSIRKEYSVSRVNVSITLCVLGLIDTETAMKAVSGIVHMQAAPKEECALEIIKGGALRQEEVYYDSSLWTTLLIRNPCRKILEFLYSTSYNMDRFINK 9W6V 11-beta-hydroxysteroid dehydrogenase 1 DHI1_HUMAN P28845 B2R9Z1 D3DT89 11-beta-hydroxysteroid dehydrogenase 1 X5D2L1_HUMAN X5D2L1 50564964 C1CCc2nnc(n2CC1)C34CC5CC(C3)CC(C5)C4 InChI=1S/C17H25N3/c1-2-4-15-18-19-16(20(15)5-3-1)17-9-12-6-13(10-17)8-14(7-12)11-17/h12-14H,1-11H2 VFTQRHWULYJKCI-UHFFFAOYSA-N 50239401 MERCK-544::3-Adamantan-1-yl-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine::CHEMBL256777 11-beta-hydroxysteroid dehydrogenase 1 Homo sapiens 7.5 ChEMBL 10.1016/j.bmcl.2010.01.082 10.7270/Q2NV9JC3 20149650 Shah, U; Boyle, CD; Chackalamannil, S; Baker, H; Kowalski, T; Lee, J; Terracina, G; Zhang, L 2/22/2010 11/18/2010 Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50239401 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1406&target=11-beta-hydroxysteroid+dehydrogenase+1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50239401&enzyme=11-beta-hydroxysteroid+dehydrogenase+1&column=ki&startPg=0&Increment=50&submit=Search A1MBC 9W6V 3630776 104056507 CHEMBL256777 1 MAFMKKYLLPILGLFMAYYYYSANEEFRPEMLQGKKVIVTGASKGIGREMAYHLAKMGAHVVVTARSKETLQKVVSHCLELGAASAHYIAGTMEDMTFAEQFVAQAGKLMGGLDMLILNHITNTSLNLFHDDIHHVRKSMEVNFLSYVVLTVAALPMLKQSNGSIVVVSSLAGKVAYPMVAAYSASKFALDGFFSSIRKEYSVSRVNVSITLCVLGLIDTETAMKAVSGIVHMQAAPKEECALEIIKGGALRQEEVYYDSSLWTTLLIRNPCRKILEFLYSTSYNMDRFINK 9W6V 11-beta-hydroxysteroid dehydrogenase 1 DHI1_HUMAN P28845 B2R9Z1 D3DT89 11-beta-hydroxysteroid dehydrogenase 1 X5D2L1_HUMAN X5D2L1 50870387 C1CCc2nnc(n2CC1)C34CC5CC(C3)CC(C5)C4 InChI=1S/C17H25N3/c1-2-4-15-18-19-16(20(15)5-3-1)17-9-12-6-13(10-17)8-14(7-12)11-17/h12-14H,1-11H2 VFTQRHWULYJKCI-UHFFFAOYSA-N 50239401 MERCK-544::3-Adamantan-1-yl-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine::CHEMBL256777 11-beta-hydroxysteroid dehydrogenase 1 Homo sapiens 7.8 ChEMBL 10.1016/j.bmcl.2008.04.014 10.7270/Q2H99625 18440812 Zhu, Y; Olson, SH; Graham, D; Patel, G; Hermanowski-Vosatka, A; Mundt, S; Shah, K; Springer, M; Thieringer, R; Wright, S; Xiao, J; Zokian, H; Dragovic, J; Balkovec, JM 5/30/2008 12/16/2012 Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50239401 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1406&target=11-beta-hydroxysteroid+dehydrogenase+1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50239401&enzyme=11-beta-hydroxysteroid+dehydrogenase+1&column=ki&startPg=0&Increment=50&submit=Search A1MBC 9W6V 3630776 104056507 CHEMBL256777 1 MAFMKKYLLPILGLFMAYYYYSANEEFRPEMLQGKKVIVTGASKGIGREMAYHLAKMGAHVVVTARSKETLQKVVSHCLELGAASAHYIAGTMEDMTFAEQFVAQAGKLMGGLDMLILNHITNTSLNLFHDDIHHVRKSMEVNFLSYVVLTVAALPMLKQSNGSIVVVSSLAGKVAYPMVAAYSASKFALDGFFSSIRKEYSVSRVNVSITLCVLGLIDTETAMKAVSGIVHMQAAPKEECALEIIKGGALRQEEVYYDSSLWTTLLIRNPCRKILEFLYSTSYNMDRFINK 9W6V 11-beta-hydroxysteroid dehydrogenase 1 DHI1_HUMAN P28845 B2R9Z1 D3DT89 11-beta-hydroxysteroid dehydrogenase 1 X5D2L1_HUMAN X5D2L1 51069751 C1CCc2nnc(n2CC1)C34CC5CC(C3)CC(C5)C4 InChI=1S/C17H25N3/c1-2-4-15-18-19-16(20(15)5-3-1)17-9-12-6-13(10-17)8-14(7-12)11-17/h12-14H,1-11H2 VFTQRHWULYJKCI-UHFFFAOYSA-N 50239401 MERCK-544::3-Adamantan-1-yl-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine::CHEMBL256777 11-beta-hydroxysteroid dehydrogenase 1 Homo sapiens 7.5 ChEMBL 10.1016/j.ejmech.2013.05.010 10.7270/Q2JS9RV7 23747808 Deng, X; Shen, Y; Yang, J; He, J; Zhao, Y; Peng, LY; Leng, Y; Zhao, QS 7/22/2013 4/13/2014 Chinese Academy of Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50239401 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1406&target=11-beta-hydroxysteroid+dehydrogenase+1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50239401&enzyme=11-beta-hydroxysteroid+dehydrogenase+1&column=ki&startPg=0&Increment=50&submit=Search A1MBC 9W6V 3630776 104056507 CHEMBL256777 1 MAFMKKYLLPILGLFMAYYYYSANEEFRPEMLQGKKVIVTGASKGIGREMAYHLAKMGAHVVVTARSKETLQKVVSHCLELGAASAHYIAGTMEDMTFAEQFVAQAGKLMGGLDMLILNHITNTSLNLFHDDIHHVRKSMEVNFLSYVVLTVAALPMLKQSNGSIVVVSSLAGKVAYPMVAAYSASKFALDGFFSSIRKEYSVSRVNVSITLCVLGLIDTETAMKAVSGIVHMQAAPKEECALEIIKGGALRQEEVYYDSSLWTTLLIRNPCRKILEFLYSTSYNMDRFINK 9W6V 11-beta-hydroxysteroid dehydrogenase 1 DHI1_HUMAN P28845 B2R9Z1 D3DT89 11-beta-hydroxysteroid dehydrogenase 1 X5D2L1_HUMAN X5D2L1 51476188 C1CCc2nnc(n2CC1)C34CC5CC(C3)CC(C5)C4 InChI=1S/C17H25N3/c1-2-4-15-18-19-16(20(15)5-3-1)17-9-12-6-13(10-17)8-14(7-12)11-17/h12-14H,1-11H2 VFTQRHWULYJKCI-UHFFFAOYSA-N 50239401 MERCK-544::3-Adamantan-1-yl-6,7,8,9-tetrahydro-5H-[1,2,4]triazolo[4,3-a]azepine::CHEMBL256777 11-beta-hydroxysteroid dehydrogenase 1 Homo sapiens 7.7 ChEMBL 10.7270/Q2FF3XBX 35537608 Zhang, C; Xu, M; He, C; Zhuo, J; Burns, DM; Qian, DQ; Lin, Q; Li, YL; Chen, L; Shi, E; Agrios, C; Weng, L; Sharief, V; Jalluri, R; Li, Y; Scherle, P; Diamond, S; Hunter, D; Covington, M; Marando, C; Wynn, R; Katiyar, K; Contel, N; Vaddi, K; Yeleswaram, S; Hollis, G; Huber, R; Friedman, S; Metcalf, B; Yao, W 8/1/2022 6/21/2023 Incyte Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50239401 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1406&target=11-beta-hydroxysteroid+dehydrogenase+1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50239401&enzyme=11-beta-hydroxysteroid+dehydrogenase+1&column=ki&startPg=0&Increment=50&submit=Search A1MBC 9W6V 3630776 104056507 CHEMBL256777 1 MAFMKKYLLPILGLFMAYYYYSANEEFRPEMLQGKKVIVTGASKGIGREMAYHLAKMGAHVVVTARSKETLQKVVSHCLELGAASAHYIAGTMEDMTFAEQFVAQAGKLMGGLDMLILNHITNTSLNLFHDDIHHVRKSMEVNFLSYVVLTVAALPMLKQSNGSIVVVSSLAGKVAYPMVAAYSASKFALDGFFSSIRKEYSVSRVNVSITLCVLGLIDTETAMKAVSGIVHMQAAPKEECALEIIKGGALRQEEVYYDSSLWTTLLIRNPCRKILEFLYSTSYNMDRFINK 9W6V 11-beta-hydroxysteroid dehydrogenase 1 DHI1_HUMAN P28845 B2R9Z1 D3DT89 11-beta-hydroxysteroid dehydrogenase 1 X5D2L1_HUMAN X5D2L1 51579794 c1ccc(cc1)CCNC(=O)COc2ccccc2P(=O)(O)O InChI=1S/C16H18NO5P/c18-16(17-11-10-13-6-2-1-3-7-13)12-22-14-8-4-5-9-15(14)23(19,20)21/h1-9H,10-12H2,(H,17,18)(H2,19,20,21) FRNXSTXSXYWTDK-UHFFFAOYSA-N 50635850 CHEMBL5564234 14-3-3 protein beta/alpha Homo sapiens 5200 ChEMBL 10.7270/Q21V5KJN 37984298 Jiang, W; Jiang, Y; Luo, Y; Qiao, W; Yang, T //0 10/11/2025 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50635850 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50007113&target=14-3-3+protein+beta%2Falpha&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50635850&enzyme=14-3-3+protein+beta%2Falpha&column=ki&startPg=0&Increment=50&submit=Search OQE 6YGJ,8BTQ 16419672 519656253 1 MTMDKSELVQKAKLAEQAERYDDMAAAMKAVTEQGHELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTERNEKKQQMGKEYREKIEAELQDICNDVLELLDKYLIPNATQPESKVFYLKMKGDYFRYLSEVASGDNKQTTVSNSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLNEESYKDSTLIMQLLRDNLTLWTSENQGDEGDAGEGEN 8DP5,5N10,4DNK,6A5Q,6HEP,7QI1,6YGJ,9GCP,6BYK,8WF6,8WE2,2V7D,7EXE,4HKC,6EF5,3RDH,9FVL,9FUM,9O2Z,8VYW,8VYV,8VYU,8VYR,8VYQ,8VYP,7MFF,7MFE,7MFD,6Q0K,4BG6,3NKX,3CU8,2WH0,1QJB,1QJA,1IB1,1A4O,1A38,1A37,5ULO,4WRQ,2C1N,2C1J,5XY9,5WXN,9SV3,7D9V,7D8P,7D8H 14-3-3 protein beta/alpha 1433B_HUMAN P31946 A8K9K2 E1P616 50771503 Cc1c(c(c(c(n1)/N=N/c2ccc(cc2)C(=O)O)COP(=O)(O)O)C=O)O InChI=1S/C15H14N3O8P/c1-8-13(20)11(6-19)12(7-26-27(23,24)25)14(16-8)18-17-10-4-2-9(3-5-10)15(21)22/h2-6,20H,7H2,1H3,(H,21,22)(H2,23,24,25) NPBWMMRUXMTIRC-UHFFFAOYSA-N 50102295 4-(4-Formyl-5-hydroxy-6-methyl-3-phosphonooxymethyl-pyridin-2-ylazo)-benzoic acid::CHEMBL119235 14-3-3 protein zeta/delta Homo sapiens 9300 ChEMBL 10.1021/acs.jmedchem.7b01780 10.7270/Q2B27XQN 29328660 Gilberg, E; Gütschow, M; Bajorath, J 2/8/2018 11/3/2019 Rheinische Friedrich-Wilhelms-Universit£T http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50102295 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50007433&target=14-3-3+protein+zeta%2Fdelta&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50102295&enzyme=14-3-3+protein+zeta%2Fdelta&column=ki&startPg=0&Increment=50&submit=Search 3RD 3RDH 6258690 103998835 CHEMBL119235 1 MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQQMAREYREKIETELRDICNDVLSLLEKFLIPNASQAESKVFYLKMKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDTQGDEAEAGEGGEN 7D9V,7D8P,7D8H,5XY9,5WXN,2C1N,2C1J,9FVL,9FUM,8WF6,8WE2,6EF5,3RDH,9SV3,9O2Z,8VYW,8VYV,8VYU,8VYR,8VYQ,8VYP,7MFF,7MFE,7MFD,6Q0K,5ULO,4WRQ,4HKC,4BG6,3NKX,3CU8,2WH0,2V7D,1QJB,1QJA,1IB1,1A4O,1A38,1A37,8VYS,6XAG,6U2H,8QDV,7ZIT,6RLZ,6FNC,6FNB,6FNA,6FN9,6F09,6F08,5M37,5JM4,5J31,5EXA,5EWZ,5D3F,5D2D,2O02,5NAS,6EWW,6EJL,8A9G,6YOS,6YO8,6YMO,4N7Y,4N7G,4IHL,4FJ3,8VYO,5M36,5M35,4N84,8AH2,6ZFG,6ZFD,8P1H,9UJ2,5N10,8DP5,6A5Q,4DNK 14-3-3 protein zeta/delta 1433Z_HUMAN P63104 A8K1N0 B7Z465 P29213 P29312 Q32P43 Q5XJ08 Q6GPI2 Q6IN74 Q6NUR9 Q6P3U9 Q86V33 51126652 Cc1c(c(c(c(n1)/N=N/c2ccc(cc2)C(=O)O)COP(=O)(O)O)C=O)O InChI=1S/C15H14N3O8P/c1-8-13(20)11(6-19)12(7-26-27(23,24)25)14(16-8)18-17-10-4-2-9(3-5-10)15(21)22/h2-6,20H,7H2,1H3,(H,21,22)(H2,23,24,25) NPBWMMRUXMTIRC-UHFFFAOYSA-N 50102295 4-(4-Formyl-5-hydroxy-6-methyl-3-phosphonooxymethyl-pyridin-2-ylazo)-benzoic acid::CHEMBL119235 14-3-3 protein zeta/delta Homo sapiens 9300 ChEMBL 10.1021/acs.jmedchem.7b00574 10.7270/Q2RB7781 28968506 Stevers, LM; Sijbesma, E; Botta, M; MacKintosh, C; Obsil, T; Landrieu, I; Cau, Y; Wilson, AJ; Karawajczyk, A; Eickhoff, J; Davis, J; Hann, M; O'Mahony, G; Doveston, RG; Brunsveld, L; Ottmann, C 5/10/2018 8/17/2020 Eindhoven University of Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50102295 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50007433&target=14-3-3+protein+zeta%2Fdelta&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50102295&enzyme=14-3-3+protein+zeta%2Fdelta&column=ki&startPg=0&Increment=50&submit=Search 3RD 3RDH 6258690 103998835 CHEMBL119235 1 MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQQMAREYREKIETELRDICNDVLSLLEKFLIPNASQAESKVFYLKMKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDTQGDEAEAGEGGEN 7D9V,7D8P,7D8H,5XY9,5WXN,2C1N,2C1J,9FVL,9FUM,8WF6,8WE2,6EF5,3RDH,9SV3,9O2Z,8VYW,8VYV,8VYU,8VYR,8VYQ,8VYP,7MFF,7MFE,7MFD,6Q0K,5ULO,4WRQ,4HKC,4BG6,3NKX,3CU8,2WH0,2V7D,1QJB,1QJA,1IB1,1A4O,1A38,1A37,8VYS,6XAG,6U2H,8QDV,7ZIT,6RLZ,6FNC,6FNB,6FNA,6FN9,6F09,6F08,5M37,5JM4,5J31,5EXA,5EWZ,5D3F,5D2D,2O02,5NAS,6EWW,6EJL,8A9G,6YOS,6YO8,6YMO,4N7Y,4N7G,4IHL,4FJ3,8VYO,5M36,5M35,4N84,8AH2,6ZFG,6ZFD,8P1H,9UJ2,5N10,8DP5,6A5Q,4DNK 14-3-3 protein zeta/delta 1433Z_HUMAN P63104 A8K1N0 B7Z465 P29213 P29312 Q32P43 Q5XJ08 Q6GPI2 Q6IN74 Q6NUR9 Q6P3U9 Q86V33 50073621 C[C@@H](c1c(cncn1)F)[C@](Cn2cncn2)(c3ccc(cc3F)F)O InChI=1S/C16H14F3N5O/c1-10(15-14(19)5-20-7-22-15)16(25,6-24-9-21-8-23-24)12-3-2-11(17)4-13(12)18/h2-5,7-10,25H,6H2,1H3 BCEHBSKCWLPMDN-UHFFFAOYSA-N 50333117 (2R,3S)-2,3-bis(2,4-difluorophenyl)-1-(1H-1,2,4-triazol-1-yl)butan-2-ol::(2R,3S)-2-(2,4-Difluoro-phenyl)-3-(5-fluoro-pyrimidin-4-yl)-1-[1,2,4]triazol-1-yl-butan-2-ol::(2R,3S)-2-(2,4-difluorophenyl)-3-(5-fluoropyrimidin-4-yl)-1-(1H-1,2,4-triazol-1-yl)butan-2-ol::UK-109496::Vfend::CHEMBL638::VORICONAZOLE::US9221791, Voriconazole::US11247981, Example Voriconazole Lanosterol 14a-demethylase Aspergillus fumigatus 423 ChEMBL 10.1128/AAC.00316-10 10.7270/Q2X34XRK 20660663 Warrilow, AG; Melo, N; Martel, CM; Parker, JE; Nes, WD; Kelly, SL; Kelly, DE 9/20/2010 8/23/2011 Swansea University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50333117 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50004698&target=Lanosterol+14a-demethylase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50333117&enzyme=Lanosterol+14a-demethylase&column=ki&startPg=0&Increment=50&submit=Search VOR 3MDT,4UYM,4ZE0,5HS1,6AY6,6H1O,7RY8,7RY9,7RYB 71616 125083219 CHEMBL638 DB00582 C07622 1 MGLIAFILDGICKHCSTQSTWVLVGIGLLSILAVSVIINVLQQLLFKNPHEPPVVFHWFPFIGSTISYGIDPYKFFFDCRAKYGDIFTFILLGKKTTVYLGTKGNDFILNGKLRDVCAEEVYSPLTTPVFGRHVVYDCPNAKLMEQKKFVKYGLTSDALRSYVPLITDEVESFVKNSPAFQGHKGVFDVCKTIAEITIYTASRSLQGKEVRSKFDSTFAELYHNLDMGFAPINFMLPWAPLPHNRKRDAAQRKLTETYMEIIKARRQAGSKKDSEDMVWNLMSCVYKNGTPVPDEEIAHMMIALLMAGQHSSSSTASWIVLRLATRPDIMEELYQEQIRVLGSDLPPLTYDNLQKLDLHAKVIKETLRLHAPIHSIIRAVKNPMAVDGTSYVIPTSHNVLSSPGVTARSEEHFPNPLEWNPHRWDENIAASAEDDEKVDYGYGLVSKGTNSPYLPFGAGRHRCIGEQFAYLQLGTITAVLVRLFRFRNLPGVDGIPDTDYSSLFSKPLGRSFVEFEKRESATKA 5FRB,6CR2,4UYM,4UYL sterol 14alpha-demethylase Q96W81_ASPFM Q96W81 Q4WG45 50622449 C[C@@H](c1c(cncn1)F)[C@](Cn2cncn2)(c3ccc(cc3F)F)O InChI=1S/C16H14F3N5O/c1-10(15-14(19)5-20-7-22-15)16(25,6-24-9-21-8-23-24)12-3-2-11(17)4-13(12)18/h2-5,7-10,25H,6H2,1H3 BCEHBSKCWLPMDN-UHFFFAOYSA-N 50333117 (2R,3S)-2,3-bis(2,4-difluorophenyl)-1-(1H-1,2,4-triazol-1-yl)butan-2-ol::(2R,3S)-2-(2,4-Difluoro-phenyl)-3-(5-fluoro-pyrimidin-4-yl)-1-[1,2,4]triazol-1-yl-butan-2-ol::(2R,3S)-2-(2,4-difluorophenyl)-3-(5-fluoropyrimidin-4-yl)-1-(1H-1,2,4-triazol-1-yl)butan-2-ol::UK-109496::Vfend::CHEMBL638::VORICONAZOLE::US9221791, Voriconazole::US11247981, Example Voriconazole Lanosterol 14a-demethylase Aspergillus fumigatus 429 ChEMBL 10.1128/AAC.00316-10 10.7270/Q2X34XRK 20660663 Warrilow, AG; Melo, N; Martel, CM; Parker, JE; Nes, WD; Kelly, SL; Kelly, DE 9/20/2010 8/23/2011 Swansea University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50333117 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50004698&target=Lanosterol+14a-demethylase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50333117&enzyme=Lanosterol+14a-demethylase&column=ki&startPg=0&Increment=50&submit=Search VOR 3MDT,4UYM,4ZE0,5HS1,6AY6,6H1O,7RY8,7RY9,7RYB 71616 125083219 CHEMBL638 DB00582 C07622 1 MGLIAFILDGICKHCSTQSTWVLVGIGLLSILAVSVIINVLQQLLFKNPHEPPVVFHWFPFIGSTISYGIDPYKFFFDCRAKYGDIFTFILLGKKTTVYLGTKGNDFILNGKLRDVCAEEVYSPLTTPVFGRHVVYDCPNAKLMEQKKFVKYGLTSDALRSYVPLITDEVESFVKNSPAFQGHKGVFDVCKTIAEITIYTASRSLQGKEVRSKFDSTFAELYHNLDMGFAPINFMLPWAPLPHNRKRDAAQRKLTETYMEIIKARRQAGSKKDSEDMVWNLMSCVYKNGTPVPDEEIAHMMIALLMAGQHSSSSTASWIVLRLATRPDIMEELYQEQIRVLGSDLPPLTYDNLQKLDLHAKVIKETLRLHAPIHSIIRAVKNPMAVDGTSYVIPTSHNVLSSPGVTARSEEHFPNPLEWNPHRWDENIAASAEDDEKVDYGYGLVSKGTNSPYLPFGAGRHRCIGEQFAYLQLGTITAVLVRLFRFRNLPGVDGIPDTDYSSLFSKPLGRSFVEFEKRESATKA 5FRB,6CR2,4UYM,4UYL sterol 14alpha-demethylase Q96W81_ASPFM Q96W81 Q4WG45 51101711 c1cc(cc2c1ccc(n2)C(=O)c3ccc(c(c3)O)F)C#N InChI=1S/C17H9FN2O2/c18-13-5-3-12(8-16(13)21)17(22)14-6-4-11-2-1-10(9-19)7-15(11)20-14/h1-8,21H LDOZUOMHDNDABQ-UHFFFAOYSA-N 50422419 CHEMBL4168004 17-beta-hydroxysteroid dehydrogenase 14 Homo sapiens 9.0 ChEMBL 10.1016/j.ejmech.2018.05.029 10.7270/Q23F4S76 29859505 Braun, F; Bertoletti, N; Möller, G; Adamski, J; Frotscher, M; Guragossian, N; Madeira Gírio, PA; Le Borgne, M; Ettouati, L; Falson, P; Müller, S; Vollmer, G; Heine, A; Klebe, G; Marchais-Oberwinkler, S 7/15/2018 8/15/2020 Philipps University Marburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50422419 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50007140&target=17-beta-hydroxysteroid+dehydrogenase+14&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50422419&enzyme=17-beta-hydroxysteroid+dehydrogenase+14&column=ki&startPg=0&Increment=50&submit=Search 9N2 5O7C 134158360 164151294 1 MATGTRYAGKVVVVTGGGRGIGAGIVRAFVNSGARVVICDKDESGGRALEQELPGAVFILCDVTQEDDVKTLVSETIRRFGRLDCVVNNAGHHPPPQRPEETSAQGFRQLLELNLLGTYTLTKLALPYLRKSQGNVINISSLVGAIGQAQAVPYVATKGAVTAMTKALALDESPYGVRVNCISPGNIWTPLWEELAALMPDPRATIREGMLAQPLGRMGQPAEVGAAAVFLASEANFCTGIELLVTGGAELGYGCKASRSTPVDAPDIPS 5EN4,6QCK,6GTU,6GTB,6EMM,5O7C,5O72,5O6Z,5O6X,5O6O,5O43,5O42,5L7Y,5L7W,5L7T,5JS6,5ICM,5HS6 L-fucose dehydrogenase DHB14_HUMAN Q9BPX1 Q9UKU3 51101708 c1ccc2c(c1)ccc(n2)C(=O)c3ccc(c(c3)O)F InChI=1S/C16H10FNO2/c17-12-7-5-11(9-15(12)19)16(20)14-8-6-10-3-1-2-4-13(10)18-14/h1-9,19H JNWWABLECBACFV-UHFFFAOYSA-N 50422416 CHEMBL4171902 17-beta-hydroxysteroid dehydrogenase 14 Homo sapiens 12 ChEMBL 10.1016/j.ejmech.2018.05.029 10.7270/Q23F4S76 29859505 Braun, F; Bertoletti, N; Möller, G; Adamski, J; Frotscher, M; Guragossian, N; Madeira Gírio, PA; Le Borgne, M; Ettouati, L; Falson, P; Müller, S; Vollmer, G; Heine, A; Klebe, G; Marchais-Oberwinkler, S 7/15/2018 8/15/2020 Philipps University Marburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50422416 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50007140&target=17-beta-hydroxysteroid+dehydrogenase+14&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50422416&enzyme=17-beta-hydroxysteroid+dehydrogenase+14&column=ki&startPg=0&Increment=50&submit=Search 9ME 5O6Z 134158358 164151291 1 MATGTRYAGKVVVVTGGGRGIGAGIVRAFVNSGARVVICDKDESGGRALEQELPGAVFILCDVTQEDDVKTLVSETIRRFGRLDCVVNNAGHHPPPQRPEETSAQGFRQLLELNLLGTYTLTKLALPYLRKSQGNVINISSLVGAIGQAQAVPYVATKGAVTAMTKALALDESPYGVRVNCISPGNIWTPLWEELAALMPDPRATIREGMLAQPLGRMGQPAEVGAAAVFLASEANFCTGIELLVTGGAELGYGCKASRSTPVDAPDIPS 5EN4,6QCK,6GTU,6GTB,6EMM,5O7C,5O72,5O6Z,5O6X,5O6O,5O43,5O42,5L7Y,5L7W,5L7T,5JS6,5ICM,5HS6 L-fucose dehydrogenase DHB14_HUMAN Q9BPX1 Q9UKU3 51101704 Cc1ccc2c(c1)ccc(n2)C(=O)c3ccc(c(c3)O)F InChI=1S/C17H12FNO2/c1-10-2-6-14-11(8-10)4-7-15(19-14)17(21)12-3-5-13(18)16(20)9-12/h2-9,20H,1H3 DIBIPWTWYDLKIZ-UHFFFAOYSA-N 50422397 CHEMBL4176263 17-beta-hydroxysteroid dehydrogenase 14 Homo sapiens 6.0 ChEMBL 10.1016/j.ejmech.2018.05.029 10.7270/Q23F4S76 29859505 Braun, F; Bertoletti, N; Möller, G; Adamski, J; Frotscher, M; Guragossian, N; Madeira Gírio, PA; Le Borgne, M; Ettouati, L; Falson, P; Müller, S; Vollmer, G; Heine, A; Klebe, G; Marchais-Oberwinkler, S 7/15/2018 8/15/2020 Philipps University Marburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50422397 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50007140&target=17-beta-hydroxysteroid+dehydrogenase+14&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50422397&enzyme=17-beta-hydroxysteroid+dehydrogenase+14&column=ki&startPg=0&Increment=50&submit=Search 9MK 5O6X 134158357 164151272 1 MATGTRYAGKVVVVTGGGRGIGAGIVRAFVNSGARVVICDKDESGGRALEQELPGAVFILCDVTQEDDVKTLVSETIRRFGRLDCVVNNAGHHPPPQRPEETSAQGFRQLLELNLLGTYTLTKLALPYLRKSQGNVINISSLVGAIGQAQAVPYVATKGAVTAMTKALALDESPYGVRVNCISPGNIWTPLWEELAALMPDPRATIREGMLAQPLGRMGQPAEVGAAAVFLASEANFCTGIELLVTGGAELGYGCKASRSTPVDAPDIPS 5EN4,6QCK,6GTU,6GTB,6EMM,5O7C,5O72,5O6Z,5O6X,5O6O,5O43,5O42,5L7Y,5L7W,5L7T,5JS6,5ICM,5HS6 L-fucose dehydrogenase DHB14_HUMAN Q9BPX1 Q9UKU3 51101707 c1cc(c(c(c1)O)F)c2cccc(n2)Oc3ccc(c(c3)O)F InChI=1S/C17H11F2NO3/c18-12-8-7-10(9-15(12)22)23-16-6-2-4-13(20-16)11-3-1-5-14(21)17(11)19/h1-9,21-22H URNXTVXZHNOBRL-UHFFFAOYSA-N 50422402 CHEMBL4171183 17-beta-hydroxysteroid dehydrogenase 14 Homo sapiens 58 ChEMBL 10.1016/j.ejmech.2018.05.029 10.7270/Q23F4S76 29859505 Braun, F; Bertoletti, N; Möller, G; Adamski, J; Frotscher, M; Guragossian, N; Madeira Gírio, PA; Le Borgne, M; Ettouati, L; Falson, P; Müller, S; Vollmer, G; Heine, A; Klebe, G; Marchais-Oberwinkler, S 7/15/2018 8/15/2020 Philipps University Marburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50422402 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50007140&target=17-beta-hydroxysteroid+dehydrogenase+14&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50422402&enzyme=17-beta-hydroxysteroid+dehydrogenase+14&column=ki&startPg=0&Increment=50&submit=Search 9MB 5O6O 134158356 164151277 1 MATGTRYAGKVVVVTGGGRGIGAGIVRAFVNSGARVVICDKDESGGRALEQELPGAVFILCDVTQEDDVKTLVSETIRRFGRLDCVVNNAGHHPPPQRPEETSAQGFRQLLELNLLGTYTLTKLALPYLRKSQGNVINISSLVGAIGQAQAVPYVATKGAVTAMTKALALDESPYGVRVNCISPGNIWTPLWEELAALMPDPRATIREGMLAQPLGRMGQPAEVGAAAVFLASEANFCTGIELLVTGGAELGYGCKASRSTPVDAPDIPS 5EN4,6QCK,6GTU,6GTB,6EMM,5O7C,5O72,5O6Z,5O6X,5O6O,5O43,5O42,5L7Y,5L7W,5L7T,5JS6,5ICM,5HS6 L-fucose dehydrogenase DHB14_HUMAN Q9BPX1 Q9UKU3 51101718 CN(c1ccc(c(c1)O)F)c2cccc(n2)c3cccc(c3F)O InChI=1S/C18H14F2N2O2/c1-22(11-8-9-13(19)16(24)10-11)17-7-3-5-14(21-17)12-4-2-6-15(23)18(12)20/h2-10,23-24H,1H3 TZILIAOKSRIZHK-UHFFFAOYSA-N 50422426 CHEMBL4169325 17-beta-hydroxysteroid dehydrogenase 14 Homo sapiens 42 ChEMBL 10.1016/j.ejmech.2018.05.029 10.7270/Q23F4S76 29859505 Braun, F; Bertoletti, N; Möller, G; Adamski, J; Frotscher, M; Guragossian, N; Madeira Gírio, PA; Le Borgne, M; Ettouati, L; Falson, P; Müller, S; Vollmer, G; Heine, A; Klebe, G; Marchais-Oberwinkler, S 7/15/2018 8/15/2020 Philipps University Marburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50422426 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50007140&target=17-beta-hydroxysteroid+dehydrogenase+14&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50422426&enzyme=17-beta-hydroxysteroid+dehydrogenase+14&column=ki&startPg=0&Increment=50&submit=Search 9JQ 5O43 134158355 164151301 1 MATGTRYAGKVVVVTGGGRGIGAGIVRAFVNSGARVVICDKDESGGRALEQELPGAVFILCDVTQEDDVKTLVSETIRRFGRLDCVVNNAGHHPPPQRPEETSAQGFRQLLELNLLGTYTLTKLALPYLRKSQGNVINISSLVGAIGQAQAVPYVATKGAVTAMTKALALDESPYGVRVNCISPGNIWTPLWEELAALMPDPRATIREGMLAQPLGRMGQPAEVGAAAVFLASEANFCTGIELLVTGGAELGYGCKASRSTPVDAPDIPS 5EN4,6QCK,6GTU,6GTB,6EMM,5O7C,5O72,5O6Z,5O6X,5O6O,5O43,5O42,5L7Y,5L7W,5L7T,5JS6,5ICM,5HS6 L-fucose dehydrogenase DHB14_HUMAN Q9BPX1 Q9UKU3 50523713 Cc1cc(ccc1O)c2cccc(n2)C(=O)c3ccc(c(c3)O)F InChI=1S/C19H14FNO3/c1-11-9-12(6-8-17(11)22)15-3-2-4-16(21-15)19(24)13-5-7-14(20)18(23)10-13/h2-10,22-23H,1H3 QDDLZOOWBSJEFI-UHFFFAOYSA-N 50360236 CHEMBL1928172 17-beta-hydroxysteroid dehydrogenase 14 Homo sapiens 26 ChEMBL 10.1021/acs.jmedchem.6b01436 10.7270/Q2KH0Q9S 27933965 Braun, F; Bertoletti, N; Möller, G; Adamski, J; Steinmetzer, T; Salah, M; Abdelsamie, AS; van Koppen, CJ; Heine, A; Klebe, G; Marchais-Oberwinkler, S 12/8/2016 7/17/2018 Philipps University Marburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50360236 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50007140&target=17-beta-hydroxysteroid+dehydrogenase+14&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50360236&enzyme=17-beta-hydroxysteroid+dehydrogenase+14&column=ki&startPg=0&Increment=50&submit=Search 6QJ 5L7T 57395345 136964298 CHEMBL1928172 1 MATGTRYAGKVVVVTGGGRGIGAGIVRAFVNSGARVVICDKDESGGRALEQELPGAVFILCDVTQEDDVKTLVSETIRRFGRLDCVVNNAGHHPPPQRPEETSAQGFRQLLELNLLGTYTLTKLALPYLRKSQGNVINISSLVGAIGQAQAVPYVATKGAVTAMTKALALDESPYGVRVNCISPGNIWTPLWEELAALMPDPRATIREGMLAQPLGRMGQPAEVGAAAVFLASEANFCTGIELLVTGGAELGYGCKASRSTPVDAPDIPS 5EN4,6QCK,6GTU,6GTB,6EMM,5O7C,5O72,5O6Z,5O6X,5O6O,5O43,5O42,5L7Y,5L7W,5L7T,5JS6,5ICM,5HS6 L-fucose dehydrogenase DHB14_HUMAN Q9BPX1 Q9UKU3 51101717 C=C(c1ccc(c(c1)O)F)c2cccc(n2)c3cccc(c3F)O InChI=1S/C19H13F2NO2/c1-11(12-8-9-14(20)18(24)10-12)15-5-3-6-16(22-15)13-4-2-7-17(23)19(13)21/h2-10,23-24H,1H2 LSHVGZUGKOCADJ-UHFFFAOYSA-N 50422425 CHEMBL4175585 17-beta-hydroxysteroid dehydrogenase 14 Homo sapiens 1.5 ChEMBL 10.1016/j.ejmech.2018.05.029 10.7270/Q23F4S76 29859505 Braun, F; Bertoletti, N; Möller, G; Adamski, J; Frotscher, M; Guragossian, N; Madeira Gírio, PA; Le Borgne, M; Ettouati, L; Falson, P; Müller, S; Vollmer, G; Heine, A; Klebe, G; Marchais-Oberwinkler, S 7/15/2018 8/15/2020 Philipps University Marburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50422425 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50007140&target=17-beta-hydroxysteroid+dehydrogenase+14&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50422425&enzyme=17-beta-hydroxysteroid+dehydrogenase+14&column=ki&startPg=0&Increment=50&submit=Search 9JW 5O42 134158354 164151300 1 MATGTRYAGKVVVVTGGGRGIGAGIVRAFVNSGARVVICDKDESGGRALEQELPGAVFILCDVTQEDDVKTLVSETIRRFGRLDCVVNNAGHHPPPQRPEETSAQGFRQLLELNLLGTYTLTKLALPYLRKSQGNVINISSLVGAIGQAQAVPYVATKGAVTAMTKALALDESPYGVRVNCISPGNIWTPLWEELAALMPDPRATIREGMLAQPLGRMGQPAEVGAAAVFLASEANFCTGIELLVTGGAELGYGCKASRSTPVDAPDIPS 5EN4,6QCK,6GTU,6GTB,6EMM,5O7C,5O72,5O6Z,5O6X,5O6O,5O43,5O42,5L7Y,5L7W,5L7T,5JS6,5ICM,5HS6 L-fucose dehydrogenase DHB14_HUMAN Q9BPX1 Q9UKU3 50147450 C[C@]12CC[C@@H]3c4ccc(cc4CC[C@H]3[C@@H]1CCC2=O)O InChI=1S/C18H22O2/c1-18-9-8-14-13-5-3-12(19)10-11(13)2-4-15(14)16(18)6-7-17(18)20/h3,5,10,14-16,19H,2,4,6-9H2,1H3 DNXHEGUUPJUMQT-UHFFFAOYSA-N 17289 folliculin::(1S,10R,11S,15S)-5-hydroxy-15-methyltetracyclo[8.7.0.0^{2,7}.0^{11,15}]heptadeca-2,4,6-trien-14-one::[2,4,6,7-3H]-Estrone::Theelin::CHEMBL1405::[2,4,6,7-3H]-E1::Estrone (E1)::Estrone::Estrovarin::Kestrone::Unigen::Estrone, 15 17-beta-hydroxysteroid dehydrogenase type 1 Homo sapiens 810 ChEMBL 10.1016/j.ejmech.2008.01.044 10.7270/Q2P84BP6 18372081 Fournier, D; Poirier, D; Mazumdar, M; Lin, SX 10/28/2008 1/11/2010 Chuq-Pavillon Chul and Université http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=17289 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5642&target=17-beta-hydroxysteroid+dehydrogenase+type+1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=17289&enzyme=17-beta-hydroxysteroid+dehydrogenase+type+1&column=ki&startPg=0&Increment=50&submit=Search J3Z 3HM1,5HS6,6MNC,6MNE,7RY4,7X3Z 5870 46517467 CHEMBL1405 DB00655 C00468 1 MARTVVLITGCSSGIGLHLAVRLASDPSQSFKVYATLRDLKTQGRLWEAARALACPPGSLETLQLDVRDSKSVAAARERVTEGRVDVLVCNAGLGLLGPLEALGEDAVASVLDVNVVGTVRMLQAFLPDMKRRGSGRVLVTGSVGGLMGLPFNDVYCASKFALEGLCESLAVLLLPFGVHLSLIECGPVHTAFMEKVLGSPEEVLDRTDIHTFHRFYQYLAHSKQVFREAAQNPEEVAEVFLTALRAPKPTLRYFTTERFLPLLRMRLDDPSGSNYVTAMHREVFGDVPAKAEAGAEAGGGAGPGAEDEAGRGAVGDPELGDPPAAPQ 7X3Z,6MNE,6MNC,6DTP,6CGE,6CGC,1A27 17-beta-hydroxysteroid dehydrogenase type 1 DHB1_HUMAN P14061 B3KXS1 Q2M2L8 50147451 C[C@]12CC[C@@H]3c4ccc(cc4CC[C@H]3[C@@H]1CCC2=O)O InChI=1S/C18H22O2/c1-18-9-8-14-13-5-3-12(19)10-11(13)2-4-15(14)16(18)6-7-17(18)20/h3,5,10,14-16,19H,2,4,6-9H2,1H3 DNXHEGUUPJUMQT-UHFFFAOYSA-N 17289 folliculin::(1S,10R,11S,15S)-5-hydroxy-15-methyltetracyclo[8.7.0.0^{2,7}.0^{11,15}]heptadeca-2,4,6-trien-14-one::[2,4,6,7-3H]-Estrone::Theelin::CHEMBL1405::[2,4,6,7-3H]-E1::Estrone (E1)::Estrone::Estrovarin::Kestrone::Unigen::Estrone, 15 17-beta-hydroxysteroid dehydrogenase type 1 Homo sapiens 600 ChEMBL 10.1016/j.ejmech.2008.01.044 10.7270/Q2P84BP6 18372081 Fournier, D; Poirier, D; Mazumdar, M; Lin, SX 10/28/2008 1/11/2010 Chuq-Pavillon Chul and Université http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=17289 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5642&target=17-beta-hydroxysteroid+dehydrogenase+type+1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=17289&enzyme=17-beta-hydroxysteroid+dehydrogenase+type+1&column=ki&startPg=0&Increment=50&submit=Search J3Z 3HM1,5HS6,6MNC,6MNE,7RY4,7X3Z 5870 46517467 CHEMBL1405 DB00655 C00468 1 MARTVVLITGCSSGIGLHLAVRLASDPSQSFKVYATLRDLKTQGRLWEAARALACPPGSLETLQLDVRDSKSVAAARERVTEGRVDVLVCNAGLGLLGPLEALGEDAVASVLDVNVVGTVRMLQAFLPDMKRRGSGRVLVTGSVGGLMGLPFNDVYCASKFALEGLCESLAVLLLPFGVHLSLIECGPVHTAFMEKVLGSPEEVLDRTDIHTFHRFYQYLAHSKQVFREAAQNPEEVAEVFLTALRAPKPTLRYFTTERFLPLLRMRLDDPSGSNYVTAMHREVFGDVPAKAEAGAEAGGGAGPGAEDEAGRGAVGDPELGDPPAAPQ 7X3Z,6MNE,6MNC,6DTP,6CGE,6CGC,1A27 17-beta-hydroxysteroid dehydrogenase type 1 DHB1_HUMAN P14061 B3KXS1 Q2M2L8 50147455 C[C@]12CC[C@@H]3c4ccc(cc4CC[C@H]3[C@@H]1CCC2=O)O InChI=1S/C18H22O2/c1-18-9-8-14-13-5-3-12(19)10-11(13)2-4-15(14)16(18)6-7-17(18)20/h3,5,10,14-16,19H,2,4,6-9H2,1H3 DNXHEGUUPJUMQT-UHFFFAOYSA-N 17289 folliculin::(1S,10R,11S,15S)-5-hydroxy-15-methyltetracyclo[8.7.0.0^{2,7}.0^{11,15}]heptadeca-2,4,6-trien-14-one::[2,4,6,7-3H]-Estrone::Theelin::CHEMBL1405::[2,4,6,7-3H]-E1::Estrone (E1)::Estrone::Estrovarin::Kestrone::Unigen::Estrone, 15 17-beta-hydroxysteroid dehydrogenase type 1 Homo sapiens 3 ChEMBL 10.1016/j.ejmech.2008.01.044 10.7270/Q2P84BP6 18372081 Fournier, D; Poirier, D; Mazumdar, M; Lin, SX 10/28/2008 1/11/2010 Chuq-Pavillon Chul and Université http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=17289 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5642&target=17-beta-hydroxysteroid+dehydrogenase+type+1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=17289&enzyme=17-beta-hydroxysteroid+dehydrogenase+type+1&column=ki&startPg=0&Increment=50&submit=Search J3Z 3HM1,5HS6,6MNC,6MNE,7RY4,7X3Z 5870 46517467 CHEMBL1405 DB00655 C00468 1 MARTVVLITGCSSGIGLHLAVRLASDPSQSFKVYATLRDLKTQGRLWEAARALACPPGSLETLQLDVRDSKSVAAARERVTEGRVDVLVCNAGLGLLGPLEALGEDAVASVLDVNVVGTVRMLQAFLPDMKRRGSGRVLVTGSVGGLMGLPFNDVYCASKFALEGLCESLAVLLLPFGVHLSLIECGPVHTAFMEKVLGSPEEVLDRTDIHTFHRFYQYLAHSKQVFREAAQNPEEVAEVFLTALRAPKPTLRYFTTERFLPLLRMRLDDPSGSNYVTAMHREVFGDVPAKAEAGAEAGGGAGPGAEDEAGRGAVGDPELGDPPAAPQ 7X3Z,6MNE,6MNC,6DTP,6CGE,6CGC,1A27 17-beta-hydroxysteroid dehydrogenase type 1 DHB1_HUMAN P14061 B3KXS1 Q2M2L8 50836306 C[C@]12CC[C@@H]3c4ccc(cc4CC[C@H]3[C@@H]1CCC2=O)O InChI=1S/C18H22O2/c1-18-9-8-14-13-5-3-12(19)10-11(13)2-4-15(14)16(18)6-7-17(18)20/h3,5,10,14-16,19H,2,4,6-9H2,1H3 DNXHEGUUPJUMQT-UHFFFAOYSA-N 17289 folliculin::(1S,10R,11S,15S)-5-hydroxy-15-methyltetracyclo[8.7.0.0^{2,7}.0^{11,15}]heptadeca-2,4,6-trien-14-one::[2,4,6,7-3H]-Estrone::Theelin::CHEMBL1405::[2,4,6,7-3H]-E1::Estrone (E1)::Estrone::Estrovarin::Kestrone::Unigen::Estrone, 15 17-beta-hydroxysteroid dehydrogenase type 1 Homo sapiens 330 ChEMBL 10.1021/jm050830t 10.7270/Q2C24X7J 16480268 Allan, GM; Lawrence, HR; Cornet, J; Bubert, C; Fischer, DS; Vicker, N; Smith, A; Tutill, HJ; Purohit, A; Day, JM; Mahon, MF; Reed, MJ; Potter, BV 2/16/2006 12/6/2012 University of Bath http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=17289 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5642&target=17-beta-hydroxysteroid+dehydrogenase+type+1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=17289&enzyme=17-beta-hydroxysteroid+dehydrogenase+type+1&column=ki&startPg=0&Increment=50&submit=Search J3Z 3HM1,5HS6,6MNC,6MNE,7RY4,7X3Z 5870 46517467 CHEMBL1405 DB00655 C00468 1 MARTVVLITGCSSGIGLHLAVRLASDPSQSFKVYATLRDLKTQGRLWEAARALACPPGSLETLQLDVRDSKSVAAARERVTEGRVDVLVCNAGLGLLGPLEALGEDAVASVLDVNVVGTVRMLQAFLPDMKRRGSGRVLVTGSVGGLMGLPFNDVYCASKFALEGLCESLAVLLLPFGVHLSLIECGPVHTAFMEKVLGSPEEVLDRTDIHTFHRFYQYLAHSKQVFREAAQNPEEVAEVFLTALRAPKPTLRYFTTERFLPLLRMRLDDPSGSNYVTAMHREVFGDVPAKAEAGAEAGGGAGPGAEDEAGRGAVGDPELGDPPAAPQ 7X3Z,6MNE,6MNC,6DTP,6CGE,6CGC,1A27 17-beta-hydroxysteroid dehydrogenase type 1 DHB1_HUMAN P14061 B3KXS1 Q2M2L8 50860030 C[C@]12CC[C@@H]3c4ccc(cc4CC[C@H]3[C@@H]1CCC2=O)O InChI=1S/C18H22O2/c1-18-9-8-14-13-5-3-12(19)10-11(13)2-4-15(14)16(18)6-7-17(18)20/h3,5,10,14-16,19H,2,4,6-9H2,1H3 DNXHEGUUPJUMQT-UHFFFAOYSA-N 17289 folliculin::(1S,10R,11S,15S)-5-hydroxy-15-methyltetracyclo[8.7.0.0^{2,7}.0^{11,15}]heptadeca-2,4,6-trien-14-one::[2,4,6,7-3H]-Estrone::Theelin::CHEMBL1405::[2,4,6,7-3H]-E1::Estrone (E1)::Estrone::Estrovarin::Kestrone::Unigen::Estrone, 15 17-beta-hydroxysteroid dehydrogenase type 1 Homo sapiens 218 ChEMBL 10.1016/j.bmc.2007.11.007 10.7270/Q2KP8302 18035543 Laplante, Y; Cadot, C; Fournier, MA; Poirier, D 2/18/2008 12/15/2012 Chuq-Pavillon Chul and Universit£ http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=17289 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5642&target=17-beta-hydroxysteroid+dehydrogenase+type+1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=17289&enzyme=17-beta-hydroxysteroid+dehydrogenase+type+1&column=ki&startPg=0&Increment=50&submit=Search J3Z 3HM1,5HS6,6MNC,6MNE,7RY4,7X3Z 5870 46517467 CHEMBL1405 DB00655 C00468 1 MARTVVLITGCSSGIGLHLAVRLASDPSQSFKVYATLRDLKTQGRLWEAARALACPPGSLETLQLDVRDSKSVAAARERVTEGRVDVLVCNAGLGLLGPLEALGEDAVASVLDVNVVGTVRMLQAFLPDMKRRGSGRVLVTGSVGGLMGLPFNDVYCASKFALEGLCESLAVLLLPFGVHLSLIECGPVHTAFMEKVLGSPEEVLDRTDIHTFHRFYQYLAHSKQVFREAAQNPEEVAEVFLTALRAPKPTLRYFTTERFLPLLRMRLDDPSGSNYVTAMHREVFGDVPAKAEAGAEAGGGAGPGAEDEAGRGAVGDPELGDPPAAPQ 7X3Z,6MNE,6MNC,6DTP,6CGE,6CGC,1A27 17-beta-hydroxysteroid dehydrogenase type 1 DHB1_HUMAN P14061 B3KXS1 Q2M2L8 50909886 C[C@]12CC[C@@H]3c4ccc(cc4CC[C@H]3[C@@H]1CCC2=O)O InChI=1S/C18H22O2/c1-18-9-8-14-13-5-3-12(19)10-11(13)2-4-15(14)16(18)6-7-17(18)20/h3,5,10,14-16,19H,2,4,6-9H2,1H3 DNXHEGUUPJUMQT-UHFFFAOYSA-N 17289 folliculin::(1S,10R,11S,15S)-5-hydroxy-15-methyltetracyclo[8.7.0.0^{2,7}.0^{11,15}]heptadeca-2,4,6-trien-14-one::[2,4,6,7-3H]-Estrone::Theelin::CHEMBL1405::[2,4,6,7-3H]-E1::Estrone (E1)::Estrone::Estrovarin::Kestrone::Unigen::Estrone, 15 17-beta-hydroxysteroid dehydrogenase type 1 Homo sapiens 109 ChEMBL 10.1016/j.bmcl.2009.09.113 10.7270/Q20K29HP 19836949 Moller, G; Deluca, D; Gege, C; Rosinus, A; Kowalik, D; Peters, O; Droescher, P; Elger, W; Adamski, J; Hillisch, A 11/5/2009 12/29/2012 Institute of Experimental Genetics http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=17289 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5642&target=17-beta-hydroxysteroid+dehydrogenase+type+1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=17289&enzyme=17-beta-hydroxysteroid+dehydrogenase+type+1&column=ki&startPg=0&Increment=50&submit=Search J3Z 3HM1,5HS6,6MNC,6MNE,7RY4,7X3Z 5870 46517467 CHEMBL1405 DB00655 C00468 1 MARTVVLITGCSSGIGLHLAVRLASDPSQSFKVYATLRDLKTQGRLWEAARALACPPGSLETLQLDVRDSKSVAAARERVTEGRVDVLVCNAGLGLLGPLEALGEDAVASVLDVNVVGTVRMLQAFLPDMKRRGSGRVLVTGSVGGLMGLPFNDVYCASKFALEGLCESLAVLLLPFGVHLSLIECGPVHTAFMEKVLGSPEEVLDRTDIHTFHRFYQYLAHSKQVFREAAQNPEEVAEVFLTALRAPKPTLRYFTTERFLPLLRMRLDDPSGSNYVTAMHREVFGDVPAKAEAGAEAGGGAGPGAEDEAGRGAVGDPELGDPPAAPQ 7X3Z,6MNE,6MNC,6DTP,6CGE,6CGC,1A27 17-beta-hydroxysteroid dehydrogenase type 1 DHB1_HUMAN P14061 B3KXS1 Q2M2L8 50977487 C[C@]12CC[C@@H]3c4ccc(cc4CC[C@H]3[C@@H]1CCC2=O)O InChI=1S/C18H22O2/c1-18-9-8-14-13-5-3-12(19)10-11(13)2-4-15(14)16(18)6-7-17(18)20/h3,5,10,14-16,19H,2,4,6-9H2,1H3 DNXHEGUUPJUMQT-UHFFFAOYSA-N 17289 folliculin::(1S,10R,11S,15S)-5-hydroxy-15-methyltetracyclo[8.7.0.0^{2,7}.0^{11,15}]heptadeca-2,4,6-trien-14-one::[2,4,6,7-3H]-Estrone::Theelin::CHEMBL1405::[2,4,6,7-3H]-E1::Estrone (E1)::Estrone::Estrovarin::Kestrone::Unigen::Estrone, 15 17-beta-hydroxysteroid dehydrogenase type 1 Homo sapiens 9500 ChEMBL 10.1021/jm1013693 10.7270/Q24M95PH 21413808 Meanwell, NA 4/21/2011 5/17/2013 Bristol-Myers Squibb Pharmaceutical Research and Development http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=17289 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5642&target=17-beta-hydroxysteroid+dehydrogenase+type+1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=17289&enzyme=17-beta-hydroxysteroid+dehydrogenase+type+1&column=ki&startPg=0&Increment=50&submit=Search J3Z 3HM1,5HS6,6MNC,6MNE,7RY4,7X3Z 5870 46517467 CHEMBL1405 DB00655 C00468 1 MARTVVLITGCSSGIGLHLAVRLASDPSQSFKVYATLRDLKTQGRLWEAARALACPPGSLETLQLDVRDSKSVAAARERVTEGRVDVLVCNAGLGLLGPLEALGEDAVASVLDVNVVGTVRMLQAFLPDMKRRGSGRVLVTGSVGGLMGLPFNDVYCASKFALEGLCESLAVLLLPFGVHLSLIECGPVHTAFMEKVLGSPEEVLDRTDIHTFHRFYQYLAHSKQVFREAAQNPEEVAEVFLTALRAPKPTLRYFTTERFLPLLRMRLDDPSGSNYVTAMHREVFGDVPAKAEAGAEAGGGAGPGAEDEAGRGAVGDPELGDPPAAPQ 7X3Z,6MNE,6MNC,6DTP,6CGE,6CGC,1A27 17-beta-hydroxysteroid dehydrogenase type 1 DHB1_HUMAN P14061 B3KXS1 Q2M2L8 51401133 c1cc(nc(c1)C(=O)O)C(=O)O InChI=1S/C7H5NO4/c9-6(10)4-2-1-3-5(8-4)7(11)12/h1-3H,(H,9,10)(H,11,12) WJJMNDUMQPNECX-UHFFFAOYSA-N 26116 Dipicolinate::CHEMBL284104::pyridine-2,6-dicarboxylic acid::pyridine carboxylate, 6d 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase Homo sapiens 15200 ChEMBL 10.1021/acs.jmedchem.0c01762 10.7270/Q22N5605 33369426 Yang, Y; Borel, T; de Azambuja, F; Johnson, D; Sorrentino, JP; Udokwu, C; Davis, I; Liu, A; Altman, RA 1/14/2021 3/30/2022 University of Texas At San Antonio http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=26116 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=415&target=2-amino-3-carboxymuconate-6-semialdehyde+decarboxylase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=26116&enzyme=2-amino-3-carboxymuconate-6-semialdehyde+decarboxylase&column=ki&startPg=0&Increment=50&submit=Search PDC 1ARZ,1C3V,1P9L,2PC2,2PE7,2PES,3LGR,3OJO,4IH3,4IRW,5CQ6,5TEM,5TJY,5TJZ,5US6,5Z2E,5Z2F,8S3A 10367 56464553 CHEMBL284104 DB04267 1 MKIDIHSHILPKEWPDLKKRFGYGGWVQLQHHSKGEAKLLKDGKVFRVVRENCWDPEVRIREMDQKGVTVQALSTVPVMFSYWAKPEDTLNLCQLLNNDLASTVVSYPRRFVGLGTLPMQAPELAVKEMERCVKELGFPGVQIGTHVNEWDLNAQELFPVYAAAERLKCSLFVHPWDMQMDGRMAKYWLPWLVGMPAETTIAICSMIMGGVFEKFPKLKVCFAHGGGAFPFTVGRISHGFSMRPDLCAQDNPMNPKKYLGSFYTDALVHDPLSLKLLTDVIGKDKVILGTDYPFPLGELEPGKLIESMEEFDEETKNKLKAGNALAFLGLERKQFE 7PWY,2WM1,4OFC,4IH3,4IGM 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase ACMSD_HUMAN Q8TDX5 Q3B7X3 Q53SR5 Q96KY2 51401135 c1cc(nc(c1)C(=O)O)C(=O)O InChI=1S/C7H5NO4/c9-6(10)4-2-1-3-5(8-4)7(11)12/h1-3H,(H,9,10)(H,11,12) WJJMNDUMQPNECX-UHFFFAOYSA-N 26116 Dipicolinate::CHEMBL284104::pyridine-2,6-dicarboxylic acid::pyridine carboxylate, 6d 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase Homo sapiens 15200 ChEMBL 10.1021/acs.jmedchem.0c01762 10.7270/Q22N5605 33369426 Yang, Y; Borel, T; de Azambuja, F; Johnson, D; Sorrentino, JP; Udokwu, C; Davis, I; Liu, A; Altman, RA 1/14/2021 3/30/2022 University of Texas At San Antonio http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=26116 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=415&target=2-amino-3-carboxymuconate-6-semialdehyde+decarboxylase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=26116&enzyme=2-amino-3-carboxymuconate-6-semialdehyde+decarboxylase&column=ki&startPg=0&Increment=50&submit=Search PDC 1ARZ,1C3V,1P9L,2PC2,2PE7,2PES,3LGR,3OJO,4IH3,4IRW,5CQ6,5TEM,5TJY,5TJZ,5US6,5Z2E,5Z2F,8S3A 10367 56464553 CHEMBL284104 DB04267 1 MKIDIHSHILPKEWPDLKKRFGYGGWVQLQHHSKGEAKLLKDGKVFRVVRENCWDPEVRIREMDQKGVTVQALSTVPVMFSYWAKPEDTLNLCQLLNNDLASTVVSYPRRFVGLGTLPMQAPELAVKEMERCVKELGFPGVQIGTHVNEWDLNAQELFPVYAAAERLKCSLFVHPWDMQMDGRMAKYWLPWLVGMPAETTIAICSMIMGGVFEKFPKLKVCFAHGGGAFPFTVGRISHGFSMRPDLCAQDNPMNPKKYLGSFYTDALVHDPLSLKLLTDVIGKDKVILGTDYPFPLGELEPGKLIESMEEFDEETKNKLKAGNALAFLGLERKQFE 7PWY,2WM1,4OFC,4IH3,4IGM 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase ACMSD_HUMAN Q8TDX5 Q3B7X3 Q53SR5 Q96KY2 493601 c1cc(cc(c1)CSC2=NC(=C(C(=O)N2)C#N)c3cccs3)CC(=O)O InChI=1S/C18H13N3O3S2/c19-9-13-16(14-5-2-6-25-14)20-18(21-17(13)24)26-10-12-4-1-3-11(7-12)8-15(22)23/h1-7H,8,10H2,(H,22,23)(H,20,21,24) RJQYGCGMQYVVIB-UHFFFAOYSA-N 261607 US9708272, 18::US10513499, Compound 18::US11254644, Compound 18 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase Homo sapiens 10.00 US Patent 10.7270/Q20P1215 aid1795200 US9708272 Pellicciari, R; Auwerx, J; Raffaelli, N 7/18/2017 10/30/2018 Tes Pharma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=261607 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=415&target=2-amino-3-carboxymuconate-6-semialdehyde+decarboxylase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=261607&enzyme=2-amino-3-carboxymuconate-6-semialdehyde+decarboxylase&column=ki&startPg=0&Increment=50&submit=Search 8EK 7PWY 134823475 376223449 1 MKIDIHSHILPKEWPDLKKRFGYGGWVQLQHHSKGEAKLLKDGKVFRVVRENCWDPEVRIREMDQKGVTVQALSTVPVMFSYWAKPEDTLNLCQLLNNDLASTVVSYPRRFVGLGTLPMQAPELAVKEMERCVKELGFPGVQIGTHVNEWDLNAQELFPVYAAAERLKCSLFVHPWDMQMDGRMAKYWLPWLVGMPAETTIAICSMIMGGVFEKFPKLKVCFAHGGGAFPFTVGRISHGFSMRPDLCAQDNPMNPKKYLGSFYTDALVHDPLSLKLLTDVIGKDKVILGTDYPFPLGELEPGKLIESMEEFDEETKNKLKAGNALAFLGLERKQFE 7PWY,2WM1,4OFC,4IH3,4IGM 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase ACMSD_HUMAN Q8TDX5 Q3B7X3 Q53SR5 Q96KY2 858629 c1cc(cc(c1)CSC2=NC(=C(C(=O)N2)C#N)c3cccs3)CC(=O)O InChI=1S/C18H13N3O3S2/c19-9-13-16(14-5-2-6-25-14)20-18(21-17(13)24)26-10-12-4-1-3-11(7-12)8-15(22)23/h1-7H,8,10H2,(H,22,23)(H,20,21,24) RJQYGCGMQYVVIB-UHFFFAOYSA-N 261607 US9708272, 18::US10513499, Compound 18::US11254644, Compound 18 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase Homo sapiens 10.00 US Patent 10.7270/Q2H41TTQ aid1804077 US10513499 Pellicciari, R; Auwerx, J; Raffaelli, N 12/24/2019 10/24/2020 Tes Pharma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=261607 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=415&target=2-amino-3-carboxymuconate-6-semialdehyde+decarboxylase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=261607&enzyme=2-amino-3-carboxymuconate-6-semialdehyde+decarboxylase&column=ki&startPg=0&Increment=50&submit=Search 8EK 7PWY 134823475 376223449 1 MKIDIHSHILPKEWPDLKKRFGYGGWVQLQHHSKGEAKLLKDGKVFRVVRENCWDPEVRIREMDQKGVTVQALSTVPVMFSYWAKPEDTLNLCQLLNNDLASTVVSYPRRFVGLGTLPMQAPELAVKEMERCVKELGFPGVQIGTHVNEWDLNAQELFPVYAAAERLKCSLFVHPWDMQMDGRMAKYWLPWLVGMPAETTIAICSMIMGGVFEKFPKLKVCFAHGGGAFPFTVGRISHGFSMRPDLCAQDNPMNPKKYLGSFYTDALVHDPLSLKLLTDVIGKDKVILGTDYPFPLGELEPGKLIESMEEFDEETKNKLKAGNALAFLGLERKQFE 7PWY,2WM1,4OFC,4IH3,4IGM 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase ACMSD_HUMAN Q8TDX5 Q3B7X3 Q53SR5 Q96KY2 1141319 c1cc(cc(c1)CSC2=NC(=C(C(=O)N2)C#N)c3cccs3)CC(=O)O InChI=1S/C18H13N3O3S2/c19-9-13-16(14-5-2-6-25-14)20-18(21-17(13)24)26-10-12-4-1-3-11(7-12)8-15(22)23/h1-7H,8,10H2,(H,22,23)(H,20,21,24) RJQYGCGMQYVVIB-UHFFFAOYSA-N 261607 US9708272, 18::US10513499, Compound 18::US11254644, Compound 18 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase Homo sapiens 10.00 US Patent 10.7270/Q2H1356H aid1806358 US11254644 Pellicciari, R; Auwerx, J; Raffaelli, N 2/22/2022 6/17/2022 Tes Pharma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=261607 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=415&target=2-amino-3-carboxymuconate-6-semialdehyde+decarboxylase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=261607&enzyme=2-amino-3-carboxymuconate-6-semialdehyde+decarboxylase&column=ki&startPg=0&Increment=50&submit=Search 8EK 7PWY 134823475 376223449 1 MKIDIHSHILPKEWPDLKKRFGYGGWVQLQHHSKGEAKLLKDGKVFRVVRENCWDPEVRIREMDQKGVTVQALSTVPVMFSYWAKPEDTLNLCQLLNNDLASTVVSYPRRFVGLGTLPMQAPELAVKEMERCVKELGFPGVQIGTHVNEWDLNAQELFPVYAAAERLKCSLFVHPWDMQMDGRMAKYWLPWLVGMPAETTIAICSMIMGGVFEKFPKLKVCFAHGGGAFPFTVGRISHGFSMRPDLCAQDNPMNPKKYLGSFYTDALVHDPLSLKLLTDVIGKDKVILGTDYPFPLGELEPGKLIESMEEFDEETKNKLKAGNALAFLGLERKQFE 7PWY,2WM1,4OFC,4IH3,4IGM 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase ACMSD_HUMAN Q8TDX5 Q3B7X3 Q53SR5 Q96KY2 50771517 c1cc(cc(c1)CSC2=NC(=C(C(=O)N2)C#N)c3cccs3)CC(=O)O InChI=1S/C18H13N3O3S2/c19-9-13-16(14-5-2-6-25-14)20-18(21-17(13)24)26-10-12-4-1-3-11(7-12)8-15(22)23/h1-7H,8,10H2,(H,22,23)(H,20,21,24) RJQYGCGMQYVVIB-UHFFFAOYSA-N 261607 US9708272, 18::US10513499, Compound 18::US11254644, Compound 18 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase Homo sapiens 13 ChEMBL 10.1021/acs.jmedchem.7b01254 10.7270/Q22J6F80 29345930 Pellicciari, R; Liscio, P; Giacchè, N; De Franco, F; Carotti, A; Robertson, J; Cialabrini, L; Katsyuba, E; Raffaelli, N; Auwerx, J 2/8/2018 11/3/2019 Tes Pharma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=261607 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=415&target=2-amino-3-carboxymuconate-6-semialdehyde+decarboxylase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=261607&enzyme=2-amino-3-carboxymuconate-6-semialdehyde+decarboxylase&column=ki&startPg=0&Increment=50&submit=Search 8EK 7PWY 134823475 376223449 1 MKIDIHSHILPKEWPDLKKRFGYGGWVQLQHHSKGEAKLLKDGKVFRVVRENCWDPEVRIREMDQKGVTVQALSTVPVMFSYWAKPEDTLNLCQLLNNDLASTVVSYPRRFVGLGTLPMQAPELAVKEMERCVKELGFPGVQIGTHVNEWDLNAQELFPVYAAAERLKCSLFVHPWDMQMDGRMAKYWLPWLVGMPAETTIAICSMIMGGVFEKFPKLKVCFAHGGGAFPFTVGRISHGFSMRPDLCAQDNPMNPKKYLGSFYTDALVHDPLSLKLLTDVIGKDKVILGTDYPFPLGELEPGKLIESMEEFDEETKNKLKAGNALAFLGLERKQFE 7PWY,2WM1,4OFC,4IH3,4IGM 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase ACMSD_HUMAN Q8TDX5 Q3B7X3 Q53SR5 Q96KY2 50502206 Nc1nc2[nH]c(SCC(=O)c3ccc(Br)cc3)nc2c(=O)[nH]1 InChI=1S/C13H10BrN5O2S/c14-7-3-1-6(2-4-7)8(20)5-22-13-16-9-10(18-13)17-12(15)19-11(9)21/h1-4H,5H2,(H4,15,16,17,18,19,21) NIDWVLLSHNTXJV-UHFFFAOYSA-N 50181848 CHEMBL3818894 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase Escherichia coli (strain K12) 700 ChEMBL 10.1021/acs.jmedchem.6b00002 10.7270/Q2057HWV 27094768 Dennis, ML; Pitcher, NP; Lee, MD; DeBono, AJ; Wang, ZC; Harjani, JR; Rahmani, R; Cleary, B; Peat, TS; Baell, JB; Swarbrick, JD 6/10/2016 9/24/2017 Monash University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50181848 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50007127&target=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine+pyrophosphokinase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50181848&enzyme=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine+pyrophosphokinase&column=ki&startPg=0&Increment=50&submit=Search 5RZ 5ETP,5ETV 118988417 346549916 CHEMBL3818894 1 MTVAYIAIGSNLASPLEQVNAALKALGDIPESHILTVSSFYRTPPLGPQDQPDYLNAAVALETSLAPEELLNHTQRIELQQGRVRKAERWGPRTLDLDIMLFGNEVINTERLTVPHYDMKNRGFMLWPLFEIAPELVFPDGEMLRQILHTRAFDKLNKW 5ETP,5ETO,5ETN,5ETM,5ETL,5ETK,8SIF,4M5N,4M5M,4M5L,4M5K,4M5J,4M5I,4M5H,4M5G,7KDR,7KDO,6AN6,6AN4,4F7V,3UDV,3UDE,3UD5,3IP0,2F65,2F63,1RB0,1RAO,1Q0N,1HKA,1EX8,1EQM,1EQ0,1DY3 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase HPPK_ECOLI P26281 50502212 N#Cc1ccc(CSc2nc3c(=O)[nH]c(N)nc3[nH]2)c(F)c1 InChI=1S/C13H9FN6OS/c14-8-3-6(4-15)1-2-7(8)5-22-13-17-9-10(19-13)18-12(16)20-11(9)21/h1-3H,5H2,(H4,16,17,18,19,20,21) GEUVDHJEINQZML-UHFFFAOYSA-N 50181523 CHEMBL3819281 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase Escherichia coli (strain K12) 2700 ChEMBL 10.1021/acs.jmedchem.6b00002 10.7270/Q2057HWV 27094768 Dennis, ML; Pitcher, NP; Lee, MD; DeBono, AJ; Wang, ZC; Harjani, JR; Rahmani, R; Cleary, B; Peat, TS; Baell, JB; Swarbrick, JD 6/10/2016 9/24/2017 Monash University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50181523 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50007127&target=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine+pyrophosphokinase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50181523&enzyme=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine+pyrophosphokinase&column=ki&startPg=0&Increment=50&submit=Search 5RY 5ETO,5ETT 118988416 104066361 CHEMBL3819281 1 MTVAYIAIGSNLASPLEQVNAALKALGDIPESHILTVSSFYRTPPLGPQDQPDYLNAAVALETSLAPEELLNHTQRIELQQGRVRKAERWGPRTLDLDIMLFGNEVINTERLTVPHYDMKNRGFMLWPLFEIAPELVFPDGEMLRQILHTRAFDKLNKW 5ETP,5ETO,5ETN,5ETM,5ETL,5ETK,8SIF,4M5N,4M5M,4M5L,4M5K,4M5J,4M5I,4M5H,4M5G,7KDR,7KDO,6AN6,6AN4,4F7V,3UDV,3UDE,3UD5,3IP0,2F65,2F63,1RB0,1RAO,1Q0N,1HKA,1EX8,1EQM,1EQ0,1DY3 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase HPPK_ECOLI P26281 51209593 Cc1ccccc1C(=O)CSc1nc2nc(N)[nH]c(=O)c2[nH]1 InChI=1S/C14H13N5O2S/c1-7-4-2-3-5-8(7)9(20)6-22-14-16-10-11(18-14)17-13(15)19-12(10)21/h2-5H,6H2,1H3,(H4,15,16,17,18,19,21) YXZULINHSYINAQ-UHFFFAOYSA-N 50497026 CHEMBL3233209 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase Escherichia coli (strain K12) 18900 ChEMBL 10.1016/j.bmc.2014.02.022 10.7270/Q2ST7SSH 24613625 Yun, MK; Hoagland, D; Kumar, G; Waddell, MB; Rock, CO; Lee, RE; White, SW 4/1/2014 9/2/2020 St. Jude Children'S Research Hospital http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50497026 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50007127&target=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine+pyrophosphokinase&column=ki&startPg=0&Increment=50&submit=Search 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K12) 243000 ChEMBL 10.1016/j.bmc.2014.02.022 10.7270/Q2ST7SSH 24613625 Yun, MK; Hoagland, D; Kumar, G; Waddell, MB; Rock, CO; Lee, RE; White, SW 4/1/2014 9/2/2020 St. Jude Children'S Research Hospital http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50497026 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50007127&target=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine+pyrophosphokinase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50497026&enzyme=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine+pyrophosphokinase&column=ki&startPg=0&Increment=50&submit=Search YH4 4M5L 135566868 433964291 1 MTVAYIAIGSNLASPLEQVNAALKALGDIPESHILTVSSFYRTPPLGPQDQPDYLNAAVALETSLAPEELLNHTQRIELQQGRVRKAERWGPRTLDLDIMLFGNEVINTERLTVPHYDMKNRGFMLWPLFEIAPELVFPDGEMLRQILHTRAFDKLNKW 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http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50007127&target=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine+pyrophosphokinase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50484526&enzyme=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine+pyrophosphokinase&column=ki&startPg=0&Increment=50&submit=Search J1A 3UD5 135566603 433951791 1 MTVAYIAIGSNLASPLEQVNAALKALGDIPESHILTVSSFYRTPPLGPQDQPDYLNAAVALETSLAPEELLNHTQRIELQQGRVRKAERWGPRTLDLDIMLFGNEVINTERLTVPHYDMKNRGFMLWPLFEIAPELVFPDGEMLRQILHTRAFDKLNKW 5ETP,5ETO,5ETN,5ETM,5ETL,5ETK,8SIF,4M5N,4M5M,4M5L,4M5K,4M5J,4M5I,4M5H,4M5G,7KDR,7KDO,6AN6,6AN4,4F7V,3UDV,3UDE,3UD5,3IP0,2F65,2F63,1RB0,1RAO,1Q0N,1HKA,1EX8,1EQM,1EQ0,1DY3 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase HPPK_ECOLI P26281 51178726 c1c(nc2c(n1)N=C(NC2=O)N)CNCCN3CCC(CC3)SC[C@@H]4[C@H]([C@H]([C@@H](O4)n5cnc6c5ncnc6N)O)O InChI=1S/C24H32N12O4S/c25-19-15-21(30-10-29-19)36(11-31-15)23-18(38)17(37)14(40-23)9-41-13-1-4-35(5-2-13)6-3-27-7-12-8-28-20-16(32-12)22(39)34-24(26)33-20/h8,10-11,13-14,17-18,23,27,37-38H,1-7,9H2,(H2,25,29,30)(H3,26,28,33,34,39) KWIHONXLDHOYOZ-UHFFFAOYSA-N 50484526 CHEMBL1928284 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase Escherichia coli (strain K12) >100000 ChEMBL 10.1016/j.bmc.2011.11.032 10.7270/Q2HX1GJX 22169600 Shi, G; Shaw, G; Liang, YH; Subburaman, P; Li, Y; Wu, Y; Yan, H; Ji, X 1/1/2012 8/29/2020 National Cancer Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50484526 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50007127&target=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine+pyrophosphokinase&column=ki&startPg=0&Increment=50&submit=Search 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InChI=1S/C26H36N12O5S/c1-26(2)18(33-15-20(36-26)34-25(28)35-22(15)41)23(42)29-5-8-37-6-3-12(4-7-37)44-9-13-16(39)17(40)24(43-13)38-11-32-14-19(27)30-10-31-21(14)38/h10-13,16-17,24,39-40H,3-9H2,1-2H3,(H,29,42)(H2,27,30,31)(H4,28,34,35,36,41) LXHMIPYFQUZUMS-UHFFFAOYSA-N 50484528 CHEMBL1928285 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase Escherichia coli (strain K12) 2550 ChEMBL 10.1016/j.bmc.2011.11.032 10.7270/Q2HX1GJX 22169600 Shi, G; Shaw, G; Liang, YH; Subburaman, P; Li, Y; Wu, Y; Yan, H; Ji, X 1/1/2012 8/29/2020 National Cancer Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50484528 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50007127&target=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine+pyrophosphokinase&column=ki&startPg=0&Increment=50&submit=Search 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InChI=1S/C26H36N12O5S/c1-26(2)18(33-15-20(36-26)34-25(28)35-22(15)41)23(42)29-5-8-37-6-3-12(4-7-37)44-9-13-16(39)17(40)24(43-13)38-11-32-14-19(27)30-10-31-21(14)38/h10-13,16-17,24,39-40H,3-9H2,1-2H3,(H,29,42)(H2,27,30,31)(H4,28,34,35,36,41) LXHMIPYFQUZUMS-UHFFFAOYSA-N 50484528 CHEMBL1928285 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase Escherichia coli (strain K12) 3160 ChEMBL 10.1016/j.bmc.2011.11.032 10.7270/Q2HX1GJX 22169600 Shi, G; Shaw, G; Liang, YH; Subburaman, P; Li, Y; Wu, Y; Yan, H; Ji, X 1/1/2012 8/29/2020 National Cancer Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50484528 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50007127&target=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine+pyrophosphokinase&column=ki&startPg=0&Increment=50&submit=Search 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InChI=1S/C26H36N12O5S/c1-26(2)18(33-15-20(36-26)34-25(28)35-22(15)41)23(42)29-5-8-37-6-3-12(4-7-37)44-9-13-16(39)17(40)24(43-13)38-11-32-14-19(27)30-10-31-21(14)38/h10-13,16-17,24,39-40H,3-9H2,1-2H3,(H,29,42)(H2,27,30,31)(H4,28,34,35,36,41) LXHMIPYFQUZUMS-UHFFFAOYSA-N 50484528 CHEMBL1928285 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase Escherichia coli (strain K12) 2550 ChEMBL 10.1016/j.bmc.2012.05.060 10.7270/Q2HM5CBD 22727779 Shi, G; Shaw, G; Li, Y; Wu, Y; Yan, H; Ji, X 7/15/2012 8/29/2020 National Cancer Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50484528 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50007127&target=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine+pyrophosphokinase&column=ki&startPg=0&Increment=50&submit=Search 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InChI=1S/C26H36N12O5S/c1-26(2)18(33-15-20(36-26)34-25(28)35-22(15)41)23(42)29-5-8-37-6-3-12(4-7-37)44-9-13-16(39)17(40)24(43-13)38-11-32-14-19(27)30-10-31-21(14)38/h10-13,16-17,24,39-40H,3-9H2,1-2H3,(H,29,42)(H2,27,30,31)(H4,28,34,35,36,41) LXHMIPYFQUZUMS-UHFFFAOYSA-N 50484528 CHEMBL1928285 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase Escherichia coli (strain K12) 3160 ChEMBL 10.1016/j.bmc.2012.05.060 10.7270/Q2HM5CBD 22727779 Shi, G; Shaw, G; Li, Y; Wu, Y; Yan, H; Ji, X 7/15/2012 8/29/2020 National Cancer Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50484528 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50007127&target=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine+pyrophosphokinase&column=ki&startPg=0&Increment=50&submit=Search 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InChI=1S/C23H30N12O8S/c1-23(2)15(31-12-17(34-23)32-22(25)33-19(12)39)20(40)27-5-10(36)26-3-4-44(41,42)6-9-13(37)14(38)21(43-9)35-8-30-11-16(24)28-7-29-18(11)35/h7-9,13-14,21,37-38H,3-6H2,1-2H3,(H,26,36)(H,27,40)(H2,24,28,29)(H4,25,32,33,34,39) QCWCABDSXQYDST-UHFFFAOYSA-N 50485340 CHEMBL2046607 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase Escherichia coli (strain K12) 9530 ChEMBL 10.1016/j.bmc.2012.05.060 10.7270/Q2HM5CBD 22727779 Shi, G; Shaw, G; Li, Y; Wu, Y; Yan, H; Ji, X 7/15/2012 8/29/2020 National Cancer Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50485340 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50007127&target=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine+pyrophosphokinase&column=ki&startPg=0&Increment=50&submit=Search 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InChI=1S/C23H30N12O8S/c1-23(2)15(31-12-17(34-23)32-22(25)33-19(12)39)20(40)27-5-10(36)26-3-4-44(41,42)6-9-13(37)14(38)21(43-9)35-8-30-11-16(24)28-7-29-18(11)35/h7-9,13-14,21,37-38H,3-6H2,1-2H3,(H,26,36)(H,27,40)(H2,24,28,29)(H4,25,32,33,34,39) QCWCABDSXQYDST-UHFFFAOYSA-N 50485340 CHEMBL2046607 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase Escherichia coli (strain K12) 4160 ChEMBL 10.1016/j.bmc.2012.05.060 10.7270/Q2HM5CBD 22727779 Shi, G; Shaw, G; Li, Y; Wu, Y; Yan, H; Ji, X 7/15/2012 8/29/2020 National Cancer Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50485340 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50007127&target=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine+pyrophosphokinase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50485340&enzyme=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine+pyrophosphokinase&column=ki&startPg=0&Increment=50&submit=Search J1D 4F7V,4PZV 136266900 433952605 1 MTVAYIAIGSNLASPLEQVNAALKALGDIPESHILTVSSFYRTPPLGPQDQPDYLNAAVALETSLAPEELLNHTQRIELQQGRVRKAERWGPRTLDLDIMLFGNEVINTERLTVPHYDMKNRGFMLWPLFEIAPELVFPDGEMLRQILHTRAFDKLNKW 5ETP,5ETO,5ETN,5ETM,5ETL,5ETK,8SIF,4M5N,4M5M,4M5L,4M5K,4M5J,4M5I,4M5H,4M5G,7KDR,7KDO,6AN6,6AN4,4F7V,3UDV,3UDE,3UD5,3IP0,2F65,2F63,1RB0,1RAO,1Q0N,1HKA,1EX8,1EQM,1EQ0,1DY3 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase HPPK_ECOLI P26281 51209604 Cc1ccc(C(=O)CSc2nc3nc(N)[nH]c(=O)c3[nH]2)cc1 InChI=1S/C14H13N5O2S/c1-7-2-4-8(5-3-7)9(20)6-22-14-16-10-11(18-14)17-13(15)19-12(10)21/h2-5H,6H2,1H3,(H4,15,16,17,18,19,21) HIGGTDYQNPXEFT-UHFFFAOYSA-N 50497030 CHEMBL3233203 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase Escherichia coli (strain K12) 64000 ChEMBL 10.1016/j.bmc.2014.02.022 10.7270/Q2ST7SSH 24613625 Yun, MK; Hoagland, D; Kumar, G; Waddell, MB; Rock, CO; Lee, RE; White, SW 4/1/2014 9/2/2020 St. Jude Children'S Research Hospital http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50497030 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50007127&target=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine+pyrophosphokinase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50497030&enzyme=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine+pyrophosphokinase&column=ki&startPg=0&Increment=50&submit=Search YH6 4M5I 135548073 433964295 1 MTVAYIAIGSNLASPLEQVNAALKALGDIPESHILTVSSFYRTPPLGPQDQPDYLNAAVALETSLAPEELLNHTQRIELQQGRVRKAERWGPRTLDLDIMLFGNEVINTERLTVPHYDMKNRGFMLWPLFEIAPELVFPDGEMLRQILHTRAFDKLNKW 5ETP,5ETO,5ETN,5ETM,5ETL,5ETK,8SIF,4M5N,4M5M,4M5L,4M5K,4M5J,4M5I,4M5H,4M5G,7KDR,7KDO,6AN6,6AN4,4F7V,3UDV,3UDE,3UD5,3IP0,2F65,2F63,1RB0,1RAO,1Q0N,1HKA,1EX8,1EQM,1EQ0,1DY3 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase HPPK_ECOLI P26281 51209611 Cc1ccc(C(=O)CSc2nc3nc(N)[nH]c(=O)c3[nH]2)cc1 InChI=1S/C14H13N5O2S/c1-7-2-4-8(5-3-7)9(20)6-22-14-16-10-11(18-14)17-13(15)19-12(10)21/h2-5H,6H2,1H3,(H4,15,16,17,18,19,21) HIGGTDYQNPXEFT-UHFFFAOYSA-N 50497030 CHEMBL3233203 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase Escherichia coli (strain K12) 6700 ChEMBL 10.1016/j.bmc.2014.02.022 10.7270/Q2ST7SSH 24613625 Yun, MK; Hoagland, D; Kumar, G; Waddell, MB; Rock, CO; Lee, RE; White, SW 4/1/2014 9/2/2020 St. Jude Children'S Research Hospital http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50497030 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50007127&target=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine+pyrophosphokinase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50497030&enzyme=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine+pyrophosphokinase&column=ki&startPg=0&Increment=50&submit=Search YH6 4M5I 135548073 433964295 1 MTVAYIAIGSNLASPLEQVNAALKALGDIPESHILTVSSFYRTPPLGPQDQPDYLNAAVALETSLAPEELLNHTQRIELQQGRVRKAERWGPRTLDLDIMLFGNEVINTERLTVPHYDMKNRGFMLWPLFEIAPELVFPDGEMLRQILHTRAFDKLNKW 5ETP,5ETO,5ETN,5ETM,5ETL,5ETK,8SIF,4M5N,4M5M,4M5L,4M5K,4M5J,4M5I,4M5H,4M5G,7KDR,7KDO,6AN6,6AN4,4F7V,3UDV,3UDE,3UD5,3IP0,2F65,2F63,1RB0,1RAO,1Q0N,1HKA,1EX8,1EQM,1EQ0,1DY3 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase HPPK_ECOLI P26281 51403498 N[C@@H](Cc1c[nH]c2ccccc12)C(=O)NO InChI=1S/C11H13N3O2/c12-9(11(15)14-16)5-7-6-13-10-4-2-1-3-8(7)10/h1-4,6,9,13,16H,5,12H2,(H,14,15) LBMAEBPZXXNKMZ-UHFFFAOYSA-N 31916 Tryptophanhydroxamate, 13 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase Burkholderia pseudomallei (strain K96243) 36000 ChEMBL 10.1016/j.bmcl.2021.128273 10.7270/Q2VT1WTJ 34298132 Blain, JM; Grote, DL; Watkins, SM; Goshu, GM; Muller, C; Gorman, JL; Ranieri, G; Walter, RL; Hofstetter, H; Horn, JR; Hagen, TJ 9/15/2021 8/19/2022 Northern Illinois University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=31916 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006455&target=2-C-methyl-D-erythritol+2%2C4-cyclodiphosphate+synthase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=31916&enzyme=2-C-methyl-D-erythritol+2%2C4-cyclodiphosphate+synthase&column=ki&startPg=0&Increment=50&submit=Search 6ZB 5L03 667595 85240542 1 MDFRIGQGYDVHQLVPGRPLIIGGVTIPYERGLLGHSDADVLLHAITDALFGAAALGDIGRHFSDTDPRFKGADSRALLRECASRVAQAGFAIRNVDSTIIAQAPKLAPHIDAMRANIAADLDLPLDRVNVKAKTNEKLGYLGRGEGIEAQAAALVVREAAA 6NMO,6V3M,3QHD,3Q8H,3P10,3P0Z,3MBM,3KE1,3K2X,3K14,3JVH,3IEW,3IEQ,3F0G,3F0F,3F0E,3F0D,6MWK,6MWJ,6MWI,6MWF,3IKF,3IKE,5L03,4C8I,4C8G,4C8E 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase ISPF_BURPS Q63T71 51403502 N[C@@H](Cc1c[nH]c2ccccc12)C(=O)NO InChI=1S/C11H13N3O2/c12-9(11(15)14-16)5-7-6-13-10-4-2-1-3-8(7)10/h1-4,6,9,13,16H,5,12H2,(H,14,15) LBMAEBPZXXNKMZ-UHFFFAOYSA-N 31916 Tryptophanhydroxamate, 13 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase Burkholderia pseudomallei (strain K96243) 848000 ChEMBL 10.1016/j.bmcl.2021.128273 10.7270/Q2VT1WTJ 34298132 Blain, JM; Grote, DL; Watkins, SM; Goshu, GM; Muller, C; Gorman, JL; Ranieri, G; Walter, RL; Hofstetter, H; Horn, JR; Hagen, TJ 9/15/2021 8/19/2022 Northern Illinois University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=31916 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006455&target=2-C-methyl-D-erythritol+2%2C4-cyclodiphosphate+synthase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=31916&enzyme=2-C-methyl-D-erythritol+2%2C4-cyclodiphosphate+synthase&column=ki&startPg=0&Increment=50&submit=Search 6ZB 5L03 667595 85240542 1 MDFRIGQGYDVHQLVPGRPLIIGGVTIPYERGLLGHSDADVLLHAITDALFGAAALGDIGRHFSDTDPRFKGADSRALLRECASRVAQAGFAIRNVDSTIIAQAPKLAPHIDAMRANIAADLDLPLDRVNVKAKTNEKLGYLGRGEGIEAQAAALVVREAAA 6NMO,6V3M,3QHD,3Q8H,3P10,3P0Z,3MBM,3KE1,3K2X,3K14,3JVH,3IEW,3IEQ,3F0G,3F0F,3F0E,3F0D,6MWK,6MWJ,6MWI,6MWF,3IKF,3IKE,5L03,4C8I,4C8G,4C8E 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase ISPF_BURPS Q63T71 51403503 N[C@@H](Cc1c[nH]c2ccccc12)C(=O)NO InChI=1S/C11H13N3O2/c12-9(11(15)14-16)5-7-6-13-10-4-2-1-3-8(7)10/h1-4,6,9,13,16H,5,12H2,(H,14,15) LBMAEBPZXXNKMZ-UHFFFAOYSA-N 31916 Tryptophanhydroxamate, 13 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase Burkholderia pseudomallei (strain K96243) 24000 ChEMBL 10.1016/j.bmcl.2021.128273 10.7270/Q2VT1WTJ 34298132 Blain, JM; Grote, DL; Watkins, SM; Goshu, GM; Muller, C; Gorman, JL; Ranieri, G; Walter, RL; Hofstetter, H; Horn, JR; Hagen, TJ 9/15/2021 8/19/2022 Northern Illinois University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=31916 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006455&target=2-C-methyl-D-erythritol+2%2C4-cyclodiphosphate+synthase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=31916&enzyme=2-C-methyl-D-erythritol+2%2C4-cyclodiphosphate+synthase&column=ki&startPg=0&Increment=50&submit=Search 6ZB 5L03 667595 85240542 1 MDFRIGQGYDVHQLVPGRPLIIGGVTIPYERGLLGHSDADVLLHAITDALFGAAALGDIGRHFSDTDPRFKGADSRALLRECASRVAQAGFAIRNVDSTIIAQAPKLAPHIDAMRANIAADLDLPLDRVNVKAKTNEKLGYLGRGEGIEAQAAALVVREAAA 6NMO,6V3M,3QHD,3Q8H,3P10,3P0Z,3MBM,3KE1,3K2X,3K14,3JVH,3IEW,3IEQ,3F0G,3F0F,3F0E,3F0D,6MWK,6MWJ,6MWI,6MWF,3IKF,3IKE,5L03,4C8I,4C8G,4C8E 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase ISPF_BURPS Q63T71 57520 C1=CN(C(=O)N=C1N)[C@H]2[C@H]([C@@H]([C@H](O2)COP(=O)(O)O)O)O InChI=1S/C9H14N3O8P/c10-5-1-2-12(9(15)11-5)8-7(14)6(13)4(20-8)3-19-21(16,17)18/h1-2,4,6-8,13-14H,3H2,(H2,10,11,15)(H2,16,17,18) IERHLVCPSMICTF-UHFFFAOYSA-N 31913 cytidylic acid::1-beta-D-arabinofuranosylcytosine 5-monophosphate::AraCMP 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase Escherichia coli (strain K12) 18910000 7.0000 10.00 C Curated from the literature by BindingDB 10.1021/jm801475n 10.7270/Q23B5XGB 19320487 aid1799187 Ramsden, NL; Buetow, L; Dawson, A; Kemp, LA; Ulaganathan, V; Brenk, R; Klebe, G; Hunter, WN 4/23/2009 9/28/2009 University of Dundee http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=31913 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3977&target=2-C-methyl-D-erythritol+2%2C4-cyclodiphosphate+synthase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=31913&enzyme=2-C-methyl-D-erythritol+2%2C4-cyclodiphosphate+synthase&column=ki&startPg=0&Increment=50&submit=Search CAR 3ERN,6PZ3,1KDR,2KP3,3MDA,1NH3,8V7F,8V7E,8V7K,8V7J,8V7I,8V7H,6Q02,170D,6D0M,6D0Z,1HO6 65177 85240539 1 MRIGHGFDVHAFGGEGPIIIGGVRIPYEKGLLAHSDGDVALHALTDALLGAAALGDIGKLFPDTDPAFKGADSRELLREAWRRIQAKGYTLGNVDVTIIAQAPKMLPHIPQMRVFIAEDLGCHMDDVNVKATTTEKLGFTGRGEGIACEAVALLIKATK 1H48,1H47,1GX1,3FBA,3ESJ,3ERN,3EOR,3ELC,2AMT,1U43,1U40,1U3P,1U3L,1KNK,1KNJ,1JY8,2GZL 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase ISPF_ECOLI P62617 P36663 Q2MA83 51084585 c1csc2n1cc(n2)CO InChI=1S/C6H6N2OS/c9-4-5-3-8-1-2-10-6(8)7-5/h1-3,9H,4H2 GBUTVPCKMACQMG-UHFFFAOYSA-N 50443773 CHEMBL1230528 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase Burkholderia pseudomallei (strain K96243) 135000 ChEMBL 10.1016/j.bmcl.2013.09.101 10.7270/Q2NC62NX 24157367 Zhang, Z; Jakkaraju, S; Blain, J; Gogol, K; Zhao, L; Hartley, RC; Karlsson, CA; Staker, BL; Edwards, TE; Stewart, LJ; Myler, PJ; Clare, M; Begley, DW; Horn, JR; Hagen, TJ 12/2/2013 7/25/2014 Northern Illinois University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50443773 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006455&target=2-C-methyl-D-erythritol+2%2C4-cyclodiphosphate+synthase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50443773&enzyme=2-C-methyl-D-erythritol+2%2C4-cyclodiphosphate+synthase&column=ki&startPg=0&Increment=50&submit=Search 717 3IKF,3MBM 4961267 194941669 CHEMBL1230528 1 MDFRIGQGYDVHQLVPGRPLIIGGVTIPYERGLLGHSDADVLLHAITDALFGAAALGDIGRHFSDTDPRFKGADSRALLRECASRVAQAGFAIRNVDSTIIAQAPKLAPHIDAMRANIAADLDLPLDRVNVKAKTNEKLGYLGRGEGIEAQAAALVVREAAA 6NMO,6V3M,3QHD,3Q8H,3P10,3P0Z,3MBM,3KE1,3K2X,3K14,3JVH,3IEW,3IEQ,3F0G,3F0F,3F0E,3F0D,6MWK,6MWJ,6MWI,6MWF,3IKF,3IKE,5L03,4C8I,4C8G,4C8E 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase ISPF_BURPS Q63T71 51084585 c1csc2n1cc(n2)CO InChI=1S/C6H6N2OS/c9-4-5-3-8-1-2-10-6(8)7-5/h1-3,9H,4H2 GBUTVPCKMACQMG-UHFFFAOYSA-N 50443773 CHEMBL1230528 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase Burkholderia pseudomallei (strain K96243) 135000 ChEMBL 10.1016/j.bmcl.2013.09.101 10.7270/Q2NC62NX 24157367 Zhang, Z; Jakkaraju, S; Blain, J; Gogol, K; Zhao, L; Hartley, RC; Karlsson, CA; Staker, BL; Edwards, TE; Stewart, LJ; Myler, PJ; Clare, M; Begley, DW; Horn, JR; Hagen, TJ 12/2/2013 7/25/2014 Northern Illinois University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50443773 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006455&target=2-C-methyl-D-erythritol+2%2C4-cyclodiphosphate+synthase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50443773&enzyme=2-C-methyl-D-erythritol+2%2C4-cyclodiphosphate+synthase&column=ki&startPg=0&Increment=50&submit=Search 717 3IKF,3MBM 4961267 194941669 CHEMBL1230528 1 MDFRIGQGYDVHQLVPGRPLIIGGVTIPYERGLLGHSDADVLLHAITDALFGAAALGDIGRHFSDTDPRFKGADSRALLRECASRVAQAGFAIRNVDSTIIAQAPKLAPHIDAMRANIAADLDLPLDRVNVKAKTNEKLGYLGRGEGIEAQAAALVVREAAA 6NMO,6V3M,3QHD,3Q8H,3P10,3P0Z,3MBM,3KE1,3K2X,3K14,3JVH,3IEW,3IEQ,3F0G,3F0F,3F0E,3F0D,6MWK,6MWJ,6MWI,6MWF,3IKF,3IKE,5L03,4C8I,4C8G,4C8E 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase ISPF_BURPS Q63T71 47450 c1cnc(cc1C(=O)O)C(=O)O InChI=1S/C7H5NO4/c9-6(10)4-1-2-8-5(3-4)7(11)12/h1-3H,(H,9,10)(H,11,12) MJIVRKPEXXHNJT-UHFFFAOYSA-N 26113 pyridine-2,4-dicarboxylic acid::cid_10365::pyridine carboxylate, 6a::2,4 PDCA Lysine-specific demethylase 4E Homo sapiens 1400 7.5000 37.00 C Curated from the literature by BindingDB 10.1021/jm800936s 10.7270/Q2959FV4 18942826 aid1798635 Rose, NR; Ng, SS; Mecinovic;, J; Liénard, MR; Bello, SH; Sun, Z; McDonough, MA; Oppermann, U; Schofield, CJ 10/23/2008 12/18/2008 University of Oxford http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=26113 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2963&target=Lysine-specific+demethylase+4E&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=26113&enzyme=Lysine-specific+demethylase+4E&column=ki&startPg=0&Increment=50&submit=Search PD2 2GKL,2JIG,2VD7,2W0X,2W2I,4D6Q,4DIQ,4IE0,4LXL,4NHK,4NHY,4NRQ,5A3W,5JTC,6I9L,7YXJ,9QN0 10365 56464550 1 MKSVHSSPQNTSHTIMTFYPTMEEFADFNTYVAYMESQGAHQAGLAKVIPPKEWKARQMYDDIEDILIATPLQQVTSGQGGVFTQYHKKKKAMRVGQYRRLANSKKYQTPPHQNFADLEQRYWKSHPGNPPIYGADISGSLFEESTKQWNLGHLGTILDLLEQECGVVIEGVNTPYLYFGMWKTTFAWHTEDMDLYSINYLHFGEPKTWYVVPPEHGQHLERLARELFPDISRGCEAFLRHKVALISPTVLKENGIPFNCMTQEAGEFMVTFPYGYHAGFNHGFNCAEAINFATPRWIDYGKMASQCSCGESTVTFSMDPFVRIVQPESYELWKHRQDLAIVEHTEPRVAESQELSNWRDDIVLRRAALGLRLLPNLTAQCPTQPVSSGHCYNPKGCGTDAVPGSAFQSSAYHTQTQSLTLGMSARVLLPSTGSWGSGRGRGRGQGQGRGCSRGRGHGCCTRELGTEEPTVQPASKRRLLMGTRSRAQGHRPQLPLANDLMTNLSL 2W2I Lysine-specific demethylase 4E KDM4E_HUMAN B2RXH2 50646281 c1cnc(cc1C(=O)O)C(=O)O InChI=1S/C7H5NO4/c9-6(10)4-1-2-8-5(3-4)7(11)12/h1-3H,(H,9,10)(H,11,12) MJIVRKPEXXHNJT-UHFFFAOYSA-N 26113 pyridine-2,4-dicarboxylic acid::cid_10365::pyridine carboxylate, 6a::2,4 PDCA Lysine-specific demethylase 4E Homo sapiens 914000 ChEMBL 10.1016/j.bmc.2011.01.046 10.7270/Q23X870S 21596573 Lohse, B; Kristensen, JL; Kristensen, LH; Agger, K; Helin, K; Gajhede, M; Clausen, RP 6/13/2011 3/23/2012 University of Copenhagen http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=26113 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2963&target=Lysine-specific+demethylase+4E&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=26113&enzyme=Lysine-specific+demethylase+4E&column=ki&startPg=0&Increment=50&submit=Search PD2 2GKL,2JIG,2VD7,2W0X,2W2I,4D6Q,4DIQ,4IE0,4LXL,4NHK,4NHY,4NRQ,5A3W,5JTC,6I9L,7YXJ,9QN0 10365 56464550 1 MKSVHSSPQNTSHTIMTFYPTMEEFADFNTYVAYMESQGAHQAGLAKVIPPKEWKARQMYDDIEDILIATPLQQVTSGQGGVFTQYHKKKKAMRVGQYRRLANSKKYQTPPHQNFADLEQRYWKSHPGNPPIYGADISGSLFEESTKQWNLGHLGTILDLLEQECGVVIEGVNTPYLYFGMWKTTFAWHTEDMDLYSINYLHFGEPKTWYVVPPEHGQHLERLARELFPDISRGCEAFLRHKVALISPTVLKENGIPFNCMTQEAGEFMVTFPYGYHAGFNHGFNCAEAINFATPRWIDYGKMASQCSCGESTVTFSMDPFVRIVQPESYELWKHRQDLAIVEHTEPRVAESQELSNWRDDIVLRRAALGLRLLPNLTAQCPTQPVSSGHCYNPKGCGTDAVPGSAFQSSAYHTQTQSLTLGMSARVLLPSTGSWGSGRGRGRGQGQGRGCSRGRGHGCCTRELGTEEPTVQPASKRRLLMGTRSRAQGHRPQLPLANDLMTNLSL 2W2I Lysine-specific demethylase 4E KDM4E_HUMAN B2RXH2 51213147 c1cnc(cc1C(=O)O)C(=O)O InChI=1S/C7H5NO4/c9-6(10)4-1-2-8-5(3-4)7(11)12/h1-3H,(H,9,10)(H,11,12) MJIVRKPEXXHNJT-UHFFFAOYSA-N 26113 pyridine-2,4-dicarboxylic acid::cid_10365::pyridine carboxylate, 6a::2,4 PDCA Lysine-specific demethylase 4E Homo sapiens 6310 ChEMBL 10.1039/C4MD00291A 10.7270/Q2KH0RBN 26682034 England, KS; Tumber, A; Krojer, T; Scozzafava, G; Ng, SS; Daniel, M; Szykowska, A; Che, K; von Delft, F; Burgess-Brown, NA; Kawamura, A; Schofield, CJ; Brennan, PE 12/1/2014 9/3/2020 University of Oxford http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=26113 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2963&target=Lysine-specific+demethylase+4E&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=26113&enzyme=Lysine-specific+demethylase+4E&column=ki&startPg=0&Increment=50&submit=Search PD2 2GKL,2JIG,2VD7,2W0X,2W2I,4D6Q,4DIQ,4IE0,4LXL,4NHK,4NHY,4NRQ,5A3W,5JTC,6I9L,7YXJ,9QN0 10365 56464550 1 MKSVHSSPQNTSHTIMTFYPTMEEFADFNTYVAYMESQGAHQAGLAKVIPPKEWKARQMYDDIEDILIATPLQQVTSGQGGVFTQYHKKKKAMRVGQYRRLANSKKYQTPPHQNFADLEQRYWKSHPGNPPIYGADISGSLFEESTKQWNLGHLGTILDLLEQECGVVIEGVNTPYLYFGMWKTTFAWHTEDMDLYSINYLHFGEPKTWYVVPPEHGQHLERLARELFPDISRGCEAFLRHKVALISPTVLKENGIPFNCMTQEAGEFMVTFPYGYHAGFNHGFNCAEAINFATPRWIDYGKMASQCSCGESTVTFSMDPFVRIVQPESYELWKHRQDLAIVEHTEPRVAESQELSNWRDDIVLRRAALGLRLLPNLTAQCPTQPVSSGHCYNPKGCGTDAVPGSAFQSSAYHTQTQSLTLGMSARVLLPSTGSWGSGRGRGRGQGQGRGCSRGRGHGCCTRELGTEEPTVQPASKRRLLMGTRSRAQGHRPQLPLANDLMTNLSL 2W2I Lysine-specific demethylase 4E KDM4E_HUMAN B2RXH2 51508427 c1cnc(cc1C(=O)O)C(=O)O InChI=1S/C7H5NO4/c9-6(10)4-1-2-8-5(3-4)7(11)12/h1-3H,(H,9,10)(H,11,12) MJIVRKPEXXHNJT-UHFFFAOYSA-N 26113 pyridine-2,4-dicarboxylic acid::cid_10365::pyridine carboxylate, 6a::2,4 PDCA Lysine-specific demethylase 4E Homo sapiens 4700 ChEMBL 10.7270/Q2J107CR 34792334 Perry, GS; Das, M; Woon, ECY 12/9/2021 4/19/2024 University College London http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=26113 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2963&target=Lysine-specific+demethylase+4E&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=26113&enzyme=Lysine-specific+demethylase+4E&column=ki&startPg=0&Increment=50&submit=Search PD2 2GKL,2JIG,2VD7,2W0X,2W2I,4D6Q,4DIQ,4IE0,4LXL,4NHK,4NHY,4NRQ,5A3W,5JTC,6I9L,7YXJ,9QN0 10365 56464550 1 MKSVHSSPQNTSHTIMTFYPTMEEFADFNTYVAYMESQGAHQAGLAKVIPPKEWKARQMYDDIEDILIATPLQQVTSGQGGVFTQYHKKKKAMRVGQYRRLANSKKYQTPPHQNFADLEQRYWKSHPGNPPIYGADISGSLFEESTKQWNLGHLGTILDLLEQECGVVIEGVNTPYLYFGMWKTTFAWHTEDMDLYSINYLHFGEPKTWYVVPPEHGQHLERLARELFPDISRGCEAFLRHKVALISPTVLKENGIPFNCMTQEAGEFMVTFPYGYHAGFNHGFNCAEAINFATPRWIDYGKMASQCSCGESTVTFSMDPFVRIVQPESYELWKHRQDLAIVEHTEPRVAESQELSNWRDDIVLRRAALGLRLLPNLTAQCPTQPVSSGHCYNPKGCGTDAVPGSAFQSSAYHTQTQSLTLGMSARVLLPSTGSWGSGRGRGRGQGQGRGCSRGRGHGCCTRELGTEEPTVQPASKRRLLMGTRSRAQGHRPQLPLANDLMTNLSL 2W2I Lysine-specific demethylase 4E KDM4E_HUMAN B2RXH2 51513909 c1cnc(cc1C(=O)O)C(=O)O InChI=1S/C7H5NO4/c9-6(10)4-1-2-8-5(3-4)7(11)12/h1-3H,(H,9,10)(H,11,12) MJIVRKPEXXHNJT-UHFFFAOYSA-N 26113 pyridine-2,4-dicarboxylic acid::cid_10365::pyridine carboxylate, 6a::2,4 PDCA Lysine-specific demethylase 4E Homo sapiens 3000 ChEMBL 10.7270/Q2N01BRW 34555614 Yang, GJ; Wu, J; Miao, L; Zhu, MH; Zhou, QJ; Lu, XJ; Lu, JF; Leung, CH; Ma, DL; Chen, J 12/15/2021 4/20/2024 Ningbo University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=26113 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2963&target=Lysine-specific+demethylase+4E&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=26113&enzyme=Lysine-specific+demethylase+4E&column=ki&startPg=0&Increment=50&submit=Search PD2 2GKL,2JIG,2VD7,2W0X,2W2I,4D6Q,4DIQ,4IE0,4LXL,4NHK,4NHY,4NRQ,5A3W,5JTC,6I9L,7YXJ,9QN0 10365 56464550 1 MKSVHSSPQNTSHTIMTFYPTMEEFADFNTYVAYMESQGAHQAGLAKVIPPKEWKARQMYDDIEDILIATPLQQVTSGQGGVFTQYHKKKKAMRVGQYRRLANSKKYQTPPHQNFADLEQRYWKSHPGNPPIYGADISGSLFEESTKQWNLGHLGTILDLLEQECGVVIEGVNTPYLYFGMWKTTFAWHTEDMDLYSINYLHFGEPKTWYVVPPEHGQHLERLARELFPDISRGCEAFLRHKVALISPTVLKENGIPFNCMTQEAGEFMVTFPYGYHAGFNHGFNCAEAINFATPRWIDYGKMASQCSCGESTVTFSMDPFVRIVQPESYELWKHRQDLAIVEHTEPRVAESQELSNWRDDIVLRRAALGLRLLPNLTAQCPTQPVSSGHCYNPKGCGTDAVPGSAFQSSAYHTQTQSLTLGMSARVLLPSTGSWGSGRGRGRGQGQGRGCSRGRGHGCCTRELGTEEPTVQPASKRRLLMGTRSRAQGHRPQLPLANDLMTNLSL 2W2I Lysine-specific demethylase 4E KDM4E_HUMAN B2RXH2 51561555 c1cnc(cc1C(=O)O)C(=O)O InChI=1S/C7H5NO4/c9-6(10)4-1-2-8-5(3-4)7(11)12/h1-3H,(H,9,10)(H,11,12) MJIVRKPEXXHNJT-UHFFFAOYSA-N 26113 pyridine-2,4-dicarboxylic acid::cid_10365::pyridine carboxylate, 6a::2,4 PDCA Lysine-specific demethylase 4E Homo sapiens 300 ChEMBL 10.7270/Q21Z48T5 37527664 Brewitz, L; Nakashima, Y; Piasecka, SK; Salah, E; Fletcher, SC; Tumber, A; Corner, TP; Kennedy, TJ; Fiorini, G; Thalhammer, A; Christensen, KE; Coleman, ML; Schofield, CJ 8/10/2023 12/19/2024 University of Oxford http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=26113 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2963&target=Lysine-specific+demethylase+4E&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=26113&enzyme=Lysine-specific+demethylase+4E&column=ki&startPg=0&Increment=50&submit=Search PD2 2GKL,2JIG,2VD7,2W0X,2W2I,4D6Q,4DIQ,4IE0,4LXL,4NHK,4NHY,4NRQ,5A3W,5JTC,6I9L,7YXJ,9QN0 10365 56464550 1 MKSVHSSPQNTSHTIMTFYPTMEEFADFNTYVAYMESQGAHQAGLAKVIPPKEWKARQMYDDIEDILIATPLQQVTSGQGGVFTQYHKKKKAMRVGQYRRLANSKKYQTPPHQNFADLEQRYWKSHPGNPPIYGADISGSLFEESTKQWNLGHLGTILDLLEQECGVVIEGVNTPYLYFGMWKTTFAWHTEDMDLYSINYLHFGEPKTWYVVPPEHGQHLERLARELFPDISRGCEAFLRHKVALISPTVLKENGIPFNCMTQEAGEFMVTFPYGYHAGFNHGFNCAEAINFATPRWIDYGKMASQCSCGESTVTFSMDPFVRIVQPESYELWKHRQDLAIVEHTEPRVAESQELSNWRDDIVLRRAALGLRLLPNLTAQCPTQPVSSGHCYNPKGCGTDAVPGSAFQSSAYHTQTQSLTLGMSARVLLPSTGSWGSGRGRGRGQGQGRGCSRGRGHGCCTRELGTEEPTVQPASKRRLLMGTRSRAQGHRPQLPLANDLMTNLSL 2W2I Lysine-specific demethylase 4E KDM4E_HUMAN B2RXH2 122677 C[C@H]1C[C@@H](C(=O)[C@@H](C1)[C@@H](CC2CC(=O)NC(=O)C2)O)C InChI=1S/C15H23NO4/c1-8-3-9(2)15(20)11(4-8)12(17)5-10-6-13(18)16-14(19)7-10/h8-12,17H,3-7H2,1-2H3,(H,16,18,19) YPHMISFOHDHNIV-UHFFFAOYSA-N 50080528 Cycloheximid::3-((R)-2-((1S,3S,5S)-3,5-dimethyl-2-oxocyclohexyl)-2-hydroxyethyl)glutarimide::CHEMBL123292::cycloheximide::Zykloheximid::cid_6197::4-{(2R)-2-[(1S,3S,5S)-3,5-dimethyl-2-oxocyclohexyl]-2-hydroxyethyl}piperidine-2,6-dione::med.21724, Compound Cycloheximide 60S ribosomal protein L19-A Saccharomyces cerevisiae (strain ATCC 204508 / S288c) 644 PubChem 10.7270/Q2JQ0ZGP aid2740 PubChem, PC 4/1/2010 7/11/2011 Nmmlsc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50080528 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4787&target=60S+ribosomal+protein+L19-A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50080528&enzyme=60S+ribosomal+protein+L19-A&column=ki&startPg=0&Increment=50&submit=Search 3HE 4U3U,5GAK,5LKS,6HD7,6TNU,6Y0G,6Y2L,7N8B,7Q08,7R81,8BN3,8G6J,8IPA,8IPB,8T2X,8T2Y,8T2Z,8T30,8UT0,8UTI,9BH5,9CAI,9FQZ,9P7F,9P7G,9P7H,9P7I,9P7J,9P8I 6197 103980685 CHEMBL123292 C06685 1 MANLRTQKRLAASVVGVGKRKVWLDPNETSEIAQANSRNAIRKLVKNGTIVKKAVTVHSKSRTRAHAQSKREGRHSGYGKRKGTREARLPSQVVWIRRLRVLRRLLAKYRDAGKIDKHLYHVLYKESKGNAFKHKRALVEHIIQAKADAQREKALNEEAEARRLKNRAARDRRAQRVAEKRDALLKEDA 9R9P,9R9O,9PN5,9F9S,9DP7,9DOV,8Y0U,8V87,8T3F,8T3E,8T3D,8T3C,8T3B,8T3A,8T30,8T2Z,8T2Y,8T2X,8PNN,8PFR,8P9A,8P8U,8P8N,8P8M,8P85,8P4V,8K82,8K2D,8HFR,8EWC,8EWB,8EVT,8EVS,8EVR,8EVQ,8EVP,8EUB,8CMJ,8CKU,8CIV,8CGN,8CG8,8CF5,8CEH,8CDR,8CDL,8CCS,8AGZ,8AGX,8AGW,8AGV,8AGU,8AGT,8AAF,7ZW0,7Z34,7V08,7UQZ,7UQB,7UOO,7UG6,7U0H,7TOP,7TOO,7RR5,7R7A,7R72,7OHV,7OHR,7OHQ,7OH3,7OF1,7NAD,7NAC,7BTB,7BT6,7AZY,6Z6K,6Z6J,6YLY,6YLX,6YLH,6YLG,6XIR,6XIQ,6T83,6T7I,6SV4,6S05,6RZZ,6RI5,6QTZ,6QT0,6QIK,6N8L,6N8K,6N8J,6M62,6HHQ,6HD7,6FT6,6EM5,6ELZ,5MC6,5JUU,5JUT,5JUS,5JUP,5JUO,5JCS,5H4P,5GAK,5APO,5APN,4V91,4V8T,4V88,4V7R,4V7F,4V6I,3JCT,2WWB,2WWA,2WW9,8ZHC,8ZHB,8ZH3,8ZGY,8ZGR,8Z71,8Z70,8YLR,8YLD,8XU8,8UTI,8UT0,8BQX,8BQD,8BN3,8BJQ,8BIP,7ZUX,7ZUW,7ZRS,7ZPQ,7NRD,7NRC,7N8B,7MPJ,7MPI,7B7D,6WOO,6TNU,6TB3,6T7T,6T4Q,6S47,6Q8Y,6OIG,6I7O,6GQV,6GQB,6GQ1,5TGM,5TGA,5TBW,5ON6,5OBM,5NDW,5NDV,5NDG,5MEI,5M1J,5LYB,5I4L,5FCJ,5FCI,5DGV,5DGF,5DGE,5DC3,5DAT,4V8Z,4V8Y,4U6F,4U56,4U55,4U53,4U52,4U51,4U50,4U4Z,4U4Y,4U4U,4U4R,4U4Q,4U4O,4U4N,4U3U,4U3N,4U3M,7ZS5,6R87,6R86,6R84,4V4B,4V7H Large ribosomal subunit protein eL19A RL19A_YEAST P0CX82 D6VPX3 P05735 122677 C[C@H]1C[C@@H](C(=O)[C@@H](C1)[C@@H](CC2CC(=O)NC(=O)C2)O)C InChI=1S/C15H23NO4/c1-8-3-9(2)15(20)11(4-8)12(17)5-10-6-13(18)16-14(19)7-10/h8-12,17H,3-7H2,1-2H3,(H,16,18,19) YPHMISFOHDHNIV-UHFFFAOYSA-N 50080528 Cycloheximid::3-((R)-2-((1S,3S,5S)-3,5-dimethyl-2-oxocyclohexyl)-2-hydroxyethyl)glutarimide::CHEMBL123292::cycloheximide::Zykloheximid::cid_6197::4-{(2R)-2-[(1S,3S,5S)-3,5-dimethyl-2-oxocyclohexyl]-2-hydroxyethyl}piperidine-2,6-dione::med.21724, Compound Cycloheximide 60S ribosomal protein L19-A Saccharomyces cerevisiae (strain ATCC 204508 / S288c) 644 PubChem 10.7270/Q2JQ0ZGP aid2740 PubChem, PC 4/1/2010 7/11/2011 Nmmlsc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50080528 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4787&target=60S+ribosomal+protein+L19-A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50080528&enzyme=60S+ribosomal+protein+L19-A&column=ki&startPg=0&Increment=50&submit=Search 3HE 4U3U,5GAK,5LKS,6HD7,6TNU,6Y0G,6Y2L,7N8B,7Q08,7R81,8BN3,8G6J,8IPA,8IPB,8T2X,8T2Y,8T2Z,8T30,8UT0,8UTI,9BH5,9CAI,9FQZ,9P7F,9P7G,9P7H,9P7I,9P7J,9P8I 6197 103980685 CHEMBL123292 C06685 1 MANLRTQKRLAASVVGVGKRKVWLDPNETSEIAQANSRNAIRKLVKNGTIVKKAVTVHSKSRTRAHAQSKREGRHSGYGKRKGTREARLPSQVVWIRRLRVLRRLLAKYRDAGKIDKHLYHVLYKESKGNAFKHKRALVEHIIQAKADAQREKALNEEAEARRLKNRAARDRRAQRVAEKRDALLKEDA 9R9P,9R9O,9PN5,9F9S,9DP7,9DOV,8Y0U,8V87,8T3F,8T3E,8T3D,8T3C,8T3B,8T3A,8T30,8T2Z,8T2Y,8T2X,8PNN,8PFR,8P9A,8P8U,8P8N,8P8M,8P85,8P4V,8K82,8K2D,8HFR,8EWC,8EWB,8EVT,8EVS,8EVR,8EVQ,8EVP,8EUB,8CMJ,8CKU,8CIV,8CGN,8CG8,8CF5,8CEH,8CDR,8CDL,8CCS,8AGZ,8AGX,8AGW,8AGV,8AGU,8AGT,8AAF,7ZW0,7Z34,7V08,7UQZ,7UQB,7UOO,7UG6,7U0H,7TOP,7TOO,7RR5,7R7A,7R72,7OHV,7OHR,7OHQ,7OH3,7OF1,7NAD,7NAC,7BTB,7BT6,7AZY,6Z6K,6Z6J,6YLY,6YLX,6YLH,6YLG,6XIR,6XIQ,6T83,6T7I,6SV4,6S05,6RZZ,6RI5,6QTZ,6QT0,6QIK,6N8L,6N8K,6N8J,6M62,6HHQ,6HD7,6FT6,6EM5,6ELZ,5MC6,5JUU,5JUT,5JUS,5JUP,5JUO,5JCS,5H4P,5GAK,5APO,5APN,4V91,4V8T,4V88,4V7R,4V7F,4V6I,3JCT,2WWB,2WWA,2WW9,8ZHC,8ZHB,8ZH3,8ZGY,8ZGR,8Z71,8Z70,8YLR,8YLD,8XU8,8UTI,8UT0,8BQX,8BQD,8BN3,8BJQ,8BIP,7ZUX,7ZUW,7ZRS,7ZPQ,7NRD,7NRC,7N8B,7MPJ,7MPI,7B7D,6WOO,6TNU,6TB3,6T7T,6T4Q,6S47,6Q8Y,6OIG,6I7O,6GQV,6GQB,6GQ1,5TGM,5TGA,5TBW,5ON6,5OBM,5NDW,5NDV,5NDG,5MEI,5M1J,5LYB,5I4L,5FCJ,5FCI,5DGV,5DGF,5DGE,5DC3,5DAT,4V8Z,4V8Y,4U6F,4U56,4U55,4U53,4U52,4U51,4U50,4U4Z,4U4Y,4U4U,4U4R,4U4Q,4U4O,4U4N,4U3U,4U3N,4U3M,7ZS5,6R87,6R86,6R84,4V4B,4V7H Large ribosomal subunit protein eL19A RL19A_YEAST P0CX82 D6VPX3 P05735 50028847 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 120 ChEMBL 10.1021/jm00213a022 10.7270/Q26977R0 576620 Song, R; Qiao, W; He, J; Huang, J; Luo, Y; Yang, T 3/25/2021 4/18/2024 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 50029539 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 1080 ChEMBL 10.1021/jm00213a022 10.7270/Q26977R0 576620 Song, R; Qiao, W; He, J; Huang, J; Luo, Y; Yang, T 3/25/2021 4/18/2024 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 50029543 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 1.2 ChEMBL 10.1021/jm00213a022 10.7270/Q26977R0 576620 Song, R; Qiao, W; He, J; Huang, J; Luo, Y; Yang, T 3/25/2021 4/18/2024 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 50494739 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 37 ChEMBL 10.1016/j.bmcl.2016.04.067 10.7270/Q2N018GG 27158142 Yang, L; Wang, W; Sun, Q; Xu, F; Niu, Y; Wang, C; Liang, L; Xu, P 6/15/2016 8/25/2017 Peking University Health Science Center http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 50494751 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 44 ChEMBL 10.1016/j.bmcl.2016.04.067 10.7270/Q2N018GG 27158142 Yang, L; Wang, W; Sun, Q; Xu, F; Niu, Y; Wang, C; Liang, L; Xu, P 6/15/2016 8/25/2017 Peking University Health Science Center http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 50494763 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 52 ChEMBL 10.1016/j.bmcl.2016.04.067 10.7270/Q2N018GG 27158142 Yang, L; Wang, W; Sun, Q; Xu, F; Niu, Y; Wang, C; Liang, L; Xu, P 6/15/2016 8/25/2017 Peking University Health Science Center http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 50521882 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 1.4 ChEMBL 10.1016/j.ejmech.2016.05.049 10.7270/Q28C9Z6K 27318981 Di Giovanni, C; Ettari, R; Sarno, S; Rotondo, A; Bitto, A; Squadrito, F; Altavilla, D; Schirmeister, T; Novellino, E; Grasso, S; Zappalà, M; Lavecchia, A 10/4/2016 7/10/2018 University of Naples Federico Ii http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 50521890 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 22100 ChEMBL 10.1016/j.ejmech.2016.05.049 10.7270/Q28C9Z6K 27318981 Di Giovanni, C; Ettari, R; Sarno, S; Rotondo, A; Bitto, A; Squadrito, F; Altavilla, D; Schirmeister, T; Novellino, E; Grasso, S; Zappalà, M; Lavecchia, A 10/4/2016 7/10/2018 University of Naples Federico Ii http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 50521891 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 5520 ChEMBL 10.1016/j.ejmech.2016.05.049 10.7270/Q28C9Z6K 27318981 Di Giovanni, C; Ettari, R; Sarno, S; Rotondo, A; Bitto, A; Squadrito, F; Altavilla, D; Schirmeister, T; Novellino, E; Grasso, S; Zappalà, M; Lavecchia, A 10/4/2016 7/10/2018 University of Naples Federico Ii http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 50711335 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 25 ChEMBL 10.1016/j.ejmech.2016.11.024 10.7270/Q2Z03BDZ 27889629 Qin, JM; Huang, RZ; Yao, GY; Liao, ZX; Pan, YM; Wang, HS 1/27/2017 6/17/2019 Guangxi Normal University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51002658 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 470 ChEMBL 10.1021/jm058289o 10.7270/Q2FF3S0S 16686537 Rydzewski, RM; Burrill, L; Mendonca, R; Palmer, JT; Rice, M; Tahilramani, R; Bass, KE; Leung, L; Gjerstad, E; Janc, JW; Pan, L 5/11/2006 11/10/2009 Celera http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51002662 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 3.7 ChEMBL 10.1021/jm058289o 10.7270/Q2FF3S0S 16686537 Rydzewski, RM; Burrill, L; Mendonca, R; Palmer, JT; Rice, M; Tahilramani, R; Bass, KE; Leung, L; Gjerstad, E; Janc, JW; Pan, L 5/11/2006 11/10/2009 Celera http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51002664 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 330 ChEMBL 10.1021/jm058289o 10.7270/Q2FF3S0S 16686537 Rydzewski, RM; Burrill, L; Mendonca, R; Palmer, JT; Rice, M; Tahilramani, R; Bass, KE; Leung, L; Gjerstad, E; Janc, JW; Pan, L 5/11/2006 11/10/2009 Celera http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51087096 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 2100 ChEMBL 10.1016/j.ejmech.2013.11.009 10.7270/Q2222W81 24321833 Hasegawa, M; Yasuda, Y; Tanaka, M; Nakata, K; Umeda, E; Wang, Y; Watanabe, C; Uetake, S; Kunoh, T; Shionyu, M; Sasaki, R; Shiina, I; Mizukami, T 1/31/2014 7/25/2014 Institute of Bio-Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51087151 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 120 ChEMBL 10.1016/j.ejmech.2013.11.009 10.7270/Q2222W81 24321833 Hasegawa, M; Yasuda, Y; Tanaka, M; Nakata, K; Umeda, E; Wang, Y; Watanabe, C; Uetake, S; Kunoh, T; Shionyu, M; Sasaki, R; Shiina, I; Mizukami, T 1/31/2014 7/25/2014 Institute of Bio-Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51087152 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 11 ChEMBL 10.1016/j.ejmech.2013.11.009 10.7270/Q2222W81 24321833 Hasegawa, M; Yasuda, Y; Tanaka, M; Nakata, K; Umeda, E; Wang, Y; Watanabe, C; Uetake, S; Kunoh, T; Shionyu, M; Sasaki, R; Shiina, I; Mizukami, T 1/31/2014 7/25/2014 Institute of Bio-Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51110847 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 1.000000 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51110850 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 5520 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51110852 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 22100 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51110856 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 4.0 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51110862 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 130 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51110863 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 70 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51227585 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 1.2 ChEMBL 10.1016/j.bmc.2018.12.022 10.7270/Q2NP27P1 30581047 Pehere, AD; Nguyen, S; Garlick, SK; Wilson, DW; Hudson, I; Sykes, MJ; Morton, JD; Abell, AD 1/15/2019 2/18/2021 University of Adelaide http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51289132 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 1450 ChEMBL 10.1021/acsmedchemlett.9b00233 10.7270/Q2930XK7 31312413 Pacifico, S; Ferretti, V; Albanese, V; Fantinati, A; Gallerani, E; Nicoli, F; Gavioli, R; Zamberlan, F; Preti, D; Marastoni, M 7/11/2019 2/24/2021 University of Ferrara http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51289181 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 4590 ChEMBL 10.1021/acsmedchemlett.9b00233 10.7270/Q2930XK7 31312413 Pacifico, S; Ferretti, V; Albanese, V; Fantinati, A; Gallerani, E; Nicoli, F; Gavioli, R; Zamberlan, F; Preti, D; Marastoni, M 7/11/2019 2/24/2021 University of Ferrara http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51289196 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 7.0 ChEMBL 10.1021/acsmedchemlett.9b00233 10.7270/Q2930XK7 31312413 Pacifico, S; Ferretti, V; Albanese, V; Fantinati, A; Gallerani, E; Nicoli, F; Gavioli, R; Zamberlan, F; Preti, D; Marastoni, M 7/11/2019 2/24/2021 University of Ferrara http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51298902 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 30 ChEMBL 10.1016/j.bmc.2019.115161 10.7270/Q29W0JZJ 31732281 Uesugi, S; Honmura, Y; Nishiyama, M; Kusakabe, K; Tonouchi, A; Yamashita, T; Hashimoto, M; Kimura, KI 12/15/2019 2/25/2021 Iwate University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51298906 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 1600 ChEMBL 10.1016/j.bmc.2019.115161 10.7270/Q29W0JZJ 31732281 Uesugi, S; Honmura, Y; Nishiyama, M; Kusakabe, K; Tonouchi, A; Yamashita, T; Hashimoto, M; Kimura, KI 12/15/2019 2/25/2021 Iwate University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51298909 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 500 ChEMBL 10.1016/j.bmc.2019.115161 10.7270/Q29W0JZJ 31732281 Uesugi, S; Honmura, Y; Nishiyama, M; Kusakabe, K; Tonouchi, A; Yamashita, T; Hashimoto, M; Kimura, KI 12/15/2019 2/25/2021 Iwate University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51487773 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 22100 ChEMBL 10.7270/Q20R9TGT 34838650 Ettari, R; Iraci, N; Di Chio, C; Previti, S; Danzè, M; Zappalà, M 1/1/2022 6/23/2023 University of Messina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51487774 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 5520 ChEMBL 10.7270/Q20R9TGT 34838650 Ettari, R; Iraci, N; Di Chio, C; Previti, S; Danzè, M; Zappalà, M 1/1/2022 6/23/2023 University of Messina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51487775 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 1.4 ChEMBL 10.7270/Q20R9TGT 34838650 Ettari, R; Iraci, N; Di Chio, C; Previti, S; Danzè, M; Zappalà, M 1/1/2022 6/23/2023 University of Messina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51487776 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 130 ChEMBL 10.7270/Q20R9TGT 34838650 Ettari, R; Iraci, N; Di Chio, C; Previti, S; Danzè, M; Zappalà, M 1/1/2022 6/23/2023 University of Messina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51487777 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 1.000000 ChEMBL 10.7270/Q20R9TGT 34838650 Ettari, R; Iraci, N; Di Chio, C; Previti, S; Danzè, M; Zappalà, M 1/1/2022 6/23/2023 University of Messina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51159619 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 A5LHX3/O14818/P20618/P25786/P25787/P25788/P25789/P28062/P28065/P28066/P28070/P28072/P28074/P40306/P49720/P49721/P60900/Q8TAA3/Q99436 Homo sapiens 4500 ChEMBL 10.1016/j.bmcl.2005.02.013 10.7270/Q2CF9SVN 15780623 Momose, I; Umezawa, Y; Hirosawa, S; Iinuma, H; Ikeda, D 4/1/2005 8/23/2020 Numazu Bio-Medical Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000077&target=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 19 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 MALLDVCGAPRGQRPESALPVAGSGRRSDPGHYSFSMRSPELALPRGMQPTEFFQSLGGDGERNVQIEMAHGTTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAIAYATHRDSYSGGVVNMYHMKEDGWVKVESTDVSDLLHQYREANQ 6E5B,6AVO,7B12,7AWE Proteasome subunit beta type-8 PSB8_HUMAN P28062 B0UZC0 Q29824 Q5JNW6 Q5QNR8 Q96J48 MLRAGAPTGDLPRAGEVHTGTTIMAVEFDGGVVMGSDSRVSAGEAVVNRVFDKLSPLHERIYCALSGSAADAQAVADMAAYQLELHGIELEEPPLVLAAANVVRNISYKYREDLSAHLMVAGWDQREGGQVYGTLGGMLTRQPFAIGGSGSTFIYGYVDAAYKPGMSPEECRRFTTDAIALAMSRDGSSGGVIYLVTITAAGVDHRVILGNELPKFYDE 6E5B,7B12,7AWE,6AVO,8YVG,8YSX Proteasome subunit beta type-9 PSB9_HUMAN P28065 B0V0T1 Q16523 Q5JNW4 MAATLLAARGAGPAPAWGPEAFTPDWESREVSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDRIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAASLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTANALALAMERDGSSGGVIRLAAIAESGVERQVLLGDQIPKFAVATLPPA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,9RKZ,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6R70,9QVX,6XMJ,4R67,4R3O,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit beta type-6 PSB6_HUMAN P28072 Q96J55 MFRNQYDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSELAAHQKKILHVDNHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGARSQSARTYLERHMSEFMECNLNELVKHGLRALRETLPAEQDLTTKNVSIGIVGKDLEFTIYDDDDVSPFLEGLEERPQRKAQPAQPADEPAEKADEPMEH 9YUZ,9UG9,9UF8,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9VUG,9VUF,9VUE,9U7R,9U3L,9SZV,9SZT,9MBQ,9MBP,9HEU,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,7DRW,7DR7,7DR6,8YVG,8YSX,8QYS,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,5M32,9QVX Proteasome subunit alpha type-1 PSA1_HUMAN P25786 A8K400 Q53YE8 Q9BRV9 MAERGYSFSLTTFSPSGKLVQIEYALAAVAGGAPSVGIKAANGVVLATEKKQKSILYDERSVHKVEPITKHIGLVYSGMGPDYRVLVHRARKLAQQYYLVYQEPIPTAQLVQRVASVMQEYTQSGGVRPFGVSLLICGWNEGRPYLFQSDPSGAYFAWKATAMGKNYVNGKTFLEKRYNEDLELEDAIHTAILTLKESFEGQMTEDNIEVGICNEAGFRRLTPTEVKDYLAAIA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YVG,8YSX,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYS,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,9U7R,9U3L,9MBQ,9MBP,9HMN,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6XMJ,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,4R67,4R3O,22MM,1IRU,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,6R70,9QVX,7B12,7AWE Proteasome subunit alpha type-2 PSA2_HUMAN P25787 Q6ICS6 Q9BU45 MSSIGTGYDLSASTFSPDGRVFQVEYAMKAVENSSTAIGIRCKDGVVFGVEKLVLSKLYEEGSNKRLFNVDRHVGMAVAGLLADARSLADIAREEASNFRSNFGYNIPLKHLADRVAMYVHAYTLYSAVRPFGCSFMLGSYSVNDGAQLYMIDPSGVSYGYWGCAIGKARQAAKTEIEKLQMKEMTCRDIVKEVAKIIYIVHDEVKDKAFELELSWVGELTNGRHEIVPKDIREEAEKYAKESLKEEDESDDDNM 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7E55,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5DSV,5A0Q,9U7R,9U3L,9MBQ,9MBP,9HMN,8FZ6,8FZ5,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7DRW,7DR7,7DR6,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,1IRU,6TU3,6EPF,6EPE,6EPD,6EPC,8YVP,8YPK,3UNH,3UNF,3UNE,3UNB,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,8QYS,6R70,9QVX Proteasome subunit alpha type-3 PSA3_HUMAN P25788 B2RCK6 Q86U83 Q8N1D8 Q9BS70 MSRRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGEMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTRENGKTVIRVLKQKEVEQLIKKHEEEEAKAEREKKEKEQKEKDK 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,7AWE,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,6R70,8QYS,9QVX Proteasome subunit alpha type-4 PSA4_HUMAN P25789 D3DW86 Q53XP2 Q567Q5 Q8TBD1 MFLTRSEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKTLIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGEEDADPGAMSRPFGVALLFGGVDEKGPQLFHMDPSGTFVQCDARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKLNATNIELATVQPGQNFHMFTKEELEEVIKDI 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDI,9NKJ,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8O,9E8N,9E8L,9E8K,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YVP,8YVG,8YSX,8YPK,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QYO,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,22MM,8QZ9,8QYN,8QYM,8QYL,8QYJ,8QYS,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9QVX,6R70,7B12,7AWE Proteasome subunit alpha type-5 PSA5_HUMAN P28066 B2R8F6 B4E2V4 Q3T1C1 Q6IBF7 MSRGSSAGFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITENIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATAAGVKQTESTSFLEKKVKKKFDWTFEQTVETAITCLSTVLSIDFKPSEIEVGVVTVENPKFRILTEAEIDAHLVALAERD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6TU3,6RGQ,6REY,6KWY,6EPF,6EPE,6EPD,6EPC,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,6XMJ,6R70,4R67,4R3O,7B12,7AWE,9QVX,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit alpha type-6 PSA6_HUMAN P60900 B2R7J9 B4DQR4 B4DXJ9 P34062 Q6IB60 MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIGRGAKSVREFLEKNYTDEAIETDDLTIKLVIKALLEVVQSGGKNIELAVMRRDQSLKILNPEEIEKYVAEIEKEKEENEKKKQKKAS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,22MM,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7AWE,6R70,7B12,8QYS,9QVX Proteasome subunit alpha type-7 PSA7_HUMAN O14818 B2R515 Q5JXJ2 Q9BR53 Q9H4K5 Q9UEU8 MASRYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVCMAFAVLTIFIGLTADARVVINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDAIASDSEAIKLAIKALLEVVQSGGKNIELAIIRRNQPLKMFSAKEVELYVTEIEKEKEEAEKKKSKKSV Proteasome subunit alpha-type 8 PSMA8_HUMAN Q8TAA3 B0YJ75 Q8IVP4 Q8TA98 Q8TAA2 MLKPALEPRGGFSFENCQRNASLERVLPGLKVPHARKTGTTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATVTRILRQTLFRYQGHVGASLIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLLVEAVTAGILGDLGSGGNVDACVITKTGAKLLRTLSSPTEPVKRSGRYHFVPGTTAVLTQTVKPLTLELVEETVQAMEVE 6E5B,6AVO,7AWE Proteasome subunit beta type-10 PSB10_HUMAN P40306 B2R5J4 Q5U098 MALQDVCKWQSPDTQGPSPHLPRAGGWAVPRGCDPQTFLQIHGPRLAHGTTTLAFRFRHGVIAAADTRSSCGSYVACPASCKVIPVHQHLLGTTSGTSADCATWYRVLQRELRLRELREGQLPSVASAAKLLSAMMSQYRGLDLCVATALCGWDRSGPELFYVYSDGTRLQGDIFSVGSGSPYAYGVLDRGYRYDMSTQEAYALARCAVAHATHRDAYSGGSVDLFHVRESGWEHVSRSDACVLYVELQKLLEPEPEEDASHAHPEPATAHRAAEDRELSVGPGEVTPGDSRMPAGTETV Proteasome subunit beta type-11 PSB11_HUMAN A5LHX3 MSIMSYNGGAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYTLMSMVANLLYEKRFGPYYTEPVIAGLDPKTFKPFICSLDLIGCPMVTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLFETISQAMLNAVDRDAVSGMGVIVHIIEKDKITTRTLKARMD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QZ9,8QYO,8QYN,8QYM,8QYL,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,9U7R,9U3L,9RKZ,9QVX,9MBQ,9MBP,9HMN,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7B12,7AWE,6XMJ,6WJN,6WJD,6R70,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5T0J,5T0I,5T0H,5T0G,5T0C,5A0Q,4R67,4R3O,22MM,8YVP,8YPK,6TU3,3UNH,3UNF,3UNE,3UNB,8QYS Proteasome subunit beta type-3 PSB3_HUMAN P49720 P31147 Q0P6J7 Q96E27 MEAFLGSRSGLWAGGPAPGQFYRIPSTPDSFMDPASALYRGPITRTQNPMVTGTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNNSTMLGASGDYADFQYLKQVLGQMVIDEELLGDGHSYSPRAIHSWLTRAMYSRRSKMNPLWNTMVIGGYADGESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREVLEKQPVLSQTEARDLVERCMRVLYYRDARSYNRFQIATVTEKGVEIEGPLSTETNWDIAHMISGFE 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9BW4,9BV3,9BV2,9BV1,9BUI,8TM6,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YIZ,8YIY,8YIX,9RKZ,9HMN,8UD9,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,6AVO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,6XMJ,4R67,4R3O,6R70,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,7B12,7AWE,9QVX Proteasome subunit beta type-4 PSB4_HUMAN P28070 B2R9L3 P31148 Q5SZS5 Q6IBI4 Q969L6 MAAVSVYAPPVGGFSFDNCRRNAVLEADFAKRGYKLPKVRKTGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTANRMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAIAAGIFNDLGSGSNIDLCVISKNKLDFLRPYTVPNKKGTRLGRYRCEKGTTAVLTEKITPLEIEVLEETVQTMDTS 8QZ9,8QYN,8QYM,8QYL,8QYJ,9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8TM6,8TM5,8TM4,8QYO,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,9RKZ,9HMN,8UD9,8CVS,8CVR,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,9QVX,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O Proteasome subunit beta type-7 PSB7_HUMAN Q99436 B4E0P1 Q5TBG6 Q96AG8 Q9BWA7 51159624 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 A5LHX3/O14818/P20618/P25786/P25787/P25788/P25789/P28062/P28065/P28066/P28070/P28072/P28074/P40306/P49720/P49721/P60900/Q8TAA3/Q99436 Homo sapiens 1400 ChEMBL 10.1016/j.bmcl.2005.02.013 10.7270/Q2CF9SVN 15780623 Momose, I; Umezawa, Y; Hirosawa, S; Iinuma, H; Ikeda, D 4/1/2005 8/23/2020 Numazu Bio-Medical Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000077&target=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 19 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 MALLDVCGAPRGQRPESALPVAGSGRRSDPGHYSFSMRSPELALPRGMQPTEFFQSLGGDGERNVQIEMAHGTTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAIAYATHRDSYSGGVVNMYHMKEDGWVKVESTDVSDLLHQYREANQ 6E5B,6AVO,7B12,7AWE Proteasome subunit beta type-8 PSB8_HUMAN P28062 B0UZC0 Q29824 Q5JNW6 Q5QNR8 Q96J48 MLRAGAPTGDLPRAGEVHTGTTIMAVEFDGGVVMGSDSRVSAGEAVVNRVFDKLSPLHERIYCALSGSAADAQAVADMAAYQLELHGIELEEPPLVLAAANVVRNISYKYREDLSAHLMVAGWDQREGGQVYGTLGGMLTRQPFAIGGSGSTFIYGYVDAAYKPGMSPEECRRFTTDAIALAMSRDGSSGGVIYLVTITAAGVDHRVILGNELPKFYDE 6E5B,7B12,7AWE,6AVO,8YVG,8YSX Proteasome subunit beta type-9 PSB9_HUMAN P28065 B0V0T1 Q16523 Q5JNW4 MAATLLAARGAGPAPAWGPEAFTPDWESREVSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDRIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAASLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTANALALAMERDGSSGGVIRLAAIAESGVERQVLLGDQIPKFAVATLPPA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,9RKZ,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6R70,9QVX,6XMJ,4R67,4R3O,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit beta type-6 PSB6_HUMAN P28072 Q96J55 MFRNQYDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSELAAHQKKILHVDNHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGARSQSARTYLERHMSEFMECNLNELVKHGLRALRETLPAEQDLTTKNVSIGIVGKDLEFTIYDDDDVSPFLEGLEERPQRKAQPAQPADEPAEKADEPMEH 9YUZ,9UG9,9UF8,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9VUG,9VUF,9VUE,9U7R,9U3L,9SZV,9SZT,9MBQ,9MBP,9HEU,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,7DRW,7DR7,7DR6,8YVG,8YSX,8QYS,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,5M32,9QVX Proteasome subunit alpha type-1 PSA1_HUMAN P25786 A8K400 Q53YE8 Q9BRV9 MAERGYSFSLTTFSPSGKLVQIEYALAAVAGGAPSVGIKAANGVVLATEKKQKSILYDERSVHKVEPITKHIGLVYSGMGPDYRVLVHRARKLAQQYYLVYQEPIPTAQLVQRVASVMQEYTQSGGVRPFGVSLLICGWNEGRPYLFQSDPSGAYFAWKATAMGKNYVNGKTFLEKRYNEDLELEDAIHTAILTLKESFEGQMTEDNIEVGICNEAGFRRLTPTEVKDYLAAIA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YVG,8YSX,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYS,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,9U7R,9U3L,9MBQ,9MBP,9HMN,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6XMJ,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,4R67,4R3O,22MM,1IRU,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,6R70,9QVX,7B12,7AWE Proteasome subunit alpha type-2 PSA2_HUMAN P25787 Q6ICS6 Q9BU45 MSSIGTGYDLSASTFSPDGRVFQVEYAMKAVENSSTAIGIRCKDGVVFGVEKLVLSKLYEEGSNKRLFNVDRHVGMAVAGLLADARSLADIAREEASNFRSNFGYNIPLKHLADRVAMYVHAYTLYSAVRPFGCSFMLGSYSVNDGAQLYMIDPSGVSYGYWGCAIGKARQAAKTEIEKLQMKEMTCRDIVKEVAKIIYIVHDEVKDKAFELELSWVGELTNGRHEIVPKDIREEAEKYAKESLKEEDESDDDNM 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7E55,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5DSV,5A0Q,9U7R,9U3L,9MBQ,9MBP,9HMN,8FZ6,8FZ5,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7DRW,7DR7,7DR6,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,1IRU,6TU3,6EPF,6EPE,6EPD,6EPC,8YVP,8YPK,3UNH,3UNF,3UNE,3UNB,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,8QYS,6R70,9QVX Proteasome subunit alpha type-3 PSA3_HUMAN P25788 B2RCK6 Q86U83 Q8N1D8 Q9BS70 MSRRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGEMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTRENGKTVIRVLKQKEVEQLIKKHEEEEAKAEREKKEKEQKEKDK 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,7AWE,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,6R70,8QYS,9QVX Proteasome subunit alpha type-4 PSA4_HUMAN P25789 D3DW86 Q53XP2 Q567Q5 Q8TBD1 MFLTRSEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKTLIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGEEDADPGAMSRPFGVALLFGGVDEKGPQLFHMDPSGTFVQCDARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKLNATNIELATVQPGQNFHMFTKEELEEVIKDI 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDI,9NKJ,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8O,9E8N,9E8L,9E8K,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YVP,8YVG,8YSX,8YPK,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QYO,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,22MM,8QZ9,8QYN,8QYM,8QYL,8QYJ,8QYS,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9QVX,6R70,7B12,7AWE Proteasome subunit alpha type-5 PSA5_HUMAN P28066 B2R8F6 B4E2V4 Q3T1C1 Q6IBF7 MSRGSSAGFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITENIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATAAGVKQTESTSFLEKKVKKKFDWTFEQTVETAITCLSTVLSIDFKPSEIEVGVVTVENPKFRILTEAEIDAHLVALAERD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6TU3,6RGQ,6REY,6KWY,6EPF,6EPE,6EPD,6EPC,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,6XMJ,6R70,4R67,4R3O,7B12,7AWE,9QVX,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit alpha type-6 PSA6_HUMAN P60900 B2R7J9 B4DQR4 B4DXJ9 P34062 Q6IB60 MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIGRGAKSVREFLEKNYTDEAIETDDLTIKLVIKALLEVVQSGGKNIELAVMRRDQSLKILNPEEIEKYVAEIEKEKEENEKKKQKKAS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,22MM,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7AWE,6R70,7B12,8QYS,9QVX Proteasome subunit alpha type-7 PSA7_HUMAN O14818 B2R515 Q5JXJ2 Q9BR53 Q9H4K5 Q9UEU8 MASRYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVCMAFAVLTIFIGLTADARVVINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDAIASDSEAIKLAIKALLEVVQSGGKNIELAIIRRNQPLKMFSAKEVELYVTEIEKEKEEAEKKKSKKSV Proteasome subunit alpha-type 8 PSMA8_HUMAN Q8TAA3 B0YJ75 Q8IVP4 Q8TA98 Q8TAA2 MLKPALEPRGGFSFENCQRNASLERVLPGLKVPHARKTGTTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATVTRILRQTLFRYQGHVGASLIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLLVEAVTAGILGDLGSGGNVDACVITKTGAKLLRTLSSPTEPVKRSGRYHFVPGTTAVLTQTVKPLTLELVEETVQAMEVE 6E5B,6AVO,7AWE Proteasome subunit beta type-10 PSB10_HUMAN P40306 B2R5J4 Q5U098 MALQDVCKWQSPDTQGPSPHLPRAGGWAVPRGCDPQTFLQIHGPRLAHGTTTLAFRFRHGVIAAADTRSSCGSYVACPASCKVIPVHQHLLGTTSGTSADCATWYRVLQRELRLRELREGQLPSVASAAKLLSAMMSQYRGLDLCVATALCGWDRSGPELFYVYSDGTRLQGDIFSVGSGSPYAYGVLDRGYRYDMSTQEAYALARCAVAHATHRDAYSGGSVDLFHVRESGWEHVSRSDACVLYVELQKLLEPEPEEDASHAHPEPATAHRAAEDRELSVGPGEVTPGDSRMPAGTETV Proteasome subunit beta type-11 PSB11_HUMAN A5LHX3 MSIMSYNGGAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYTLMSMVANLLYEKRFGPYYTEPVIAGLDPKTFKPFICSLDLIGCPMVTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLFETISQAMLNAVDRDAVSGMGVIVHIIEKDKITTRTLKARMD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QZ9,8QYO,8QYN,8QYM,8QYL,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,9U7R,9U3L,9RKZ,9QVX,9MBQ,9MBP,9HMN,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7B12,7AWE,6XMJ,6WJN,6WJD,6R70,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5T0J,5T0I,5T0H,5T0G,5T0C,5A0Q,4R67,4R3O,22MM,8YVP,8YPK,6TU3,3UNH,3UNF,3UNE,3UNB,8QYS Proteasome subunit beta type-3 PSB3_HUMAN P49720 P31147 Q0P6J7 Q96E27 MEAFLGSRSGLWAGGPAPGQFYRIPSTPDSFMDPASALYRGPITRTQNPMVTGTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNNSTMLGASGDYADFQYLKQVLGQMVIDEELLGDGHSYSPRAIHSWLTRAMYSRRSKMNPLWNTMVIGGYADGESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREVLEKQPVLSQTEARDLVERCMRVLYYRDARSYNRFQIATVTEKGVEIEGPLSTETNWDIAHMISGFE 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9BW4,9BV3,9BV2,9BV1,9BUI,8TM6,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YIZ,8YIY,8YIX,9RKZ,9HMN,8UD9,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,6AVO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,6XMJ,4R67,4R3O,6R70,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,7B12,7AWE,9QVX Proteasome subunit beta type-4 PSB4_HUMAN P28070 B2R9L3 P31148 Q5SZS5 Q6IBI4 Q969L6 MAAVSVYAPPVGGFSFDNCRRNAVLEADFAKRGYKLPKVRKTGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTANRMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAIAAGIFNDLGSGSNIDLCVISKNKLDFLRPYTVPNKKGTRLGRYRCEKGTTAVLTEKITPLEIEVLEETVQTMDTS 8QZ9,8QYN,8QYM,8QYL,8QYJ,9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8TM6,8TM5,8TM4,8QYO,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,9RKZ,9HMN,8UD9,8CVS,8CVR,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,9QVX,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O Proteasome subunit beta type-7 PSB7_HUMAN Q99436 B4E0P1 Q5TBG6 Q96AG8 Q9BWA7 51159634 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 A5LHX3/O14818/P20618/P25786/P25787/P25788/P25789/P28062/P28065/P28066/P28070/P28072/P28074/P40306/P49720/P49721/P60900/Q8TAA3/Q99436 Homo sapiens 68 ChEMBL 10.1016/j.bmcl.2005.02.013 10.7270/Q2CF9SVN 15780623 Momose, I; Umezawa, Y; Hirosawa, S; Iinuma, H; Ikeda, D 4/1/2005 8/23/2020 Numazu Bio-Medical Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000077&target=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 19 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 MALLDVCGAPRGQRPESALPVAGSGRRSDPGHYSFSMRSPELALPRGMQPTEFFQSLGGDGERNVQIEMAHGTTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAIAYATHRDSYSGGVVNMYHMKEDGWVKVESTDVSDLLHQYREANQ 6E5B,6AVO,7B12,7AWE Proteasome subunit beta type-8 PSB8_HUMAN P28062 B0UZC0 Q29824 Q5JNW6 Q5QNR8 Q96J48 MLRAGAPTGDLPRAGEVHTGTTIMAVEFDGGVVMGSDSRVSAGEAVVNRVFDKLSPLHERIYCALSGSAADAQAVADMAAYQLELHGIELEEPPLVLAAANVVRNISYKYREDLSAHLMVAGWDQREGGQVYGTLGGMLTRQPFAIGGSGSTFIYGYVDAAYKPGMSPEECRRFTTDAIALAMSRDGSSGGVIYLVTITAAGVDHRVILGNELPKFYDE 6E5B,7B12,7AWE,6AVO,8YVG,8YSX Proteasome subunit beta type-9 PSB9_HUMAN P28065 B0V0T1 Q16523 Q5JNW4 MAATLLAARGAGPAPAWGPEAFTPDWESREVSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDRIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAASLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTANALALAMERDGSSGGVIRLAAIAESGVERQVLLGDQIPKFAVATLPPA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,9RKZ,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6R70,9QVX,6XMJ,4R67,4R3O,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit beta type-6 PSB6_HUMAN P28072 Q96J55 MFRNQYDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSELAAHQKKILHVDNHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGARSQSARTYLERHMSEFMECNLNELVKHGLRALRETLPAEQDLTTKNVSIGIVGKDLEFTIYDDDDVSPFLEGLEERPQRKAQPAQPADEPAEKADEPMEH 9YUZ,9UG9,9UF8,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9VUG,9VUF,9VUE,9U7R,9U3L,9SZV,9SZT,9MBQ,9MBP,9HEU,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,7DRW,7DR7,7DR6,8YVG,8YSX,8QYS,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,5M32,9QVX Proteasome subunit alpha type-1 PSA1_HUMAN P25786 A8K400 Q53YE8 Q9BRV9 MAERGYSFSLTTFSPSGKLVQIEYALAAVAGGAPSVGIKAANGVVLATEKKQKSILYDERSVHKVEPITKHIGLVYSGMGPDYRVLVHRARKLAQQYYLVYQEPIPTAQLVQRVASVMQEYTQSGGVRPFGVSLLICGWNEGRPYLFQSDPSGAYFAWKATAMGKNYVNGKTFLEKRYNEDLELEDAIHTAILTLKESFEGQMTEDNIEVGICNEAGFRRLTPTEVKDYLAAIA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YVG,8YSX,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYS,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,9U7R,9U3L,9MBQ,9MBP,9HMN,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6XMJ,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,4R67,4R3O,22MM,1IRU,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,6R70,9QVX,7B12,7AWE Proteasome subunit alpha type-2 PSA2_HUMAN P25787 Q6ICS6 Q9BU45 MSSIGTGYDLSASTFSPDGRVFQVEYAMKAVENSSTAIGIRCKDGVVFGVEKLVLSKLYEEGSNKRLFNVDRHVGMAVAGLLADARSLADIAREEASNFRSNFGYNIPLKHLADRVAMYVHAYTLYSAVRPFGCSFMLGSYSVNDGAQLYMIDPSGVSYGYWGCAIGKARQAAKTEIEKLQMKEMTCRDIVKEVAKIIYIVHDEVKDKAFELELSWVGELTNGRHEIVPKDIREEAEKYAKESLKEEDESDDDNM 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7E55,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5DSV,5A0Q,9U7R,9U3L,9MBQ,9MBP,9HMN,8FZ6,8FZ5,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7DRW,7DR7,7DR6,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,1IRU,6TU3,6EPF,6EPE,6EPD,6EPC,8YVP,8YPK,3UNH,3UNF,3UNE,3UNB,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,8QYS,6R70,9QVX Proteasome subunit alpha type-3 PSA3_HUMAN P25788 B2RCK6 Q86U83 Q8N1D8 Q9BS70 MSRRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGEMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTRENGKTVIRVLKQKEVEQLIKKHEEEEAKAEREKKEKEQKEKDK 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,7AWE,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,6R70,8QYS,9QVX Proteasome subunit alpha type-4 PSA4_HUMAN P25789 D3DW86 Q53XP2 Q567Q5 Q8TBD1 MFLTRSEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKTLIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGEEDADPGAMSRPFGVALLFGGVDEKGPQLFHMDPSGTFVQCDARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKLNATNIELATVQPGQNFHMFTKEELEEVIKDI 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDI,9NKJ,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8O,9E8N,9E8L,9E8K,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YVP,8YVG,8YSX,8YPK,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QYO,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,22MM,8QZ9,8QYN,8QYM,8QYL,8QYJ,8QYS,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9QVX,6R70,7B12,7AWE Proteasome subunit alpha type-5 PSA5_HUMAN P28066 B2R8F6 B4E2V4 Q3T1C1 Q6IBF7 MSRGSSAGFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITENIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATAAGVKQTESTSFLEKKVKKKFDWTFEQTVETAITCLSTVLSIDFKPSEIEVGVVTVENPKFRILTEAEIDAHLVALAERD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6TU3,6RGQ,6REY,6KWY,6EPF,6EPE,6EPD,6EPC,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,6XMJ,6R70,4R67,4R3O,7B12,7AWE,9QVX,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit alpha type-6 PSA6_HUMAN P60900 B2R7J9 B4DQR4 B4DXJ9 P34062 Q6IB60 MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIGRGAKSVREFLEKNYTDEAIETDDLTIKLVIKALLEVVQSGGKNIELAVMRRDQSLKILNPEEIEKYVAEIEKEKEENEKKKQKKAS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,22MM,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7AWE,6R70,7B12,8QYS,9QVX Proteasome subunit alpha type-7 PSA7_HUMAN O14818 B2R515 Q5JXJ2 Q9BR53 Q9H4K5 Q9UEU8 MASRYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVCMAFAVLTIFIGLTADARVVINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDAIASDSEAIKLAIKALLEVVQSGGKNIELAIIRRNQPLKMFSAKEVELYVTEIEKEKEEAEKKKSKKSV Proteasome subunit alpha-type 8 PSMA8_HUMAN Q8TAA3 B0YJ75 Q8IVP4 Q8TA98 Q8TAA2 MLKPALEPRGGFSFENCQRNASLERVLPGLKVPHARKTGTTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATVTRILRQTLFRYQGHVGASLIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLLVEAVTAGILGDLGSGGNVDACVITKTGAKLLRTLSSPTEPVKRSGRYHFVPGTTAVLTQTVKPLTLELVEETVQAMEVE 6E5B,6AVO,7AWE Proteasome subunit beta type-10 PSB10_HUMAN P40306 B2R5J4 Q5U098 MALQDVCKWQSPDTQGPSPHLPRAGGWAVPRGCDPQTFLQIHGPRLAHGTTTLAFRFRHGVIAAADTRSSCGSYVACPASCKVIPVHQHLLGTTSGTSADCATWYRVLQRELRLRELREGQLPSVASAAKLLSAMMSQYRGLDLCVATALCGWDRSGPELFYVYSDGTRLQGDIFSVGSGSPYAYGVLDRGYRYDMSTQEAYALARCAVAHATHRDAYSGGSVDLFHVRESGWEHVSRSDACVLYVELQKLLEPEPEEDASHAHPEPATAHRAAEDRELSVGPGEVTPGDSRMPAGTETV Proteasome subunit beta type-11 PSB11_HUMAN A5LHX3 MSIMSYNGGAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYTLMSMVANLLYEKRFGPYYTEPVIAGLDPKTFKPFICSLDLIGCPMVTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLFETISQAMLNAVDRDAVSGMGVIVHIIEKDKITTRTLKARMD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QZ9,8QYO,8QYN,8QYM,8QYL,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,9U7R,9U3L,9RKZ,9QVX,9MBQ,9MBP,9HMN,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7B12,7AWE,6XMJ,6WJN,6WJD,6R70,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5T0J,5T0I,5T0H,5T0G,5T0C,5A0Q,4R67,4R3O,22MM,8YVP,8YPK,6TU3,3UNH,3UNF,3UNE,3UNB,8QYS Proteasome subunit beta type-3 PSB3_HUMAN P49720 P31147 Q0P6J7 Q96E27 MEAFLGSRSGLWAGGPAPGQFYRIPSTPDSFMDPASALYRGPITRTQNPMVTGTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNNSTMLGASGDYADFQYLKQVLGQMVIDEELLGDGHSYSPRAIHSWLTRAMYSRRSKMNPLWNTMVIGGYADGESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREVLEKQPVLSQTEARDLVERCMRVLYYRDARSYNRFQIATVTEKGVEIEGPLSTETNWDIAHMISGFE 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9BW4,9BV3,9BV2,9BV1,9BUI,8TM6,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YIZ,8YIY,8YIX,9RKZ,9HMN,8UD9,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,6AVO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,6XMJ,4R67,4R3O,6R70,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,7B12,7AWE,9QVX Proteasome subunit beta type-4 PSB4_HUMAN P28070 B2R9L3 P31148 Q5SZS5 Q6IBI4 Q969L6 MAAVSVYAPPVGGFSFDNCRRNAVLEADFAKRGYKLPKVRKTGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTANRMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAIAAGIFNDLGSGSNIDLCVISKNKLDFLRPYTVPNKKGTRLGRYRCEKGTTAVLTEKITPLEIEVLEETVQTMDTS 8QZ9,8QYN,8QYM,8QYL,8QYJ,9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8TM6,8TM5,8TM4,8QYO,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,9RKZ,9HMN,8UD9,8CVS,8CVR,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,9QVX,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O Proteasome subunit beta type-7 PSB7_HUMAN Q99436 B4E0P1 Q5TBG6 Q96AG8 Q9BWA7 50028847 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 120 ChEMBL 10.1021/jm00213a022 10.7270/Q26977R0 576620 Song, R; Qiao, W; He, J; Huang, J; Luo, Y; Yang, T 3/25/2021 4/18/2024 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 50029539 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 1080 ChEMBL 10.1021/jm00213a022 10.7270/Q26977R0 576620 Song, R; Qiao, W; He, J; Huang, J; Luo, Y; Yang, T 3/25/2021 4/18/2024 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 50029543 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 1.2 ChEMBL 10.1021/jm00213a022 10.7270/Q26977R0 576620 Song, R; Qiao, W; He, J; Huang, J; Luo, Y; Yang, T 3/25/2021 4/18/2024 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 50494739 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 37 ChEMBL 10.1016/j.bmcl.2016.04.067 10.7270/Q2N018GG 27158142 Yang, L; Wang, W; Sun, Q; Xu, F; Niu, Y; Wang, C; Liang, L; Xu, P 6/15/2016 8/25/2017 Peking University Health Science Center http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 50494751 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 44 ChEMBL 10.1016/j.bmcl.2016.04.067 10.7270/Q2N018GG 27158142 Yang, L; Wang, W; Sun, Q; Xu, F; Niu, Y; Wang, C; Liang, L; Xu, P 6/15/2016 8/25/2017 Peking University Health Science Center http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 50494763 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 52 ChEMBL 10.1016/j.bmcl.2016.04.067 10.7270/Q2N018GG 27158142 Yang, L; Wang, W; Sun, Q; Xu, F; Niu, Y; Wang, C; Liang, L; Xu, P 6/15/2016 8/25/2017 Peking University Health Science Center http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 50521882 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 1.4 ChEMBL 10.1016/j.ejmech.2016.05.049 10.7270/Q28C9Z6K 27318981 Di Giovanni, C; Ettari, R; Sarno, S; Rotondo, A; Bitto, A; Squadrito, F; Altavilla, D; Schirmeister, T; Novellino, E; Grasso, S; Zappalà, M; Lavecchia, A 10/4/2016 7/10/2018 University of Naples Federico Ii http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 50521890 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 22100 ChEMBL 10.1016/j.ejmech.2016.05.049 10.7270/Q28C9Z6K 27318981 Di Giovanni, C; Ettari, R; Sarno, S; Rotondo, A; Bitto, A; Squadrito, F; Altavilla, D; Schirmeister, T; Novellino, E; Grasso, S; Zappalà, M; Lavecchia, A 10/4/2016 7/10/2018 University of Naples Federico Ii http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 50521891 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 5520 ChEMBL 10.1016/j.ejmech.2016.05.049 10.7270/Q28C9Z6K 27318981 Di Giovanni, C; Ettari, R; Sarno, S; Rotondo, A; Bitto, A; Squadrito, F; Altavilla, D; Schirmeister, T; Novellino, E; Grasso, S; Zappalà, M; Lavecchia, A 10/4/2016 7/10/2018 University of Naples Federico Ii http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 50711335 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 25 ChEMBL 10.1016/j.ejmech.2016.11.024 10.7270/Q2Z03BDZ 27889629 Qin, JM; Huang, RZ; Yao, GY; Liao, ZX; Pan, YM; Wang, HS 1/27/2017 6/17/2019 Guangxi Normal University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51002658 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 470 ChEMBL 10.1021/jm058289o 10.7270/Q2FF3S0S 16686537 Rydzewski, RM; Burrill, L; Mendonca, R; Palmer, JT; Rice, M; Tahilramani, R; Bass, KE; Leung, L; Gjerstad, E; Janc, JW; Pan, L 5/11/2006 11/10/2009 Celera http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51002662 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 3.7 ChEMBL 10.1021/jm058289o 10.7270/Q2FF3S0S 16686537 Rydzewski, RM; Burrill, L; Mendonca, R; Palmer, JT; Rice, M; Tahilramani, R; Bass, KE; Leung, L; Gjerstad, E; Janc, JW; Pan, L 5/11/2006 11/10/2009 Celera http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51002664 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 330 ChEMBL 10.1021/jm058289o 10.7270/Q2FF3S0S 16686537 Rydzewski, RM; Burrill, L; Mendonca, R; Palmer, JT; Rice, M; Tahilramani, R; Bass, KE; Leung, L; Gjerstad, E; Janc, JW; Pan, L 5/11/2006 11/10/2009 Celera http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51087096 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 2100 ChEMBL 10.1016/j.ejmech.2013.11.009 10.7270/Q2222W81 24321833 Hasegawa, M; Yasuda, Y; Tanaka, M; Nakata, K; Umeda, E; Wang, Y; Watanabe, C; Uetake, S; Kunoh, T; Shionyu, M; Sasaki, R; Shiina, I; Mizukami, T 1/31/2014 7/25/2014 Institute of Bio-Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51087151 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 120 ChEMBL 10.1016/j.ejmech.2013.11.009 10.7270/Q2222W81 24321833 Hasegawa, M; Yasuda, Y; Tanaka, M; Nakata, K; Umeda, E; Wang, Y; Watanabe, C; Uetake, S; Kunoh, T; Shionyu, M; Sasaki, R; Shiina, I; Mizukami, T 1/31/2014 7/25/2014 Institute of Bio-Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51087152 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 11 ChEMBL 10.1016/j.ejmech.2013.11.009 10.7270/Q2222W81 24321833 Hasegawa, M; Yasuda, Y; Tanaka, M; Nakata, K; Umeda, E; Wang, Y; Watanabe, C; Uetake, S; Kunoh, T; Shionyu, M; Sasaki, R; Shiina, I; Mizukami, T 1/31/2014 7/25/2014 Institute of Bio-Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51110847 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 1.000000 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51110850 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 5520 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51110852 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 22100 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51110856 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 4.0 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51110862 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 130 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51110863 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 70 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51227585 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 1.2 ChEMBL 10.1016/j.bmc.2018.12.022 10.7270/Q2NP27P1 30581047 Pehere, AD; Nguyen, S; Garlick, SK; Wilson, DW; Hudson, I; Sykes, MJ; Morton, JD; Abell, AD 1/15/2019 2/18/2021 University of Adelaide http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51289132 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 1450 ChEMBL 10.1021/acsmedchemlett.9b00233 10.7270/Q2930XK7 31312413 Pacifico, S; Ferretti, V; Albanese, V; Fantinati, A; Gallerani, E; Nicoli, F; Gavioli, R; Zamberlan, F; Preti, D; Marastoni, M 7/11/2019 2/24/2021 University of Ferrara http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51289181 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 4590 ChEMBL 10.1021/acsmedchemlett.9b00233 10.7270/Q2930XK7 31312413 Pacifico, S; Ferretti, V; Albanese, V; Fantinati, A; Gallerani, E; Nicoli, F; Gavioli, R; Zamberlan, F; Preti, D; Marastoni, M 7/11/2019 2/24/2021 University of Ferrara http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51289196 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 7.0 ChEMBL 10.1021/acsmedchemlett.9b00233 10.7270/Q2930XK7 31312413 Pacifico, S; Ferretti, V; Albanese, V; Fantinati, A; Gallerani, E; Nicoli, F; Gavioli, R; Zamberlan, F; Preti, D; Marastoni, M 7/11/2019 2/24/2021 University of Ferrara http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51298902 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 30 ChEMBL 10.1016/j.bmc.2019.115161 10.7270/Q29W0JZJ 31732281 Uesugi, S; Honmura, Y; Nishiyama, M; Kusakabe, K; Tonouchi, A; Yamashita, T; Hashimoto, M; Kimura, KI 12/15/2019 2/25/2021 Iwate University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51298906 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 1600 ChEMBL 10.1016/j.bmc.2019.115161 10.7270/Q29W0JZJ 31732281 Uesugi, S; Honmura, Y; Nishiyama, M; Kusakabe, K; Tonouchi, A; Yamashita, T; Hashimoto, M; Kimura, KI 12/15/2019 2/25/2021 Iwate University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51298909 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 500 ChEMBL 10.1016/j.bmc.2019.115161 10.7270/Q29W0JZJ 31732281 Uesugi, S; Honmura, Y; Nishiyama, M; Kusakabe, K; Tonouchi, A; Yamashita, T; Hashimoto, M; Kimura, KI 12/15/2019 2/25/2021 Iwate University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51487773 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 22100 ChEMBL 10.7270/Q20R9TGT 34838650 Ettari, R; Iraci, N; Di Chio, C; Previti, S; Danzè, M; Zappalà, M 1/1/2022 6/23/2023 University of Messina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51487774 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 5520 ChEMBL 10.7270/Q20R9TGT 34838650 Ettari, R; Iraci, N; Di Chio, C; Previti, S; Danzè, M; Zappalà, M 1/1/2022 6/23/2023 University of Messina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51487775 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 1.4 ChEMBL 10.7270/Q20R9TGT 34838650 Ettari, R; Iraci, N; Di Chio, C; Previti, S; Danzè, M; Zappalà, M 1/1/2022 6/23/2023 University of Messina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51487776 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 130 ChEMBL 10.7270/Q20R9TGT 34838650 Ettari, R; Iraci, N; Di Chio, C; Previti, S; Danzè, M; Zappalà, M 1/1/2022 6/23/2023 University of Messina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51487777 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 1.000000 ChEMBL 10.7270/Q20R9TGT 34838650 Ettari, R; Iraci, N; Di Chio, C; Previti, S; Danzè, M; Zappalà, M 1/1/2022 6/23/2023 University of Messina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51159619 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 A5LHX3/O14818/P20618/P25786/P25787/P25788/P25789/P28062/P28065/P28066/P28070/P28072/P28074/P40306/P49720/P49721/P60900/Q8TAA3/Q99436 Homo sapiens 4500 ChEMBL 10.1016/j.bmcl.2005.02.013 10.7270/Q2CF9SVN 15780623 Momose, I; Umezawa, Y; Hirosawa, S; Iinuma, H; Ikeda, D 4/1/2005 8/23/2020 Numazu Bio-Medical Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000077&target=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 19 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 MALLDVCGAPRGQRPESALPVAGSGRRSDPGHYSFSMRSPELALPRGMQPTEFFQSLGGDGERNVQIEMAHGTTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAIAYATHRDSYSGGVVNMYHMKEDGWVKVESTDVSDLLHQYREANQ 6E5B,6AVO,7B12,7AWE Proteasome subunit beta type-8 PSB8_HUMAN P28062 B0UZC0 Q29824 Q5JNW6 Q5QNR8 Q96J48 MLRAGAPTGDLPRAGEVHTGTTIMAVEFDGGVVMGSDSRVSAGEAVVNRVFDKLSPLHERIYCALSGSAADAQAVADMAAYQLELHGIELEEPPLVLAAANVVRNISYKYREDLSAHLMVAGWDQREGGQVYGTLGGMLTRQPFAIGGSGSTFIYGYVDAAYKPGMSPEECRRFTTDAIALAMSRDGSSGGVIYLVTITAAGVDHRVILGNELPKFYDE 6E5B,7B12,7AWE,6AVO,8YVG,8YSX Proteasome subunit beta type-9 PSB9_HUMAN P28065 B0V0T1 Q16523 Q5JNW4 MAATLLAARGAGPAPAWGPEAFTPDWESREVSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDRIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAASLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTANALALAMERDGSSGGVIRLAAIAESGVERQVLLGDQIPKFAVATLPPA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,9RKZ,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6R70,9QVX,6XMJ,4R67,4R3O,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit beta type-6 PSB6_HUMAN P28072 Q96J55 MFRNQYDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSELAAHQKKILHVDNHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGARSQSARTYLERHMSEFMECNLNELVKHGLRALRETLPAEQDLTTKNVSIGIVGKDLEFTIYDDDDVSPFLEGLEERPQRKAQPAQPADEPAEKADEPMEH 9YUZ,9UG9,9UF8,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9VUG,9VUF,9VUE,9U7R,9U3L,9SZV,9SZT,9MBQ,9MBP,9HEU,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,7DRW,7DR7,7DR6,8YVG,8YSX,8QYS,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,5M32,9QVX Proteasome subunit alpha type-1 PSA1_HUMAN P25786 A8K400 Q53YE8 Q9BRV9 MAERGYSFSLTTFSPSGKLVQIEYALAAVAGGAPSVGIKAANGVVLATEKKQKSILYDERSVHKVEPITKHIGLVYSGMGPDYRVLVHRARKLAQQYYLVYQEPIPTAQLVQRVASVMQEYTQSGGVRPFGVSLLICGWNEGRPYLFQSDPSGAYFAWKATAMGKNYVNGKTFLEKRYNEDLELEDAIHTAILTLKESFEGQMTEDNIEVGICNEAGFRRLTPTEVKDYLAAIA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YVG,8YSX,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYS,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,9U7R,9U3L,9MBQ,9MBP,9HMN,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6XMJ,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,4R67,4R3O,22MM,1IRU,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,6R70,9QVX,7B12,7AWE Proteasome subunit alpha type-2 PSA2_HUMAN P25787 Q6ICS6 Q9BU45 MSSIGTGYDLSASTFSPDGRVFQVEYAMKAVENSSTAIGIRCKDGVVFGVEKLVLSKLYEEGSNKRLFNVDRHVGMAVAGLLADARSLADIAREEASNFRSNFGYNIPLKHLADRVAMYVHAYTLYSAVRPFGCSFMLGSYSVNDGAQLYMIDPSGVSYGYWGCAIGKARQAAKTEIEKLQMKEMTCRDIVKEVAKIIYIVHDEVKDKAFELELSWVGELTNGRHEIVPKDIREEAEKYAKESLKEEDESDDDNM 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7E55,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5DSV,5A0Q,9U7R,9U3L,9MBQ,9MBP,9HMN,8FZ6,8FZ5,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7DRW,7DR7,7DR6,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,1IRU,6TU3,6EPF,6EPE,6EPD,6EPC,8YVP,8YPK,3UNH,3UNF,3UNE,3UNB,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,8QYS,6R70,9QVX Proteasome subunit alpha type-3 PSA3_HUMAN P25788 B2RCK6 Q86U83 Q8N1D8 Q9BS70 MSRRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGEMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTRENGKTVIRVLKQKEVEQLIKKHEEEEAKAEREKKEKEQKEKDK 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,7AWE,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,6R70,8QYS,9QVX Proteasome subunit alpha type-4 PSA4_HUMAN P25789 D3DW86 Q53XP2 Q567Q5 Q8TBD1 MFLTRSEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKTLIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGEEDADPGAMSRPFGVALLFGGVDEKGPQLFHMDPSGTFVQCDARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKLNATNIELATVQPGQNFHMFTKEELEEVIKDI 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDI,9NKJ,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8O,9E8N,9E8L,9E8K,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YVP,8YVG,8YSX,8YPK,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QYO,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,22MM,8QZ9,8QYN,8QYM,8QYL,8QYJ,8QYS,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9QVX,6R70,7B12,7AWE Proteasome subunit alpha type-5 PSA5_HUMAN P28066 B2R8F6 B4E2V4 Q3T1C1 Q6IBF7 MSRGSSAGFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITENIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATAAGVKQTESTSFLEKKVKKKFDWTFEQTVETAITCLSTVLSIDFKPSEIEVGVVTVENPKFRILTEAEIDAHLVALAERD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6TU3,6RGQ,6REY,6KWY,6EPF,6EPE,6EPD,6EPC,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,6XMJ,6R70,4R67,4R3O,7B12,7AWE,9QVX,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit alpha type-6 PSA6_HUMAN P60900 B2R7J9 B4DQR4 B4DXJ9 P34062 Q6IB60 MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIGRGAKSVREFLEKNYTDEAIETDDLTIKLVIKALLEVVQSGGKNIELAVMRRDQSLKILNPEEIEKYVAEIEKEKEENEKKKQKKAS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,22MM,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7AWE,6R70,7B12,8QYS,9QVX Proteasome subunit alpha type-7 PSA7_HUMAN O14818 B2R515 Q5JXJ2 Q9BR53 Q9H4K5 Q9UEU8 MASRYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVCMAFAVLTIFIGLTADARVVINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDAIASDSEAIKLAIKALLEVVQSGGKNIELAIIRRNQPLKMFSAKEVELYVTEIEKEKEEAEKKKSKKSV Proteasome subunit alpha-type 8 PSMA8_HUMAN Q8TAA3 B0YJ75 Q8IVP4 Q8TA98 Q8TAA2 MLKPALEPRGGFSFENCQRNASLERVLPGLKVPHARKTGTTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATVTRILRQTLFRYQGHVGASLIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLLVEAVTAGILGDLGSGGNVDACVITKTGAKLLRTLSSPTEPVKRSGRYHFVPGTTAVLTQTVKPLTLELVEETVQAMEVE 6E5B,6AVO,7AWE Proteasome subunit beta type-10 PSB10_HUMAN P40306 B2R5J4 Q5U098 MALQDVCKWQSPDTQGPSPHLPRAGGWAVPRGCDPQTFLQIHGPRLAHGTTTLAFRFRHGVIAAADTRSSCGSYVACPASCKVIPVHQHLLGTTSGTSADCATWYRVLQRELRLRELREGQLPSVASAAKLLSAMMSQYRGLDLCVATALCGWDRSGPELFYVYSDGTRLQGDIFSVGSGSPYAYGVLDRGYRYDMSTQEAYALARCAVAHATHRDAYSGGSVDLFHVRESGWEHVSRSDACVLYVELQKLLEPEPEEDASHAHPEPATAHRAAEDRELSVGPGEVTPGDSRMPAGTETV Proteasome subunit beta type-11 PSB11_HUMAN A5LHX3 MSIMSYNGGAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYTLMSMVANLLYEKRFGPYYTEPVIAGLDPKTFKPFICSLDLIGCPMVTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLFETISQAMLNAVDRDAVSGMGVIVHIIEKDKITTRTLKARMD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QZ9,8QYO,8QYN,8QYM,8QYL,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,9U7R,9U3L,9RKZ,9QVX,9MBQ,9MBP,9HMN,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7B12,7AWE,6XMJ,6WJN,6WJD,6R70,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5T0J,5T0I,5T0H,5T0G,5T0C,5A0Q,4R67,4R3O,22MM,8YVP,8YPK,6TU3,3UNH,3UNF,3UNE,3UNB,8QYS Proteasome subunit beta type-3 PSB3_HUMAN P49720 P31147 Q0P6J7 Q96E27 MEAFLGSRSGLWAGGPAPGQFYRIPSTPDSFMDPASALYRGPITRTQNPMVTGTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNNSTMLGASGDYADFQYLKQVLGQMVIDEELLGDGHSYSPRAIHSWLTRAMYSRRSKMNPLWNTMVIGGYADGESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREVLEKQPVLSQTEARDLVERCMRVLYYRDARSYNRFQIATVTEKGVEIEGPLSTETNWDIAHMISGFE 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9BW4,9BV3,9BV2,9BV1,9BUI,8TM6,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YIZ,8YIY,8YIX,9RKZ,9HMN,8UD9,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,6AVO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,6XMJ,4R67,4R3O,6R70,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,7B12,7AWE,9QVX Proteasome subunit beta type-4 PSB4_HUMAN P28070 B2R9L3 P31148 Q5SZS5 Q6IBI4 Q969L6 MAAVSVYAPPVGGFSFDNCRRNAVLEADFAKRGYKLPKVRKTGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTANRMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAIAAGIFNDLGSGSNIDLCVISKNKLDFLRPYTVPNKKGTRLGRYRCEKGTTAVLTEKITPLEIEVLEETVQTMDTS 8QZ9,8QYN,8QYM,8QYL,8QYJ,9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8TM6,8TM5,8TM4,8QYO,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,9RKZ,9HMN,8UD9,8CVS,8CVR,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,9QVX,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O Proteasome subunit beta type-7 PSB7_HUMAN Q99436 B4E0P1 Q5TBG6 Q96AG8 Q9BWA7 51159624 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 A5LHX3/O14818/P20618/P25786/P25787/P25788/P25789/P28062/P28065/P28066/P28070/P28072/P28074/P40306/P49720/P49721/P60900/Q8TAA3/Q99436 Homo sapiens 1400 ChEMBL 10.1016/j.bmcl.2005.02.013 10.7270/Q2CF9SVN 15780623 Momose, I; Umezawa, Y; Hirosawa, S; Iinuma, H; Ikeda, D 4/1/2005 8/23/2020 Numazu Bio-Medical Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000077&target=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 19 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 MALLDVCGAPRGQRPESALPVAGSGRRSDPGHYSFSMRSPELALPRGMQPTEFFQSLGGDGERNVQIEMAHGTTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAIAYATHRDSYSGGVVNMYHMKEDGWVKVESTDVSDLLHQYREANQ 6E5B,6AVO,7B12,7AWE Proteasome subunit beta type-8 PSB8_HUMAN P28062 B0UZC0 Q29824 Q5JNW6 Q5QNR8 Q96J48 MLRAGAPTGDLPRAGEVHTGTTIMAVEFDGGVVMGSDSRVSAGEAVVNRVFDKLSPLHERIYCALSGSAADAQAVADMAAYQLELHGIELEEPPLVLAAANVVRNISYKYREDLSAHLMVAGWDQREGGQVYGTLGGMLTRQPFAIGGSGSTFIYGYVDAAYKPGMSPEECRRFTTDAIALAMSRDGSSGGVIYLVTITAAGVDHRVILGNELPKFYDE 6E5B,7B12,7AWE,6AVO,8YVG,8YSX Proteasome subunit beta type-9 PSB9_HUMAN P28065 B0V0T1 Q16523 Q5JNW4 MAATLLAARGAGPAPAWGPEAFTPDWESREVSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDRIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAASLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTANALALAMERDGSSGGVIRLAAIAESGVERQVLLGDQIPKFAVATLPPA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,9RKZ,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6R70,9QVX,6XMJ,4R67,4R3O,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit beta type-6 PSB6_HUMAN P28072 Q96J55 MFRNQYDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSELAAHQKKILHVDNHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGARSQSARTYLERHMSEFMECNLNELVKHGLRALRETLPAEQDLTTKNVSIGIVGKDLEFTIYDDDDVSPFLEGLEERPQRKAQPAQPADEPAEKADEPMEH 9YUZ,9UG9,9UF8,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9VUG,9VUF,9VUE,9U7R,9U3L,9SZV,9SZT,9MBQ,9MBP,9HEU,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,7DRW,7DR7,7DR6,8YVG,8YSX,8QYS,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,5M32,9QVX Proteasome subunit alpha type-1 PSA1_HUMAN P25786 A8K400 Q53YE8 Q9BRV9 MAERGYSFSLTTFSPSGKLVQIEYALAAVAGGAPSVGIKAANGVVLATEKKQKSILYDERSVHKVEPITKHIGLVYSGMGPDYRVLVHRARKLAQQYYLVYQEPIPTAQLVQRVASVMQEYTQSGGVRPFGVSLLICGWNEGRPYLFQSDPSGAYFAWKATAMGKNYVNGKTFLEKRYNEDLELEDAIHTAILTLKESFEGQMTEDNIEVGICNEAGFRRLTPTEVKDYLAAIA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YVG,8YSX,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYS,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,9U7R,9U3L,9MBQ,9MBP,9HMN,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6XMJ,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,4R67,4R3O,22MM,1IRU,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,6R70,9QVX,7B12,7AWE Proteasome subunit alpha type-2 PSA2_HUMAN P25787 Q6ICS6 Q9BU45 MSSIGTGYDLSASTFSPDGRVFQVEYAMKAVENSSTAIGIRCKDGVVFGVEKLVLSKLYEEGSNKRLFNVDRHVGMAVAGLLADARSLADIAREEASNFRSNFGYNIPLKHLADRVAMYVHAYTLYSAVRPFGCSFMLGSYSVNDGAQLYMIDPSGVSYGYWGCAIGKARQAAKTEIEKLQMKEMTCRDIVKEVAKIIYIVHDEVKDKAFELELSWVGELTNGRHEIVPKDIREEAEKYAKESLKEEDESDDDNM 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7E55,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5DSV,5A0Q,9U7R,9U3L,9MBQ,9MBP,9HMN,8FZ6,8FZ5,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7DRW,7DR7,7DR6,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,1IRU,6TU3,6EPF,6EPE,6EPD,6EPC,8YVP,8YPK,3UNH,3UNF,3UNE,3UNB,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,8QYS,6R70,9QVX Proteasome subunit alpha type-3 PSA3_HUMAN P25788 B2RCK6 Q86U83 Q8N1D8 Q9BS70 MSRRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGEMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTRENGKTVIRVLKQKEVEQLIKKHEEEEAKAEREKKEKEQKEKDK 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,7AWE,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,6R70,8QYS,9QVX Proteasome subunit alpha type-4 PSA4_HUMAN P25789 D3DW86 Q53XP2 Q567Q5 Q8TBD1 MFLTRSEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKTLIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGEEDADPGAMSRPFGVALLFGGVDEKGPQLFHMDPSGTFVQCDARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKLNATNIELATVQPGQNFHMFTKEELEEVIKDI 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDI,9NKJ,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8O,9E8N,9E8L,9E8K,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YVP,8YVG,8YSX,8YPK,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QYO,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,22MM,8QZ9,8QYN,8QYM,8QYL,8QYJ,8QYS,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9QVX,6R70,7B12,7AWE Proteasome subunit alpha type-5 PSA5_HUMAN P28066 B2R8F6 B4E2V4 Q3T1C1 Q6IBF7 MSRGSSAGFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITENIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATAAGVKQTESTSFLEKKVKKKFDWTFEQTVETAITCLSTVLSIDFKPSEIEVGVVTVENPKFRILTEAEIDAHLVALAERD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6TU3,6RGQ,6REY,6KWY,6EPF,6EPE,6EPD,6EPC,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,6XMJ,6R70,4R67,4R3O,7B12,7AWE,9QVX,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit alpha type-6 PSA6_HUMAN P60900 B2R7J9 B4DQR4 B4DXJ9 P34062 Q6IB60 MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIGRGAKSVREFLEKNYTDEAIETDDLTIKLVIKALLEVVQSGGKNIELAVMRRDQSLKILNPEEIEKYVAEIEKEKEENEKKKQKKAS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,22MM,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7AWE,6R70,7B12,8QYS,9QVX Proteasome subunit alpha type-7 PSA7_HUMAN O14818 B2R515 Q5JXJ2 Q9BR53 Q9H4K5 Q9UEU8 MASRYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVCMAFAVLTIFIGLTADARVVINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDAIASDSEAIKLAIKALLEVVQSGGKNIELAIIRRNQPLKMFSAKEVELYVTEIEKEKEEAEKKKSKKSV Proteasome subunit alpha-type 8 PSMA8_HUMAN Q8TAA3 B0YJ75 Q8IVP4 Q8TA98 Q8TAA2 MLKPALEPRGGFSFENCQRNASLERVLPGLKVPHARKTGTTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATVTRILRQTLFRYQGHVGASLIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLLVEAVTAGILGDLGSGGNVDACVITKTGAKLLRTLSSPTEPVKRSGRYHFVPGTTAVLTQTVKPLTLELVEETVQAMEVE 6E5B,6AVO,7AWE Proteasome subunit beta type-10 PSB10_HUMAN P40306 B2R5J4 Q5U098 MALQDVCKWQSPDTQGPSPHLPRAGGWAVPRGCDPQTFLQIHGPRLAHGTTTLAFRFRHGVIAAADTRSSCGSYVACPASCKVIPVHQHLLGTTSGTSADCATWYRVLQRELRLRELREGQLPSVASAAKLLSAMMSQYRGLDLCVATALCGWDRSGPELFYVYSDGTRLQGDIFSVGSGSPYAYGVLDRGYRYDMSTQEAYALARCAVAHATHRDAYSGGSVDLFHVRESGWEHVSRSDACVLYVELQKLLEPEPEEDASHAHPEPATAHRAAEDRELSVGPGEVTPGDSRMPAGTETV Proteasome subunit beta type-11 PSB11_HUMAN A5LHX3 MSIMSYNGGAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYTLMSMVANLLYEKRFGPYYTEPVIAGLDPKTFKPFICSLDLIGCPMVTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLFETISQAMLNAVDRDAVSGMGVIVHIIEKDKITTRTLKARMD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QZ9,8QYO,8QYN,8QYM,8QYL,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,9U7R,9U3L,9RKZ,9QVX,9MBQ,9MBP,9HMN,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7B12,7AWE,6XMJ,6WJN,6WJD,6R70,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5T0J,5T0I,5T0H,5T0G,5T0C,5A0Q,4R67,4R3O,22MM,8YVP,8YPK,6TU3,3UNH,3UNF,3UNE,3UNB,8QYS Proteasome subunit beta type-3 PSB3_HUMAN P49720 P31147 Q0P6J7 Q96E27 MEAFLGSRSGLWAGGPAPGQFYRIPSTPDSFMDPASALYRGPITRTQNPMVTGTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNNSTMLGASGDYADFQYLKQVLGQMVIDEELLGDGHSYSPRAIHSWLTRAMYSRRSKMNPLWNTMVIGGYADGESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREVLEKQPVLSQTEARDLVERCMRVLYYRDARSYNRFQIATVTEKGVEIEGPLSTETNWDIAHMISGFE 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9BW4,9BV3,9BV2,9BV1,9BUI,8TM6,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YIZ,8YIY,8YIX,9RKZ,9HMN,8UD9,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,6AVO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,6XMJ,4R67,4R3O,6R70,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,7B12,7AWE,9QVX Proteasome subunit beta type-4 PSB4_HUMAN P28070 B2R9L3 P31148 Q5SZS5 Q6IBI4 Q969L6 MAAVSVYAPPVGGFSFDNCRRNAVLEADFAKRGYKLPKVRKTGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTANRMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAIAAGIFNDLGSGSNIDLCVISKNKLDFLRPYTVPNKKGTRLGRYRCEKGTTAVLTEKITPLEIEVLEETVQTMDTS 8QZ9,8QYN,8QYM,8QYL,8QYJ,9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8TM6,8TM5,8TM4,8QYO,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,9RKZ,9HMN,8UD9,8CVS,8CVR,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,9QVX,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O Proteasome subunit beta type-7 PSB7_HUMAN Q99436 B4E0P1 Q5TBG6 Q96AG8 Q9BWA7 51159634 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 A5LHX3/O14818/P20618/P25786/P25787/P25788/P25789/P28062/P28065/P28066/P28070/P28072/P28074/P40306/P49720/P49721/P60900/Q8TAA3/Q99436 Homo sapiens 68 ChEMBL 10.1016/j.bmcl.2005.02.013 10.7270/Q2CF9SVN 15780623 Momose, I; Umezawa, Y; Hirosawa, S; Iinuma, H; Ikeda, D 4/1/2005 8/23/2020 Numazu Bio-Medical Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000077&target=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 19 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 MALLDVCGAPRGQRPESALPVAGSGRRSDPGHYSFSMRSPELALPRGMQPTEFFQSLGGDGERNVQIEMAHGTTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAIAYATHRDSYSGGVVNMYHMKEDGWVKVESTDVSDLLHQYREANQ 6E5B,6AVO,7B12,7AWE Proteasome subunit beta type-8 PSB8_HUMAN P28062 B0UZC0 Q29824 Q5JNW6 Q5QNR8 Q96J48 MLRAGAPTGDLPRAGEVHTGTTIMAVEFDGGVVMGSDSRVSAGEAVVNRVFDKLSPLHERIYCALSGSAADAQAVADMAAYQLELHGIELEEPPLVLAAANVVRNISYKYREDLSAHLMVAGWDQREGGQVYGTLGGMLTRQPFAIGGSGSTFIYGYVDAAYKPGMSPEECRRFTTDAIALAMSRDGSSGGVIYLVTITAAGVDHRVILGNELPKFYDE 6E5B,7B12,7AWE,6AVO,8YVG,8YSX Proteasome subunit beta type-9 PSB9_HUMAN P28065 B0V0T1 Q16523 Q5JNW4 MAATLLAARGAGPAPAWGPEAFTPDWESREVSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDRIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAASLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTANALALAMERDGSSGGVIRLAAIAESGVERQVLLGDQIPKFAVATLPPA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,9RKZ,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6R70,9QVX,6XMJ,4R67,4R3O,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit beta type-6 PSB6_HUMAN P28072 Q96J55 MFRNQYDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSELAAHQKKILHVDNHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGARSQSARTYLERHMSEFMECNLNELVKHGLRALRETLPAEQDLTTKNVSIGIVGKDLEFTIYDDDDVSPFLEGLEERPQRKAQPAQPADEPAEKADEPMEH 9YUZ,9UG9,9UF8,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9VUG,9VUF,9VUE,9U7R,9U3L,9SZV,9SZT,9MBQ,9MBP,9HEU,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,7DRW,7DR7,7DR6,8YVG,8YSX,8QYS,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,5M32,9QVX Proteasome subunit alpha type-1 PSA1_HUMAN P25786 A8K400 Q53YE8 Q9BRV9 MAERGYSFSLTTFSPSGKLVQIEYALAAVAGGAPSVGIKAANGVVLATEKKQKSILYDERSVHKVEPITKHIGLVYSGMGPDYRVLVHRARKLAQQYYLVYQEPIPTAQLVQRVASVMQEYTQSGGVRPFGVSLLICGWNEGRPYLFQSDPSGAYFAWKATAMGKNYVNGKTFLEKRYNEDLELEDAIHTAILTLKESFEGQMTEDNIEVGICNEAGFRRLTPTEVKDYLAAIA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YVG,8YSX,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYS,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,9U7R,9U3L,9MBQ,9MBP,9HMN,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6XMJ,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,4R67,4R3O,22MM,1IRU,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,6R70,9QVX,7B12,7AWE Proteasome subunit alpha type-2 PSA2_HUMAN P25787 Q6ICS6 Q9BU45 MSSIGTGYDLSASTFSPDGRVFQVEYAMKAVENSSTAIGIRCKDGVVFGVEKLVLSKLYEEGSNKRLFNVDRHVGMAVAGLLADARSLADIAREEASNFRSNFGYNIPLKHLADRVAMYVHAYTLYSAVRPFGCSFMLGSYSVNDGAQLYMIDPSGVSYGYWGCAIGKARQAAKTEIEKLQMKEMTCRDIVKEVAKIIYIVHDEVKDKAFELELSWVGELTNGRHEIVPKDIREEAEKYAKESLKEEDESDDDNM 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7E55,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5DSV,5A0Q,9U7R,9U3L,9MBQ,9MBP,9HMN,8FZ6,8FZ5,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7DRW,7DR7,7DR6,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,1IRU,6TU3,6EPF,6EPE,6EPD,6EPC,8YVP,8YPK,3UNH,3UNF,3UNE,3UNB,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,8QYS,6R70,9QVX Proteasome subunit alpha type-3 PSA3_HUMAN P25788 B2RCK6 Q86U83 Q8N1D8 Q9BS70 MSRRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGEMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTRENGKTVIRVLKQKEVEQLIKKHEEEEAKAEREKKEKEQKEKDK 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,7AWE,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,6R70,8QYS,9QVX Proteasome subunit alpha type-4 PSA4_HUMAN P25789 D3DW86 Q53XP2 Q567Q5 Q8TBD1 MFLTRSEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKTLIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGEEDADPGAMSRPFGVALLFGGVDEKGPQLFHMDPSGTFVQCDARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKLNATNIELATVQPGQNFHMFTKEELEEVIKDI 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDI,9NKJ,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8O,9E8N,9E8L,9E8K,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YVP,8YVG,8YSX,8YPK,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QYO,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,22MM,8QZ9,8QYN,8QYM,8QYL,8QYJ,8QYS,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9QVX,6R70,7B12,7AWE Proteasome subunit alpha type-5 PSA5_HUMAN P28066 B2R8F6 B4E2V4 Q3T1C1 Q6IBF7 MSRGSSAGFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITENIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATAAGVKQTESTSFLEKKVKKKFDWTFEQTVETAITCLSTVLSIDFKPSEIEVGVVTVENPKFRILTEAEIDAHLVALAERD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6TU3,6RGQ,6REY,6KWY,6EPF,6EPE,6EPD,6EPC,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,6XMJ,6R70,4R67,4R3O,7B12,7AWE,9QVX,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit alpha type-6 PSA6_HUMAN P60900 B2R7J9 B4DQR4 B4DXJ9 P34062 Q6IB60 MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIGRGAKSVREFLEKNYTDEAIETDDLTIKLVIKALLEVVQSGGKNIELAVMRRDQSLKILNPEEIEKYVAEIEKEKEENEKKKQKKAS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,22MM,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7AWE,6R70,7B12,8QYS,9QVX Proteasome subunit alpha type-7 PSA7_HUMAN O14818 B2R515 Q5JXJ2 Q9BR53 Q9H4K5 Q9UEU8 MASRYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVCMAFAVLTIFIGLTADARVVINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDAIASDSEAIKLAIKALLEVVQSGGKNIELAIIRRNQPLKMFSAKEVELYVTEIEKEKEEAEKKKSKKSV Proteasome subunit alpha-type 8 PSMA8_HUMAN Q8TAA3 B0YJ75 Q8IVP4 Q8TA98 Q8TAA2 MLKPALEPRGGFSFENCQRNASLERVLPGLKVPHARKTGTTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATVTRILRQTLFRYQGHVGASLIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLLVEAVTAGILGDLGSGGNVDACVITKTGAKLLRTLSSPTEPVKRSGRYHFVPGTTAVLTQTVKPLTLELVEETVQAMEVE 6E5B,6AVO,7AWE Proteasome subunit beta type-10 PSB10_HUMAN P40306 B2R5J4 Q5U098 MALQDVCKWQSPDTQGPSPHLPRAGGWAVPRGCDPQTFLQIHGPRLAHGTTTLAFRFRHGVIAAADTRSSCGSYVACPASCKVIPVHQHLLGTTSGTSADCATWYRVLQRELRLRELREGQLPSVASAAKLLSAMMSQYRGLDLCVATALCGWDRSGPELFYVYSDGTRLQGDIFSVGSGSPYAYGVLDRGYRYDMSTQEAYALARCAVAHATHRDAYSGGSVDLFHVRESGWEHVSRSDACVLYVELQKLLEPEPEEDASHAHPEPATAHRAAEDRELSVGPGEVTPGDSRMPAGTETV Proteasome subunit beta type-11 PSB11_HUMAN A5LHX3 MSIMSYNGGAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYTLMSMVANLLYEKRFGPYYTEPVIAGLDPKTFKPFICSLDLIGCPMVTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLFETISQAMLNAVDRDAVSGMGVIVHIIEKDKITTRTLKARMD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QZ9,8QYO,8QYN,8QYM,8QYL,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,9U7R,9U3L,9RKZ,9QVX,9MBQ,9MBP,9HMN,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7B12,7AWE,6XMJ,6WJN,6WJD,6R70,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5T0J,5T0I,5T0H,5T0G,5T0C,5A0Q,4R67,4R3O,22MM,8YVP,8YPK,6TU3,3UNH,3UNF,3UNE,3UNB,8QYS Proteasome subunit beta type-3 PSB3_HUMAN P49720 P31147 Q0P6J7 Q96E27 MEAFLGSRSGLWAGGPAPGQFYRIPSTPDSFMDPASALYRGPITRTQNPMVTGTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNNSTMLGASGDYADFQYLKQVLGQMVIDEELLGDGHSYSPRAIHSWLTRAMYSRRSKMNPLWNTMVIGGYADGESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREVLEKQPVLSQTEARDLVERCMRVLYYRDARSYNRFQIATVTEKGVEIEGPLSTETNWDIAHMISGFE 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9BW4,9BV3,9BV2,9BV1,9BUI,8TM6,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YIZ,8YIY,8YIX,9RKZ,9HMN,8UD9,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,6AVO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,6XMJ,4R67,4R3O,6R70,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,7B12,7AWE,9QVX Proteasome subunit beta type-4 PSB4_HUMAN P28070 B2R9L3 P31148 Q5SZS5 Q6IBI4 Q969L6 MAAVSVYAPPVGGFSFDNCRRNAVLEADFAKRGYKLPKVRKTGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTANRMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAIAAGIFNDLGSGSNIDLCVISKNKLDFLRPYTVPNKKGTRLGRYRCEKGTTAVLTEKITPLEIEVLEETVQTMDTS 8QZ9,8QYN,8QYM,8QYL,8QYJ,9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8TM6,8TM5,8TM4,8QYO,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,9RKZ,9HMN,8UD9,8CVS,8CVR,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,9QVX,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O Proteasome subunit beta type-7 PSB7_HUMAN Q99436 B4E0P1 Q5TBG6 Q96AG8 Q9BWA7 50028847 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 120 ChEMBL 10.1021/jm00213a022 10.7270/Q26977R0 576620 Song, R; Qiao, W; He, J; Huang, J; Luo, Y; Yang, T 3/25/2021 4/18/2024 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 50029539 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 1080 ChEMBL 10.1021/jm00213a022 10.7270/Q26977R0 576620 Song, R; Qiao, W; He, J; Huang, J; Luo, Y; Yang, T 3/25/2021 4/18/2024 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 50029543 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 1.2 ChEMBL 10.1021/jm00213a022 10.7270/Q26977R0 576620 Song, R; Qiao, W; He, J; Huang, J; Luo, Y; Yang, T 3/25/2021 4/18/2024 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 50494739 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 37 ChEMBL 10.1016/j.bmcl.2016.04.067 10.7270/Q2N018GG 27158142 Yang, L; Wang, W; Sun, Q; Xu, F; Niu, Y; Wang, C; Liang, L; Xu, P 6/15/2016 8/25/2017 Peking University Health Science Center http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 50494751 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 44 ChEMBL 10.1016/j.bmcl.2016.04.067 10.7270/Q2N018GG 27158142 Yang, L; Wang, W; Sun, Q; Xu, F; Niu, Y; Wang, C; Liang, L; Xu, P 6/15/2016 8/25/2017 Peking University Health Science Center http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 50494763 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 52 ChEMBL 10.1016/j.bmcl.2016.04.067 10.7270/Q2N018GG 27158142 Yang, L; Wang, W; Sun, Q; Xu, F; Niu, Y; Wang, C; Liang, L; Xu, P 6/15/2016 8/25/2017 Peking University Health Science Center http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 50521882 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 1.4 ChEMBL 10.1016/j.ejmech.2016.05.049 10.7270/Q28C9Z6K 27318981 Di Giovanni, C; Ettari, R; Sarno, S; Rotondo, A; Bitto, A; Squadrito, F; Altavilla, D; Schirmeister, T; Novellino, E; Grasso, S; Zappalà, M; Lavecchia, A 10/4/2016 7/10/2018 University of Naples Federico Ii http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 50521890 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 22100 ChEMBL 10.1016/j.ejmech.2016.05.049 10.7270/Q28C9Z6K 27318981 Di Giovanni, C; Ettari, R; Sarno, S; Rotondo, A; Bitto, A; Squadrito, F; Altavilla, D; Schirmeister, T; Novellino, E; Grasso, S; Zappalà, M; Lavecchia, A 10/4/2016 7/10/2018 University of Naples Federico Ii http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 50521891 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 5520 ChEMBL 10.1016/j.ejmech.2016.05.049 10.7270/Q28C9Z6K 27318981 Di Giovanni, C; Ettari, R; Sarno, S; Rotondo, A; Bitto, A; Squadrito, F; Altavilla, D; Schirmeister, T; Novellino, E; Grasso, S; Zappalà, M; Lavecchia, A 10/4/2016 7/10/2018 University of Naples Federico Ii http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 50711335 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 25 ChEMBL 10.1016/j.ejmech.2016.11.024 10.7270/Q2Z03BDZ 27889629 Qin, JM; Huang, RZ; Yao, GY; Liao, ZX; Pan, YM; Wang, HS 1/27/2017 6/17/2019 Guangxi Normal University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51002658 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 470 ChEMBL 10.1021/jm058289o 10.7270/Q2FF3S0S 16686537 Rydzewski, RM; Burrill, L; Mendonca, R; Palmer, JT; Rice, M; Tahilramani, R; Bass, KE; Leung, L; Gjerstad, E; Janc, JW; Pan, L 5/11/2006 11/10/2009 Celera http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51002662 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 3.7 ChEMBL 10.1021/jm058289o 10.7270/Q2FF3S0S 16686537 Rydzewski, RM; Burrill, L; Mendonca, R; Palmer, JT; Rice, M; Tahilramani, R; Bass, KE; Leung, L; Gjerstad, E; Janc, JW; Pan, L 5/11/2006 11/10/2009 Celera http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51002664 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 330 ChEMBL 10.1021/jm058289o 10.7270/Q2FF3S0S 16686537 Rydzewski, RM; Burrill, L; Mendonca, R; Palmer, JT; Rice, M; Tahilramani, R; Bass, KE; Leung, L; Gjerstad, E; Janc, JW; Pan, L 5/11/2006 11/10/2009 Celera http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51087096 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 2100 ChEMBL 10.1016/j.ejmech.2013.11.009 10.7270/Q2222W81 24321833 Hasegawa, M; Yasuda, Y; Tanaka, M; Nakata, K; Umeda, E; Wang, Y; Watanabe, C; Uetake, S; Kunoh, T; Shionyu, M; Sasaki, R; Shiina, I; Mizukami, T 1/31/2014 7/25/2014 Institute of Bio-Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51087151 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 120 ChEMBL 10.1016/j.ejmech.2013.11.009 10.7270/Q2222W81 24321833 Hasegawa, M; Yasuda, Y; Tanaka, M; Nakata, K; Umeda, E; Wang, Y; Watanabe, C; Uetake, S; Kunoh, T; Shionyu, M; Sasaki, R; Shiina, I; Mizukami, T 1/31/2014 7/25/2014 Institute of Bio-Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51087152 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 11 ChEMBL 10.1016/j.ejmech.2013.11.009 10.7270/Q2222W81 24321833 Hasegawa, M; Yasuda, Y; Tanaka, M; Nakata, K; Umeda, E; Wang, Y; Watanabe, C; Uetake, S; Kunoh, T; Shionyu, M; Sasaki, R; Shiina, I; Mizukami, T 1/31/2014 7/25/2014 Institute of Bio-Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51110847 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 1.000000 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51110850 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 5520 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51110852 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 22100 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51110856 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 4.0 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51110862 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 130 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51110863 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 70 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51227585 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 1.2 ChEMBL 10.1016/j.bmc.2018.12.022 10.7270/Q2NP27P1 30581047 Pehere, AD; Nguyen, S; Garlick, SK; Wilson, DW; Hudson, I; Sykes, MJ; Morton, JD; Abell, AD 1/15/2019 2/18/2021 University of Adelaide http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51289132 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 1450 ChEMBL 10.1021/acsmedchemlett.9b00233 10.7270/Q2930XK7 31312413 Pacifico, S; Ferretti, V; Albanese, V; Fantinati, A; Gallerani, E; Nicoli, F; Gavioli, R; Zamberlan, F; Preti, D; Marastoni, M 7/11/2019 2/24/2021 University of Ferrara http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51289181 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 4590 ChEMBL 10.1021/acsmedchemlett.9b00233 10.7270/Q2930XK7 31312413 Pacifico, S; Ferretti, V; Albanese, V; Fantinati, A; Gallerani, E; Nicoli, F; Gavioli, R; Zamberlan, F; Preti, D; Marastoni, M 7/11/2019 2/24/2021 University of Ferrara http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51289196 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 7.0 ChEMBL 10.1021/acsmedchemlett.9b00233 10.7270/Q2930XK7 31312413 Pacifico, S; Ferretti, V; Albanese, V; Fantinati, A; Gallerani, E; Nicoli, F; Gavioli, R; Zamberlan, F; Preti, D; Marastoni, M 7/11/2019 2/24/2021 University of Ferrara http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51298902 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 30 ChEMBL 10.1016/j.bmc.2019.115161 10.7270/Q29W0JZJ 31732281 Uesugi, S; Honmura, Y; Nishiyama, M; Kusakabe, K; Tonouchi, A; Yamashita, T; Hashimoto, M; Kimura, KI 12/15/2019 2/25/2021 Iwate University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51298906 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 1600 ChEMBL 10.1016/j.bmc.2019.115161 10.7270/Q29W0JZJ 31732281 Uesugi, S; Honmura, Y; Nishiyama, M; Kusakabe, K; Tonouchi, A; Yamashita, T; Hashimoto, M; Kimura, KI 12/15/2019 2/25/2021 Iwate University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51298909 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 500 ChEMBL 10.1016/j.bmc.2019.115161 10.7270/Q29W0JZJ 31732281 Uesugi, S; Honmura, Y; Nishiyama, M; Kusakabe, K; Tonouchi, A; Yamashita, T; Hashimoto, M; Kimura, KI 12/15/2019 2/25/2021 Iwate University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51487773 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 22100 ChEMBL 10.7270/Q20R9TGT 34838650 Ettari, R; Iraci, N; Di Chio, C; Previti, S; Danzè, M; Zappalà, M 1/1/2022 6/23/2023 University of Messina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51487774 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 5520 ChEMBL 10.7270/Q20R9TGT 34838650 Ettari, R; Iraci, N; Di Chio, C; Previti, S; Danzè, M; Zappalà, M 1/1/2022 6/23/2023 University of Messina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51487775 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 1.4 ChEMBL 10.7270/Q20R9TGT 34838650 Ettari, R; Iraci, N; Di Chio, C; Previti, S; Danzè, M; Zappalà, M 1/1/2022 6/23/2023 University of Messina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51487776 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 130 ChEMBL 10.7270/Q20R9TGT 34838650 Ettari, R; Iraci, N; Di Chio, C; Previti, S; Danzè, M; Zappalà, M 1/1/2022 6/23/2023 University of Messina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51487777 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 1.000000 ChEMBL 10.7270/Q20R9TGT 34838650 Ettari, R; Iraci, N; Di Chio, C; Previti, S; Danzè, M; Zappalà, M 1/1/2022 6/23/2023 University of Messina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51159619 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 A5LHX3/O14818/P20618/P25786/P25787/P25788/P25789/P28062/P28065/P28066/P28070/P28072/P28074/P40306/P49720/P49721/P60900/Q8TAA3/Q99436 Homo sapiens 4500 ChEMBL 10.1016/j.bmcl.2005.02.013 10.7270/Q2CF9SVN 15780623 Momose, I; Umezawa, Y; Hirosawa, S; Iinuma, H; Ikeda, D 4/1/2005 8/23/2020 Numazu Bio-Medical Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000077&target=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 19 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 MALLDVCGAPRGQRPESALPVAGSGRRSDPGHYSFSMRSPELALPRGMQPTEFFQSLGGDGERNVQIEMAHGTTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAIAYATHRDSYSGGVVNMYHMKEDGWVKVESTDVSDLLHQYREANQ 6E5B,6AVO,7B12,7AWE Proteasome subunit beta type-8 PSB8_HUMAN P28062 B0UZC0 Q29824 Q5JNW6 Q5QNR8 Q96J48 MLRAGAPTGDLPRAGEVHTGTTIMAVEFDGGVVMGSDSRVSAGEAVVNRVFDKLSPLHERIYCALSGSAADAQAVADMAAYQLELHGIELEEPPLVLAAANVVRNISYKYREDLSAHLMVAGWDQREGGQVYGTLGGMLTRQPFAIGGSGSTFIYGYVDAAYKPGMSPEECRRFTTDAIALAMSRDGSSGGVIYLVTITAAGVDHRVILGNELPKFYDE 6E5B,7B12,7AWE,6AVO,8YVG,8YSX Proteasome subunit beta type-9 PSB9_HUMAN P28065 B0V0T1 Q16523 Q5JNW4 MAATLLAARGAGPAPAWGPEAFTPDWESREVSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDRIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAASLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTANALALAMERDGSSGGVIRLAAIAESGVERQVLLGDQIPKFAVATLPPA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,9RKZ,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6R70,9QVX,6XMJ,4R67,4R3O,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit beta type-6 PSB6_HUMAN P28072 Q96J55 MFRNQYDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSELAAHQKKILHVDNHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGARSQSARTYLERHMSEFMECNLNELVKHGLRALRETLPAEQDLTTKNVSIGIVGKDLEFTIYDDDDVSPFLEGLEERPQRKAQPAQPADEPAEKADEPMEH 9YUZ,9UG9,9UF8,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9VUG,9VUF,9VUE,9U7R,9U3L,9SZV,9SZT,9MBQ,9MBP,9HEU,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,7DRW,7DR7,7DR6,8YVG,8YSX,8QYS,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,5M32,9QVX Proteasome subunit alpha type-1 PSA1_HUMAN P25786 A8K400 Q53YE8 Q9BRV9 MAERGYSFSLTTFSPSGKLVQIEYALAAVAGGAPSVGIKAANGVVLATEKKQKSILYDERSVHKVEPITKHIGLVYSGMGPDYRVLVHRARKLAQQYYLVYQEPIPTAQLVQRVASVMQEYTQSGGVRPFGVSLLICGWNEGRPYLFQSDPSGAYFAWKATAMGKNYVNGKTFLEKRYNEDLELEDAIHTAILTLKESFEGQMTEDNIEVGICNEAGFRRLTPTEVKDYLAAIA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YVG,8YSX,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYS,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,9U7R,9U3L,9MBQ,9MBP,9HMN,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6XMJ,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,4R67,4R3O,22MM,1IRU,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,6R70,9QVX,7B12,7AWE Proteasome subunit alpha type-2 PSA2_HUMAN P25787 Q6ICS6 Q9BU45 MSSIGTGYDLSASTFSPDGRVFQVEYAMKAVENSSTAIGIRCKDGVVFGVEKLVLSKLYEEGSNKRLFNVDRHVGMAVAGLLADARSLADIAREEASNFRSNFGYNIPLKHLADRVAMYVHAYTLYSAVRPFGCSFMLGSYSVNDGAQLYMIDPSGVSYGYWGCAIGKARQAAKTEIEKLQMKEMTCRDIVKEVAKIIYIVHDEVKDKAFELELSWVGELTNGRHEIVPKDIREEAEKYAKESLKEEDESDDDNM 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7E55,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5DSV,5A0Q,9U7R,9U3L,9MBQ,9MBP,9HMN,8FZ6,8FZ5,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7DRW,7DR7,7DR6,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,1IRU,6TU3,6EPF,6EPE,6EPD,6EPC,8YVP,8YPK,3UNH,3UNF,3UNE,3UNB,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,8QYS,6R70,9QVX Proteasome subunit alpha type-3 PSA3_HUMAN P25788 B2RCK6 Q86U83 Q8N1D8 Q9BS70 MSRRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGEMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTRENGKTVIRVLKQKEVEQLIKKHEEEEAKAEREKKEKEQKEKDK 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,7AWE,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,6R70,8QYS,9QVX Proteasome subunit alpha type-4 PSA4_HUMAN P25789 D3DW86 Q53XP2 Q567Q5 Q8TBD1 MFLTRSEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKTLIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGEEDADPGAMSRPFGVALLFGGVDEKGPQLFHMDPSGTFVQCDARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKLNATNIELATVQPGQNFHMFTKEELEEVIKDI 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDI,9NKJ,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8O,9E8N,9E8L,9E8K,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YVP,8YVG,8YSX,8YPK,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QYO,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,22MM,8QZ9,8QYN,8QYM,8QYL,8QYJ,8QYS,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9QVX,6R70,7B12,7AWE Proteasome subunit alpha type-5 PSA5_HUMAN P28066 B2R8F6 B4E2V4 Q3T1C1 Q6IBF7 MSRGSSAGFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITENIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATAAGVKQTESTSFLEKKVKKKFDWTFEQTVETAITCLSTVLSIDFKPSEIEVGVVTVENPKFRILTEAEIDAHLVALAERD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6TU3,6RGQ,6REY,6KWY,6EPF,6EPE,6EPD,6EPC,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,6XMJ,6R70,4R67,4R3O,7B12,7AWE,9QVX,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit alpha type-6 PSA6_HUMAN P60900 B2R7J9 B4DQR4 B4DXJ9 P34062 Q6IB60 MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIGRGAKSVREFLEKNYTDEAIETDDLTIKLVIKALLEVVQSGGKNIELAVMRRDQSLKILNPEEIEKYVAEIEKEKEENEKKKQKKAS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,22MM,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7AWE,6R70,7B12,8QYS,9QVX Proteasome subunit alpha type-7 PSA7_HUMAN O14818 B2R515 Q5JXJ2 Q9BR53 Q9H4K5 Q9UEU8 MASRYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVCMAFAVLTIFIGLTADARVVINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDAIASDSEAIKLAIKALLEVVQSGGKNIELAIIRRNQPLKMFSAKEVELYVTEIEKEKEEAEKKKSKKSV Proteasome subunit alpha-type 8 PSMA8_HUMAN Q8TAA3 B0YJ75 Q8IVP4 Q8TA98 Q8TAA2 MLKPALEPRGGFSFENCQRNASLERVLPGLKVPHARKTGTTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATVTRILRQTLFRYQGHVGASLIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLLVEAVTAGILGDLGSGGNVDACVITKTGAKLLRTLSSPTEPVKRSGRYHFVPGTTAVLTQTVKPLTLELVEETVQAMEVE 6E5B,6AVO,7AWE Proteasome subunit beta type-10 PSB10_HUMAN P40306 B2R5J4 Q5U098 MALQDVCKWQSPDTQGPSPHLPRAGGWAVPRGCDPQTFLQIHGPRLAHGTTTLAFRFRHGVIAAADTRSSCGSYVACPASCKVIPVHQHLLGTTSGTSADCATWYRVLQRELRLRELREGQLPSVASAAKLLSAMMSQYRGLDLCVATALCGWDRSGPELFYVYSDGTRLQGDIFSVGSGSPYAYGVLDRGYRYDMSTQEAYALARCAVAHATHRDAYSGGSVDLFHVRESGWEHVSRSDACVLYVELQKLLEPEPEEDASHAHPEPATAHRAAEDRELSVGPGEVTPGDSRMPAGTETV Proteasome subunit beta type-11 PSB11_HUMAN A5LHX3 MSIMSYNGGAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYTLMSMVANLLYEKRFGPYYTEPVIAGLDPKTFKPFICSLDLIGCPMVTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLFETISQAMLNAVDRDAVSGMGVIVHIIEKDKITTRTLKARMD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QZ9,8QYO,8QYN,8QYM,8QYL,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,9U7R,9U3L,9RKZ,9QVX,9MBQ,9MBP,9HMN,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7B12,7AWE,6XMJ,6WJN,6WJD,6R70,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5T0J,5T0I,5T0H,5T0G,5T0C,5A0Q,4R67,4R3O,22MM,8YVP,8YPK,6TU3,3UNH,3UNF,3UNE,3UNB,8QYS Proteasome subunit beta type-3 PSB3_HUMAN P49720 P31147 Q0P6J7 Q96E27 MEAFLGSRSGLWAGGPAPGQFYRIPSTPDSFMDPASALYRGPITRTQNPMVTGTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNNSTMLGASGDYADFQYLKQVLGQMVIDEELLGDGHSYSPRAIHSWLTRAMYSRRSKMNPLWNTMVIGGYADGESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREVLEKQPVLSQTEARDLVERCMRVLYYRDARSYNRFQIATVTEKGVEIEGPLSTETNWDIAHMISGFE 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9BW4,9BV3,9BV2,9BV1,9BUI,8TM6,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YIZ,8YIY,8YIX,9RKZ,9HMN,8UD9,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,6AVO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,6XMJ,4R67,4R3O,6R70,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,7B12,7AWE,9QVX Proteasome subunit beta type-4 PSB4_HUMAN P28070 B2R9L3 P31148 Q5SZS5 Q6IBI4 Q969L6 MAAVSVYAPPVGGFSFDNCRRNAVLEADFAKRGYKLPKVRKTGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTANRMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAIAAGIFNDLGSGSNIDLCVISKNKLDFLRPYTVPNKKGTRLGRYRCEKGTTAVLTEKITPLEIEVLEETVQTMDTS 8QZ9,8QYN,8QYM,8QYL,8QYJ,9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8TM6,8TM5,8TM4,8QYO,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,9RKZ,9HMN,8UD9,8CVS,8CVR,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,9QVX,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O Proteasome subunit beta type-7 PSB7_HUMAN Q99436 B4E0P1 Q5TBG6 Q96AG8 Q9BWA7 51159624 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 A5LHX3/O14818/P20618/P25786/P25787/P25788/P25789/P28062/P28065/P28066/P28070/P28072/P28074/P40306/P49720/P49721/P60900/Q8TAA3/Q99436 Homo sapiens 1400 ChEMBL 10.1016/j.bmcl.2005.02.013 10.7270/Q2CF9SVN 15780623 Momose, I; Umezawa, Y; Hirosawa, S; Iinuma, H; Ikeda, D 4/1/2005 8/23/2020 Numazu Bio-Medical Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000077&target=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 19 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 MALLDVCGAPRGQRPESALPVAGSGRRSDPGHYSFSMRSPELALPRGMQPTEFFQSLGGDGERNVQIEMAHGTTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAIAYATHRDSYSGGVVNMYHMKEDGWVKVESTDVSDLLHQYREANQ 6E5B,6AVO,7B12,7AWE Proteasome subunit beta type-8 PSB8_HUMAN P28062 B0UZC0 Q29824 Q5JNW6 Q5QNR8 Q96J48 MLRAGAPTGDLPRAGEVHTGTTIMAVEFDGGVVMGSDSRVSAGEAVVNRVFDKLSPLHERIYCALSGSAADAQAVADMAAYQLELHGIELEEPPLVLAAANVVRNISYKYREDLSAHLMVAGWDQREGGQVYGTLGGMLTRQPFAIGGSGSTFIYGYVDAAYKPGMSPEECRRFTTDAIALAMSRDGSSGGVIYLVTITAAGVDHRVILGNELPKFYDE 6E5B,7B12,7AWE,6AVO,8YVG,8YSX Proteasome subunit beta type-9 PSB9_HUMAN P28065 B0V0T1 Q16523 Q5JNW4 MAATLLAARGAGPAPAWGPEAFTPDWESREVSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDRIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAASLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTANALALAMERDGSSGGVIRLAAIAESGVERQVLLGDQIPKFAVATLPPA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,9RKZ,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6R70,9QVX,6XMJ,4R67,4R3O,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit beta type-6 PSB6_HUMAN P28072 Q96J55 MFRNQYDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSELAAHQKKILHVDNHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGARSQSARTYLERHMSEFMECNLNELVKHGLRALRETLPAEQDLTTKNVSIGIVGKDLEFTIYDDDDVSPFLEGLEERPQRKAQPAQPADEPAEKADEPMEH 9YUZ,9UG9,9UF8,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9VUG,9VUF,9VUE,9U7R,9U3L,9SZV,9SZT,9MBQ,9MBP,9HEU,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,7DRW,7DR7,7DR6,8YVG,8YSX,8QYS,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,5M32,9QVX Proteasome subunit alpha type-1 PSA1_HUMAN P25786 A8K400 Q53YE8 Q9BRV9 MAERGYSFSLTTFSPSGKLVQIEYALAAVAGGAPSVGIKAANGVVLATEKKQKSILYDERSVHKVEPITKHIGLVYSGMGPDYRVLVHRARKLAQQYYLVYQEPIPTAQLVQRVASVMQEYTQSGGVRPFGVSLLICGWNEGRPYLFQSDPSGAYFAWKATAMGKNYVNGKTFLEKRYNEDLELEDAIHTAILTLKESFEGQMTEDNIEVGICNEAGFRRLTPTEVKDYLAAIA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YVG,8YSX,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYS,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,9U7R,9U3L,9MBQ,9MBP,9HMN,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6XMJ,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,4R67,4R3O,22MM,1IRU,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,6R70,9QVX,7B12,7AWE Proteasome subunit alpha type-2 PSA2_HUMAN P25787 Q6ICS6 Q9BU45 MSSIGTGYDLSASTFSPDGRVFQVEYAMKAVENSSTAIGIRCKDGVVFGVEKLVLSKLYEEGSNKRLFNVDRHVGMAVAGLLADARSLADIAREEASNFRSNFGYNIPLKHLADRVAMYVHAYTLYSAVRPFGCSFMLGSYSVNDGAQLYMIDPSGVSYGYWGCAIGKARQAAKTEIEKLQMKEMTCRDIVKEVAKIIYIVHDEVKDKAFELELSWVGELTNGRHEIVPKDIREEAEKYAKESLKEEDESDDDNM 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7E55,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5DSV,5A0Q,9U7R,9U3L,9MBQ,9MBP,9HMN,8FZ6,8FZ5,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7DRW,7DR7,7DR6,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,1IRU,6TU3,6EPF,6EPE,6EPD,6EPC,8YVP,8YPK,3UNH,3UNF,3UNE,3UNB,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,8QYS,6R70,9QVX Proteasome subunit alpha type-3 PSA3_HUMAN P25788 B2RCK6 Q86U83 Q8N1D8 Q9BS70 MSRRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGEMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTRENGKTVIRVLKQKEVEQLIKKHEEEEAKAEREKKEKEQKEKDK 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,7AWE,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,6R70,8QYS,9QVX Proteasome subunit alpha type-4 PSA4_HUMAN P25789 D3DW86 Q53XP2 Q567Q5 Q8TBD1 MFLTRSEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKTLIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGEEDADPGAMSRPFGVALLFGGVDEKGPQLFHMDPSGTFVQCDARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKLNATNIELATVQPGQNFHMFTKEELEEVIKDI 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDI,9NKJ,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8O,9E8N,9E8L,9E8K,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YVP,8YVG,8YSX,8YPK,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QYO,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,22MM,8QZ9,8QYN,8QYM,8QYL,8QYJ,8QYS,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9QVX,6R70,7B12,7AWE Proteasome subunit alpha type-5 PSA5_HUMAN P28066 B2R8F6 B4E2V4 Q3T1C1 Q6IBF7 MSRGSSAGFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITENIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATAAGVKQTESTSFLEKKVKKKFDWTFEQTVETAITCLSTVLSIDFKPSEIEVGVVTVENPKFRILTEAEIDAHLVALAERD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6TU3,6RGQ,6REY,6KWY,6EPF,6EPE,6EPD,6EPC,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,6XMJ,6R70,4R67,4R3O,7B12,7AWE,9QVX,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit alpha type-6 PSA6_HUMAN P60900 B2R7J9 B4DQR4 B4DXJ9 P34062 Q6IB60 MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIGRGAKSVREFLEKNYTDEAIETDDLTIKLVIKALLEVVQSGGKNIELAVMRRDQSLKILNPEEIEKYVAEIEKEKEENEKKKQKKAS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,22MM,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7AWE,6R70,7B12,8QYS,9QVX Proteasome subunit alpha type-7 PSA7_HUMAN O14818 B2R515 Q5JXJ2 Q9BR53 Q9H4K5 Q9UEU8 MASRYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVCMAFAVLTIFIGLTADARVVINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDAIASDSEAIKLAIKALLEVVQSGGKNIELAIIRRNQPLKMFSAKEVELYVTEIEKEKEEAEKKKSKKSV Proteasome subunit alpha-type 8 PSMA8_HUMAN Q8TAA3 B0YJ75 Q8IVP4 Q8TA98 Q8TAA2 MLKPALEPRGGFSFENCQRNASLERVLPGLKVPHARKTGTTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATVTRILRQTLFRYQGHVGASLIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLLVEAVTAGILGDLGSGGNVDACVITKTGAKLLRTLSSPTEPVKRSGRYHFVPGTTAVLTQTVKPLTLELVEETVQAMEVE 6E5B,6AVO,7AWE Proteasome subunit beta type-10 PSB10_HUMAN P40306 B2R5J4 Q5U098 MALQDVCKWQSPDTQGPSPHLPRAGGWAVPRGCDPQTFLQIHGPRLAHGTTTLAFRFRHGVIAAADTRSSCGSYVACPASCKVIPVHQHLLGTTSGTSADCATWYRVLQRELRLRELREGQLPSVASAAKLLSAMMSQYRGLDLCVATALCGWDRSGPELFYVYSDGTRLQGDIFSVGSGSPYAYGVLDRGYRYDMSTQEAYALARCAVAHATHRDAYSGGSVDLFHVRESGWEHVSRSDACVLYVELQKLLEPEPEEDASHAHPEPATAHRAAEDRELSVGPGEVTPGDSRMPAGTETV Proteasome subunit beta type-11 PSB11_HUMAN A5LHX3 MSIMSYNGGAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYTLMSMVANLLYEKRFGPYYTEPVIAGLDPKTFKPFICSLDLIGCPMVTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLFETISQAMLNAVDRDAVSGMGVIVHIIEKDKITTRTLKARMD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QZ9,8QYO,8QYN,8QYM,8QYL,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,9U7R,9U3L,9RKZ,9QVX,9MBQ,9MBP,9HMN,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7B12,7AWE,6XMJ,6WJN,6WJD,6R70,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5T0J,5T0I,5T0H,5T0G,5T0C,5A0Q,4R67,4R3O,22MM,8YVP,8YPK,6TU3,3UNH,3UNF,3UNE,3UNB,8QYS Proteasome subunit beta type-3 PSB3_HUMAN P49720 P31147 Q0P6J7 Q96E27 MEAFLGSRSGLWAGGPAPGQFYRIPSTPDSFMDPASALYRGPITRTQNPMVTGTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNNSTMLGASGDYADFQYLKQVLGQMVIDEELLGDGHSYSPRAIHSWLTRAMYSRRSKMNPLWNTMVIGGYADGESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREVLEKQPVLSQTEARDLVERCMRVLYYRDARSYNRFQIATVTEKGVEIEGPLSTETNWDIAHMISGFE 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9BW4,9BV3,9BV2,9BV1,9BUI,8TM6,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YIZ,8YIY,8YIX,9RKZ,9HMN,8UD9,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,6AVO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,6XMJ,4R67,4R3O,6R70,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,7B12,7AWE,9QVX Proteasome subunit beta type-4 PSB4_HUMAN P28070 B2R9L3 P31148 Q5SZS5 Q6IBI4 Q969L6 MAAVSVYAPPVGGFSFDNCRRNAVLEADFAKRGYKLPKVRKTGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTANRMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAIAAGIFNDLGSGSNIDLCVISKNKLDFLRPYTVPNKKGTRLGRYRCEKGTTAVLTEKITPLEIEVLEETVQTMDTS 8QZ9,8QYN,8QYM,8QYL,8QYJ,9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8TM6,8TM5,8TM4,8QYO,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,9RKZ,9HMN,8UD9,8CVS,8CVR,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,9QVX,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O Proteasome subunit beta type-7 PSB7_HUMAN Q99436 B4E0P1 Q5TBG6 Q96AG8 Q9BWA7 51159634 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 A5LHX3/O14818/P20618/P25786/P25787/P25788/P25789/P28062/P28065/P28066/P28070/P28072/P28074/P40306/P49720/P49721/P60900/Q8TAA3/Q99436 Homo sapiens 68 ChEMBL 10.1016/j.bmcl.2005.02.013 10.7270/Q2CF9SVN 15780623 Momose, I; Umezawa, Y; Hirosawa, S; Iinuma, H; Ikeda, D 4/1/2005 8/23/2020 Numazu Bio-Medical Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000077&target=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 19 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 MALLDVCGAPRGQRPESALPVAGSGRRSDPGHYSFSMRSPELALPRGMQPTEFFQSLGGDGERNVQIEMAHGTTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAIAYATHRDSYSGGVVNMYHMKEDGWVKVESTDVSDLLHQYREANQ 6E5B,6AVO,7B12,7AWE Proteasome subunit beta type-8 PSB8_HUMAN P28062 B0UZC0 Q29824 Q5JNW6 Q5QNR8 Q96J48 MLRAGAPTGDLPRAGEVHTGTTIMAVEFDGGVVMGSDSRVSAGEAVVNRVFDKLSPLHERIYCALSGSAADAQAVADMAAYQLELHGIELEEPPLVLAAANVVRNISYKYREDLSAHLMVAGWDQREGGQVYGTLGGMLTRQPFAIGGSGSTFIYGYVDAAYKPGMSPEECRRFTTDAIALAMSRDGSSGGVIYLVTITAAGVDHRVILGNELPKFYDE 6E5B,7B12,7AWE,6AVO,8YVG,8YSX Proteasome subunit beta type-9 PSB9_HUMAN P28065 B0V0T1 Q16523 Q5JNW4 MAATLLAARGAGPAPAWGPEAFTPDWESREVSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDRIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAASLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTANALALAMERDGSSGGVIRLAAIAESGVERQVLLGDQIPKFAVATLPPA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,9RKZ,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6R70,9QVX,6XMJ,4R67,4R3O,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit beta type-6 PSB6_HUMAN P28072 Q96J55 MFRNQYDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSELAAHQKKILHVDNHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGARSQSARTYLERHMSEFMECNLNELVKHGLRALRETLPAEQDLTTKNVSIGIVGKDLEFTIYDDDDVSPFLEGLEERPQRKAQPAQPADEPAEKADEPMEH 9YUZ,9UG9,9UF8,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9VUG,9VUF,9VUE,9U7R,9U3L,9SZV,9SZT,9MBQ,9MBP,9HEU,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,7DRW,7DR7,7DR6,8YVG,8YSX,8QYS,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,5M32,9QVX Proteasome subunit alpha type-1 PSA1_HUMAN P25786 A8K400 Q53YE8 Q9BRV9 MAERGYSFSLTTFSPSGKLVQIEYALAAVAGGAPSVGIKAANGVVLATEKKQKSILYDERSVHKVEPITKHIGLVYSGMGPDYRVLVHRARKLAQQYYLVYQEPIPTAQLVQRVASVMQEYTQSGGVRPFGVSLLICGWNEGRPYLFQSDPSGAYFAWKATAMGKNYVNGKTFLEKRYNEDLELEDAIHTAILTLKESFEGQMTEDNIEVGICNEAGFRRLTPTEVKDYLAAIA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YVG,8YSX,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYS,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,9U7R,9U3L,9MBQ,9MBP,9HMN,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6XMJ,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,4R67,4R3O,22MM,1IRU,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,6R70,9QVX,7B12,7AWE Proteasome subunit alpha type-2 PSA2_HUMAN P25787 Q6ICS6 Q9BU45 MSSIGTGYDLSASTFSPDGRVFQVEYAMKAVENSSTAIGIRCKDGVVFGVEKLVLSKLYEEGSNKRLFNVDRHVGMAVAGLLADARSLADIAREEASNFRSNFGYNIPLKHLADRVAMYVHAYTLYSAVRPFGCSFMLGSYSVNDGAQLYMIDPSGVSYGYWGCAIGKARQAAKTEIEKLQMKEMTCRDIVKEVAKIIYIVHDEVKDKAFELELSWVGELTNGRHEIVPKDIREEAEKYAKESLKEEDESDDDNM 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7E55,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5DSV,5A0Q,9U7R,9U3L,9MBQ,9MBP,9HMN,8FZ6,8FZ5,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7DRW,7DR7,7DR6,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,1IRU,6TU3,6EPF,6EPE,6EPD,6EPC,8YVP,8YPK,3UNH,3UNF,3UNE,3UNB,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,8QYS,6R70,9QVX Proteasome subunit alpha type-3 PSA3_HUMAN P25788 B2RCK6 Q86U83 Q8N1D8 Q9BS70 MSRRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGEMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTRENGKTVIRVLKQKEVEQLIKKHEEEEAKAEREKKEKEQKEKDK 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,7AWE,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,6R70,8QYS,9QVX Proteasome subunit alpha type-4 PSA4_HUMAN P25789 D3DW86 Q53XP2 Q567Q5 Q8TBD1 MFLTRSEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKTLIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGEEDADPGAMSRPFGVALLFGGVDEKGPQLFHMDPSGTFVQCDARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKLNATNIELATVQPGQNFHMFTKEELEEVIKDI 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDI,9NKJ,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8O,9E8N,9E8L,9E8K,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YVP,8YVG,8YSX,8YPK,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QYO,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,22MM,8QZ9,8QYN,8QYM,8QYL,8QYJ,8QYS,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9QVX,6R70,7B12,7AWE Proteasome subunit alpha type-5 PSA5_HUMAN P28066 B2R8F6 B4E2V4 Q3T1C1 Q6IBF7 MSRGSSAGFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITENIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATAAGVKQTESTSFLEKKVKKKFDWTFEQTVETAITCLSTVLSIDFKPSEIEVGVVTVENPKFRILTEAEIDAHLVALAERD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6TU3,6RGQ,6REY,6KWY,6EPF,6EPE,6EPD,6EPC,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,6XMJ,6R70,4R67,4R3O,7B12,7AWE,9QVX,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit alpha type-6 PSA6_HUMAN P60900 B2R7J9 B4DQR4 B4DXJ9 P34062 Q6IB60 MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIGRGAKSVREFLEKNYTDEAIETDDLTIKLVIKALLEVVQSGGKNIELAVMRRDQSLKILNPEEIEKYVAEIEKEKEENEKKKQKKAS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,22MM,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7AWE,6R70,7B12,8QYS,9QVX Proteasome subunit alpha type-7 PSA7_HUMAN O14818 B2R515 Q5JXJ2 Q9BR53 Q9H4K5 Q9UEU8 MASRYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVCMAFAVLTIFIGLTADARVVINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDAIASDSEAIKLAIKALLEVVQSGGKNIELAIIRRNQPLKMFSAKEVELYVTEIEKEKEEAEKKKSKKSV Proteasome subunit alpha-type 8 PSMA8_HUMAN Q8TAA3 B0YJ75 Q8IVP4 Q8TA98 Q8TAA2 MLKPALEPRGGFSFENCQRNASLERVLPGLKVPHARKTGTTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATVTRILRQTLFRYQGHVGASLIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLLVEAVTAGILGDLGSGGNVDACVITKTGAKLLRTLSSPTEPVKRSGRYHFVPGTTAVLTQTVKPLTLELVEETVQAMEVE 6E5B,6AVO,7AWE Proteasome subunit beta type-10 PSB10_HUMAN P40306 B2R5J4 Q5U098 MALQDVCKWQSPDTQGPSPHLPRAGGWAVPRGCDPQTFLQIHGPRLAHGTTTLAFRFRHGVIAAADTRSSCGSYVACPASCKVIPVHQHLLGTTSGTSADCATWYRVLQRELRLRELREGQLPSVASAAKLLSAMMSQYRGLDLCVATALCGWDRSGPELFYVYSDGTRLQGDIFSVGSGSPYAYGVLDRGYRYDMSTQEAYALARCAVAHATHRDAYSGGSVDLFHVRESGWEHVSRSDACVLYVELQKLLEPEPEEDASHAHPEPATAHRAAEDRELSVGPGEVTPGDSRMPAGTETV Proteasome subunit beta type-11 PSB11_HUMAN A5LHX3 MSIMSYNGGAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYTLMSMVANLLYEKRFGPYYTEPVIAGLDPKTFKPFICSLDLIGCPMVTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLFETISQAMLNAVDRDAVSGMGVIVHIIEKDKITTRTLKARMD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QZ9,8QYO,8QYN,8QYM,8QYL,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,9U7R,9U3L,9RKZ,9QVX,9MBQ,9MBP,9HMN,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7B12,7AWE,6XMJ,6WJN,6WJD,6R70,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5T0J,5T0I,5T0H,5T0G,5T0C,5A0Q,4R67,4R3O,22MM,8YVP,8YPK,6TU3,3UNH,3UNF,3UNE,3UNB,8QYS Proteasome subunit beta type-3 PSB3_HUMAN P49720 P31147 Q0P6J7 Q96E27 MEAFLGSRSGLWAGGPAPGQFYRIPSTPDSFMDPASALYRGPITRTQNPMVTGTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNNSTMLGASGDYADFQYLKQVLGQMVIDEELLGDGHSYSPRAIHSWLTRAMYSRRSKMNPLWNTMVIGGYADGESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREVLEKQPVLSQTEARDLVERCMRVLYYRDARSYNRFQIATVTEKGVEIEGPLSTETNWDIAHMISGFE 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9BW4,9BV3,9BV2,9BV1,9BUI,8TM6,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YIZ,8YIY,8YIX,9RKZ,9HMN,8UD9,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,6AVO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,6XMJ,4R67,4R3O,6R70,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,7B12,7AWE,9QVX Proteasome subunit beta type-4 PSB4_HUMAN P28070 B2R9L3 P31148 Q5SZS5 Q6IBI4 Q969L6 MAAVSVYAPPVGGFSFDNCRRNAVLEADFAKRGYKLPKVRKTGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTANRMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAIAAGIFNDLGSGSNIDLCVISKNKLDFLRPYTVPNKKGTRLGRYRCEKGTTAVLTEKITPLEIEVLEETVQTMDTS 8QZ9,8QYN,8QYM,8QYL,8QYJ,9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8TM6,8TM5,8TM4,8QYO,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,9RKZ,9HMN,8UD9,8CVS,8CVR,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,9QVX,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O Proteasome subunit beta type-7 PSB7_HUMAN Q99436 B4E0P1 Q5TBG6 Q96AG8 Q9BWA7 50028847 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 120 ChEMBL 10.1021/jm00213a022 10.7270/Q26977R0 576620 Song, R; Qiao, W; He, J; Huang, J; Luo, Y; Yang, T 3/25/2021 4/18/2024 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 50029539 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 1080 ChEMBL 10.1021/jm00213a022 10.7270/Q26977R0 576620 Song, R; Qiao, W; He, J; Huang, J; Luo, Y; Yang, T 3/25/2021 4/18/2024 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 50029543 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 1.2 ChEMBL 10.1021/jm00213a022 10.7270/Q26977R0 576620 Song, R; Qiao, W; He, J; Huang, J; Luo, Y; Yang, T 3/25/2021 4/18/2024 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 50494739 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 37 ChEMBL 10.1016/j.bmcl.2016.04.067 10.7270/Q2N018GG 27158142 Yang, L; Wang, W; Sun, Q; Xu, F; Niu, Y; Wang, C; Liang, L; Xu, P 6/15/2016 8/25/2017 Peking University Health Science Center http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 50494751 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 44 ChEMBL 10.1016/j.bmcl.2016.04.067 10.7270/Q2N018GG 27158142 Yang, L; Wang, W; Sun, Q; Xu, F; Niu, Y; Wang, C; Liang, L; Xu, P 6/15/2016 8/25/2017 Peking University Health Science Center http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 50494763 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 52 ChEMBL 10.1016/j.bmcl.2016.04.067 10.7270/Q2N018GG 27158142 Yang, L; Wang, W; Sun, Q; Xu, F; Niu, Y; Wang, C; Liang, L; Xu, P 6/15/2016 8/25/2017 Peking University Health Science Center http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 50521882 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 1.4 ChEMBL 10.1016/j.ejmech.2016.05.049 10.7270/Q28C9Z6K 27318981 Di Giovanni, C; Ettari, R; Sarno, S; Rotondo, A; Bitto, A; Squadrito, F; Altavilla, D; Schirmeister, T; Novellino, E; Grasso, S; Zappalà, M; Lavecchia, A 10/4/2016 7/10/2018 University of Naples Federico Ii http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 50521890 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 22100 ChEMBL 10.1016/j.ejmech.2016.05.049 10.7270/Q28C9Z6K 27318981 Di Giovanni, C; Ettari, R; Sarno, S; Rotondo, A; Bitto, A; Squadrito, F; Altavilla, D; Schirmeister, T; Novellino, E; Grasso, S; Zappalà, M; Lavecchia, A 10/4/2016 7/10/2018 University of Naples Federico Ii http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 50521891 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 5520 ChEMBL 10.1016/j.ejmech.2016.05.049 10.7270/Q28C9Z6K 27318981 Di Giovanni, C; Ettari, R; Sarno, S; Rotondo, A; Bitto, A; Squadrito, F; Altavilla, D; Schirmeister, T; Novellino, E; Grasso, S; Zappalà, M; Lavecchia, A 10/4/2016 7/10/2018 University of Naples Federico Ii http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 50711335 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 25 ChEMBL 10.1016/j.ejmech.2016.11.024 10.7270/Q2Z03BDZ 27889629 Qin, JM; Huang, RZ; Yao, GY; Liao, ZX; Pan, YM; Wang, HS 1/27/2017 6/17/2019 Guangxi Normal University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51002658 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 470 ChEMBL 10.1021/jm058289o 10.7270/Q2FF3S0S 16686537 Rydzewski, RM; Burrill, L; Mendonca, R; Palmer, JT; Rice, M; Tahilramani, R; Bass, KE; Leung, L; Gjerstad, E; Janc, JW; Pan, L 5/11/2006 11/10/2009 Celera http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51002662 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 3.7 ChEMBL 10.1021/jm058289o 10.7270/Q2FF3S0S 16686537 Rydzewski, RM; Burrill, L; Mendonca, R; Palmer, JT; Rice, M; Tahilramani, R; Bass, KE; Leung, L; Gjerstad, E; Janc, JW; Pan, L 5/11/2006 11/10/2009 Celera http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51002664 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 330 ChEMBL 10.1021/jm058289o 10.7270/Q2FF3S0S 16686537 Rydzewski, RM; Burrill, L; Mendonca, R; Palmer, JT; Rice, M; Tahilramani, R; Bass, KE; Leung, L; Gjerstad, E; Janc, JW; Pan, L 5/11/2006 11/10/2009 Celera http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51087096 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 2100 ChEMBL 10.1016/j.ejmech.2013.11.009 10.7270/Q2222W81 24321833 Hasegawa, M; Yasuda, Y; Tanaka, M; Nakata, K; Umeda, E; Wang, Y; Watanabe, C; Uetake, S; Kunoh, T; Shionyu, M; Sasaki, R; Shiina, I; Mizukami, T 1/31/2014 7/25/2014 Institute of Bio-Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51087151 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 120 ChEMBL 10.1016/j.ejmech.2013.11.009 10.7270/Q2222W81 24321833 Hasegawa, M; Yasuda, Y; Tanaka, M; Nakata, K; Umeda, E; Wang, Y; Watanabe, C; Uetake, S; Kunoh, T; Shionyu, M; Sasaki, R; Shiina, I; Mizukami, T 1/31/2014 7/25/2014 Institute of Bio-Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51087152 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 11 ChEMBL 10.1016/j.ejmech.2013.11.009 10.7270/Q2222W81 24321833 Hasegawa, M; Yasuda, Y; Tanaka, M; Nakata, K; Umeda, E; Wang, Y; Watanabe, C; Uetake, S; Kunoh, T; Shionyu, M; Sasaki, R; Shiina, I; Mizukami, T 1/31/2014 7/25/2014 Institute of Bio-Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51110847 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 1.000000 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51110850 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 5520 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51110852 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 22100 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51110856 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 4.0 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51110862 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 130 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51110863 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 70 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51227585 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 1.2 ChEMBL 10.1016/j.bmc.2018.12.022 10.7270/Q2NP27P1 30581047 Pehere, AD; Nguyen, S; Garlick, SK; Wilson, DW; Hudson, I; Sykes, MJ; Morton, JD; Abell, AD 1/15/2019 2/18/2021 University of Adelaide http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51289132 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 1450 ChEMBL 10.1021/acsmedchemlett.9b00233 10.7270/Q2930XK7 31312413 Pacifico, S; Ferretti, V; Albanese, V; Fantinati, A; Gallerani, E; Nicoli, F; Gavioli, R; Zamberlan, F; Preti, D; Marastoni, M 7/11/2019 2/24/2021 University of Ferrara http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51289181 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 4590 ChEMBL 10.1021/acsmedchemlett.9b00233 10.7270/Q2930XK7 31312413 Pacifico, S; Ferretti, V; Albanese, V; Fantinati, A; Gallerani, E; Nicoli, F; Gavioli, R; Zamberlan, F; Preti, D; Marastoni, M 7/11/2019 2/24/2021 University of Ferrara http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51289196 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 7.0 ChEMBL 10.1021/acsmedchemlett.9b00233 10.7270/Q2930XK7 31312413 Pacifico, S; Ferretti, V; Albanese, V; Fantinati, A; Gallerani, E; Nicoli, F; Gavioli, R; Zamberlan, F; Preti, D; Marastoni, M 7/11/2019 2/24/2021 University of Ferrara http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51298902 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 30 ChEMBL 10.1016/j.bmc.2019.115161 10.7270/Q29W0JZJ 31732281 Uesugi, S; Honmura, Y; Nishiyama, M; Kusakabe, K; Tonouchi, A; Yamashita, T; Hashimoto, M; Kimura, KI 12/15/2019 2/25/2021 Iwate University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51298906 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 1600 ChEMBL 10.1016/j.bmc.2019.115161 10.7270/Q29W0JZJ 31732281 Uesugi, S; Honmura, Y; Nishiyama, M; Kusakabe, K; Tonouchi, A; Yamashita, T; Hashimoto, M; Kimura, KI 12/15/2019 2/25/2021 Iwate University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51298909 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 500 ChEMBL 10.1016/j.bmc.2019.115161 10.7270/Q29W0JZJ 31732281 Uesugi, S; Honmura, Y; Nishiyama, M; Kusakabe, K; Tonouchi, A; Yamashita, T; Hashimoto, M; Kimura, KI 12/15/2019 2/25/2021 Iwate University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51487773 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 22100 ChEMBL 10.7270/Q20R9TGT 34838650 Ettari, R; Iraci, N; Di Chio, C; Previti, S; Danzè, M; Zappalà, M 1/1/2022 6/23/2023 University of Messina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51487774 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 5520 ChEMBL 10.7270/Q20R9TGT 34838650 Ettari, R; Iraci, N; Di Chio, C; Previti, S; Danzè, M; Zappalà, M 1/1/2022 6/23/2023 University of Messina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51487775 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 1.4 ChEMBL 10.7270/Q20R9TGT 34838650 Ettari, R; Iraci, N; Di Chio, C; Previti, S; Danzè, M; Zappalà, M 1/1/2022 6/23/2023 University of Messina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51487776 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 130 ChEMBL 10.7270/Q20R9TGT 34838650 Ettari, R; Iraci, N; Di Chio, C; Previti, S; Danzè, M; Zappalà, M 1/1/2022 6/23/2023 University of Messina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51487777 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 1.000000 ChEMBL 10.7270/Q20R9TGT 34838650 Ettari, R; Iraci, N; Di Chio, C; Previti, S; Danzè, M; Zappalà, M 1/1/2022 6/23/2023 University of Messina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51159619 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 A5LHX3/O14818/P20618/P25786/P25787/P25788/P25789/P28062/P28065/P28066/P28070/P28072/P28074/P40306/P49720/P49721/P60900/Q8TAA3/Q99436 Homo sapiens 4500 ChEMBL 10.1016/j.bmcl.2005.02.013 10.7270/Q2CF9SVN 15780623 Momose, I; Umezawa, Y; Hirosawa, S; Iinuma, H; Ikeda, D 4/1/2005 8/23/2020 Numazu Bio-Medical Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000077&target=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 19 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 MALLDVCGAPRGQRPESALPVAGSGRRSDPGHYSFSMRSPELALPRGMQPTEFFQSLGGDGERNVQIEMAHGTTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAIAYATHRDSYSGGVVNMYHMKEDGWVKVESTDVSDLLHQYREANQ 6E5B,6AVO,7B12,7AWE Proteasome subunit beta type-8 PSB8_HUMAN P28062 B0UZC0 Q29824 Q5JNW6 Q5QNR8 Q96J48 MLRAGAPTGDLPRAGEVHTGTTIMAVEFDGGVVMGSDSRVSAGEAVVNRVFDKLSPLHERIYCALSGSAADAQAVADMAAYQLELHGIELEEPPLVLAAANVVRNISYKYREDLSAHLMVAGWDQREGGQVYGTLGGMLTRQPFAIGGSGSTFIYGYVDAAYKPGMSPEECRRFTTDAIALAMSRDGSSGGVIYLVTITAAGVDHRVILGNELPKFYDE 6E5B,7B12,7AWE,6AVO,8YVG,8YSX Proteasome subunit beta type-9 PSB9_HUMAN P28065 B0V0T1 Q16523 Q5JNW4 MAATLLAARGAGPAPAWGPEAFTPDWESREVSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDRIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAASLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTANALALAMERDGSSGGVIRLAAIAESGVERQVLLGDQIPKFAVATLPPA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,9RKZ,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6R70,9QVX,6XMJ,4R67,4R3O,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit beta type-6 PSB6_HUMAN P28072 Q96J55 MFRNQYDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSELAAHQKKILHVDNHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGARSQSARTYLERHMSEFMECNLNELVKHGLRALRETLPAEQDLTTKNVSIGIVGKDLEFTIYDDDDVSPFLEGLEERPQRKAQPAQPADEPAEKADEPMEH 9YUZ,9UG9,9UF8,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9VUG,9VUF,9VUE,9U7R,9U3L,9SZV,9SZT,9MBQ,9MBP,9HEU,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,7DRW,7DR7,7DR6,8YVG,8YSX,8QYS,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,5M32,9QVX Proteasome subunit alpha type-1 PSA1_HUMAN P25786 A8K400 Q53YE8 Q9BRV9 MAERGYSFSLTTFSPSGKLVQIEYALAAVAGGAPSVGIKAANGVVLATEKKQKSILYDERSVHKVEPITKHIGLVYSGMGPDYRVLVHRARKLAQQYYLVYQEPIPTAQLVQRVASVMQEYTQSGGVRPFGVSLLICGWNEGRPYLFQSDPSGAYFAWKATAMGKNYVNGKTFLEKRYNEDLELEDAIHTAILTLKESFEGQMTEDNIEVGICNEAGFRRLTPTEVKDYLAAIA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YVG,8YSX,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYS,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,9U7R,9U3L,9MBQ,9MBP,9HMN,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6XMJ,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,4R67,4R3O,22MM,1IRU,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,6R70,9QVX,7B12,7AWE Proteasome subunit alpha type-2 PSA2_HUMAN P25787 Q6ICS6 Q9BU45 MSSIGTGYDLSASTFSPDGRVFQVEYAMKAVENSSTAIGIRCKDGVVFGVEKLVLSKLYEEGSNKRLFNVDRHVGMAVAGLLADARSLADIAREEASNFRSNFGYNIPLKHLADRVAMYVHAYTLYSAVRPFGCSFMLGSYSVNDGAQLYMIDPSGVSYGYWGCAIGKARQAAKTEIEKLQMKEMTCRDIVKEVAKIIYIVHDEVKDKAFELELSWVGELTNGRHEIVPKDIREEAEKYAKESLKEEDESDDDNM 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7E55,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5DSV,5A0Q,9U7R,9U3L,9MBQ,9MBP,9HMN,8FZ6,8FZ5,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7DRW,7DR7,7DR6,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,1IRU,6TU3,6EPF,6EPE,6EPD,6EPC,8YVP,8YPK,3UNH,3UNF,3UNE,3UNB,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,8QYS,6R70,9QVX Proteasome subunit alpha type-3 PSA3_HUMAN P25788 B2RCK6 Q86U83 Q8N1D8 Q9BS70 MSRRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGEMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTRENGKTVIRVLKQKEVEQLIKKHEEEEAKAEREKKEKEQKEKDK 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,7AWE,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,6R70,8QYS,9QVX Proteasome subunit alpha type-4 PSA4_HUMAN P25789 D3DW86 Q53XP2 Q567Q5 Q8TBD1 MFLTRSEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKTLIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGEEDADPGAMSRPFGVALLFGGVDEKGPQLFHMDPSGTFVQCDARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKLNATNIELATVQPGQNFHMFTKEELEEVIKDI 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDI,9NKJ,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8O,9E8N,9E8L,9E8K,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YVP,8YVG,8YSX,8YPK,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QYO,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,22MM,8QZ9,8QYN,8QYM,8QYL,8QYJ,8QYS,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9QVX,6R70,7B12,7AWE Proteasome subunit alpha type-5 PSA5_HUMAN P28066 B2R8F6 B4E2V4 Q3T1C1 Q6IBF7 MSRGSSAGFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITENIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATAAGVKQTESTSFLEKKVKKKFDWTFEQTVETAITCLSTVLSIDFKPSEIEVGVVTVENPKFRILTEAEIDAHLVALAERD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6TU3,6RGQ,6REY,6KWY,6EPF,6EPE,6EPD,6EPC,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,6XMJ,6R70,4R67,4R3O,7B12,7AWE,9QVX,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit alpha type-6 PSA6_HUMAN P60900 B2R7J9 B4DQR4 B4DXJ9 P34062 Q6IB60 MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIGRGAKSVREFLEKNYTDEAIETDDLTIKLVIKALLEVVQSGGKNIELAVMRRDQSLKILNPEEIEKYVAEIEKEKEENEKKKQKKAS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,22MM,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7AWE,6R70,7B12,8QYS,9QVX Proteasome subunit alpha type-7 PSA7_HUMAN O14818 B2R515 Q5JXJ2 Q9BR53 Q9H4K5 Q9UEU8 MASRYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVCMAFAVLTIFIGLTADARVVINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDAIASDSEAIKLAIKALLEVVQSGGKNIELAIIRRNQPLKMFSAKEVELYVTEIEKEKEEAEKKKSKKSV Proteasome subunit alpha-type 8 PSMA8_HUMAN Q8TAA3 B0YJ75 Q8IVP4 Q8TA98 Q8TAA2 MLKPALEPRGGFSFENCQRNASLERVLPGLKVPHARKTGTTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATVTRILRQTLFRYQGHVGASLIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLLVEAVTAGILGDLGSGGNVDACVITKTGAKLLRTLSSPTEPVKRSGRYHFVPGTTAVLTQTVKPLTLELVEETVQAMEVE 6E5B,6AVO,7AWE Proteasome subunit beta type-10 PSB10_HUMAN P40306 B2R5J4 Q5U098 MALQDVCKWQSPDTQGPSPHLPRAGGWAVPRGCDPQTFLQIHGPRLAHGTTTLAFRFRHGVIAAADTRSSCGSYVACPASCKVIPVHQHLLGTTSGTSADCATWYRVLQRELRLRELREGQLPSVASAAKLLSAMMSQYRGLDLCVATALCGWDRSGPELFYVYSDGTRLQGDIFSVGSGSPYAYGVLDRGYRYDMSTQEAYALARCAVAHATHRDAYSGGSVDLFHVRESGWEHVSRSDACVLYVELQKLLEPEPEEDASHAHPEPATAHRAAEDRELSVGPGEVTPGDSRMPAGTETV Proteasome subunit beta type-11 PSB11_HUMAN A5LHX3 MSIMSYNGGAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYTLMSMVANLLYEKRFGPYYTEPVIAGLDPKTFKPFICSLDLIGCPMVTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLFETISQAMLNAVDRDAVSGMGVIVHIIEKDKITTRTLKARMD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QZ9,8QYO,8QYN,8QYM,8QYL,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,9U7R,9U3L,9RKZ,9QVX,9MBQ,9MBP,9HMN,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7B12,7AWE,6XMJ,6WJN,6WJD,6R70,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5T0J,5T0I,5T0H,5T0G,5T0C,5A0Q,4R67,4R3O,22MM,8YVP,8YPK,6TU3,3UNH,3UNF,3UNE,3UNB,8QYS Proteasome subunit beta type-3 PSB3_HUMAN P49720 P31147 Q0P6J7 Q96E27 MEAFLGSRSGLWAGGPAPGQFYRIPSTPDSFMDPASALYRGPITRTQNPMVTGTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNNSTMLGASGDYADFQYLKQVLGQMVIDEELLGDGHSYSPRAIHSWLTRAMYSRRSKMNPLWNTMVIGGYADGESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREVLEKQPVLSQTEARDLVERCMRVLYYRDARSYNRFQIATVTEKGVEIEGPLSTETNWDIAHMISGFE 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9BW4,9BV3,9BV2,9BV1,9BUI,8TM6,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YIZ,8YIY,8YIX,9RKZ,9HMN,8UD9,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,6AVO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,6XMJ,4R67,4R3O,6R70,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,7B12,7AWE,9QVX Proteasome subunit beta type-4 PSB4_HUMAN P28070 B2R9L3 P31148 Q5SZS5 Q6IBI4 Q969L6 MAAVSVYAPPVGGFSFDNCRRNAVLEADFAKRGYKLPKVRKTGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTANRMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAIAAGIFNDLGSGSNIDLCVISKNKLDFLRPYTVPNKKGTRLGRYRCEKGTTAVLTEKITPLEIEVLEETVQTMDTS 8QZ9,8QYN,8QYM,8QYL,8QYJ,9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8TM6,8TM5,8TM4,8QYO,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,9RKZ,9HMN,8UD9,8CVS,8CVR,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,9QVX,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O Proteasome subunit beta type-7 PSB7_HUMAN Q99436 B4E0P1 Q5TBG6 Q96AG8 Q9BWA7 51159624 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 A5LHX3/O14818/P20618/P25786/P25787/P25788/P25789/P28062/P28065/P28066/P28070/P28072/P28074/P40306/P49720/P49721/P60900/Q8TAA3/Q99436 Homo sapiens 1400 ChEMBL 10.1016/j.bmcl.2005.02.013 10.7270/Q2CF9SVN 15780623 Momose, I; Umezawa, Y; Hirosawa, S; Iinuma, H; Ikeda, D 4/1/2005 8/23/2020 Numazu Bio-Medical Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000077&target=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 19 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 MALLDVCGAPRGQRPESALPVAGSGRRSDPGHYSFSMRSPELALPRGMQPTEFFQSLGGDGERNVQIEMAHGTTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAIAYATHRDSYSGGVVNMYHMKEDGWVKVESTDVSDLLHQYREANQ 6E5B,6AVO,7B12,7AWE Proteasome subunit beta type-8 PSB8_HUMAN P28062 B0UZC0 Q29824 Q5JNW6 Q5QNR8 Q96J48 MLRAGAPTGDLPRAGEVHTGTTIMAVEFDGGVVMGSDSRVSAGEAVVNRVFDKLSPLHERIYCALSGSAADAQAVADMAAYQLELHGIELEEPPLVLAAANVVRNISYKYREDLSAHLMVAGWDQREGGQVYGTLGGMLTRQPFAIGGSGSTFIYGYVDAAYKPGMSPEECRRFTTDAIALAMSRDGSSGGVIYLVTITAAGVDHRVILGNELPKFYDE 6E5B,7B12,7AWE,6AVO,8YVG,8YSX Proteasome subunit beta type-9 PSB9_HUMAN P28065 B0V0T1 Q16523 Q5JNW4 MAATLLAARGAGPAPAWGPEAFTPDWESREVSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDRIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAASLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTANALALAMERDGSSGGVIRLAAIAESGVERQVLLGDQIPKFAVATLPPA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,9RKZ,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6R70,9QVX,6XMJ,4R67,4R3O,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit beta type-6 PSB6_HUMAN P28072 Q96J55 MFRNQYDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSELAAHQKKILHVDNHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGARSQSARTYLERHMSEFMECNLNELVKHGLRALRETLPAEQDLTTKNVSIGIVGKDLEFTIYDDDDVSPFLEGLEERPQRKAQPAQPADEPAEKADEPMEH 9YUZ,9UG9,9UF8,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9VUG,9VUF,9VUE,9U7R,9U3L,9SZV,9SZT,9MBQ,9MBP,9HEU,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,7DRW,7DR7,7DR6,8YVG,8YSX,8QYS,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,5M32,9QVX Proteasome subunit alpha type-1 PSA1_HUMAN P25786 A8K400 Q53YE8 Q9BRV9 MAERGYSFSLTTFSPSGKLVQIEYALAAVAGGAPSVGIKAANGVVLATEKKQKSILYDERSVHKVEPITKHIGLVYSGMGPDYRVLVHRARKLAQQYYLVYQEPIPTAQLVQRVASVMQEYTQSGGVRPFGVSLLICGWNEGRPYLFQSDPSGAYFAWKATAMGKNYVNGKTFLEKRYNEDLELEDAIHTAILTLKESFEGQMTEDNIEVGICNEAGFRRLTPTEVKDYLAAIA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YVG,8YSX,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYS,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,9U7R,9U3L,9MBQ,9MBP,9HMN,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6XMJ,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,4R67,4R3O,22MM,1IRU,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,6R70,9QVX,7B12,7AWE Proteasome subunit alpha type-2 PSA2_HUMAN P25787 Q6ICS6 Q9BU45 MSSIGTGYDLSASTFSPDGRVFQVEYAMKAVENSSTAIGIRCKDGVVFGVEKLVLSKLYEEGSNKRLFNVDRHVGMAVAGLLADARSLADIAREEASNFRSNFGYNIPLKHLADRVAMYVHAYTLYSAVRPFGCSFMLGSYSVNDGAQLYMIDPSGVSYGYWGCAIGKARQAAKTEIEKLQMKEMTCRDIVKEVAKIIYIVHDEVKDKAFELELSWVGELTNGRHEIVPKDIREEAEKYAKESLKEEDESDDDNM 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7E55,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5DSV,5A0Q,9U7R,9U3L,9MBQ,9MBP,9HMN,8FZ6,8FZ5,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7DRW,7DR7,7DR6,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,1IRU,6TU3,6EPF,6EPE,6EPD,6EPC,8YVP,8YPK,3UNH,3UNF,3UNE,3UNB,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,8QYS,6R70,9QVX Proteasome subunit alpha type-3 PSA3_HUMAN P25788 B2RCK6 Q86U83 Q8N1D8 Q9BS70 MSRRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGEMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTRENGKTVIRVLKQKEVEQLIKKHEEEEAKAEREKKEKEQKEKDK 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,7AWE,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,6R70,8QYS,9QVX Proteasome subunit alpha type-4 PSA4_HUMAN P25789 D3DW86 Q53XP2 Q567Q5 Q8TBD1 MFLTRSEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKTLIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGEEDADPGAMSRPFGVALLFGGVDEKGPQLFHMDPSGTFVQCDARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKLNATNIELATVQPGQNFHMFTKEELEEVIKDI 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDI,9NKJ,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8O,9E8N,9E8L,9E8K,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YVP,8YVG,8YSX,8YPK,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QYO,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,22MM,8QZ9,8QYN,8QYM,8QYL,8QYJ,8QYS,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9QVX,6R70,7B12,7AWE Proteasome subunit alpha type-5 PSA5_HUMAN P28066 B2R8F6 B4E2V4 Q3T1C1 Q6IBF7 MSRGSSAGFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITENIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATAAGVKQTESTSFLEKKVKKKFDWTFEQTVETAITCLSTVLSIDFKPSEIEVGVVTVENPKFRILTEAEIDAHLVALAERD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6TU3,6RGQ,6REY,6KWY,6EPF,6EPE,6EPD,6EPC,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,6XMJ,6R70,4R67,4R3O,7B12,7AWE,9QVX,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit alpha type-6 PSA6_HUMAN P60900 B2R7J9 B4DQR4 B4DXJ9 P34062 Q6IB60 MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIGRGAKSVREFLEKNYTDEAIETDDLTIKLVIKALLEVVQSGGKNIELAVMRRDQSLKILNPEEIEKYVAEIEKEKEENEKKKQKKAS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,22MM,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7AWE,6R70,7B12,8QYS,9QVX Proteasome subunit alpha type-7 PSA7_HUMAN O14818 B2R515 Q5JXJ2 Q9BR53 Q9H4K5 Q9UEU8 MASRYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVCMAFAVLTIFIGLTADARVVINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDAIASDSEAIKLAIKALLEVVQSGGKNIELAIIRRNQPLKMFSAKEVELYVTEIEKEKEEAEKKKSKKSV Proteasome subunit alpha-type 8 PSMA8_HUMAN Q8TAA3 B0YJ75 Q8IVP4 Q8TA98 Q8TAA2 MLKPALEPRGGFSFENCQRNASLERVLPGLKVPHARKTGTTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATVTRILRQTLFRYQGHVGASLIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLLVEAVTAGILGDLGSGGNVDACVITKTGAKLLRTLSSPTEPVKRSGRYHFVPGTTAVLTQTVKPLTLELVEETVQAMEVE 6E5B,6AVO,7AWE Proteasome subunit beta type-10 PSB10_HUMAN P40306 B2R5J4 Q5U098 MALQDVCKWQSPDTQGPSPHLPRAGGWAVPRGCDPQTFLQIHGPRLAHGTTTLAFRFRHGVIAAADTRSSCGSYVACPASCKVIPVHQHLLGTTSGTSADCATWYRVLQRELRLRELREGQLPSVASAAKLLSAMMSQYRGLDLCVATALCGWDRSGPELFYVYSDGTRLQGDIFSVGSGSPYAYGVLDRGYRYDMSTQEAYALARCAVAHATHRDAYSGGSVDLFHVRESGWEHVSRSDACVLYVELQKLLEPEPEEDASHAHPEPATAHRAAEDRELSVGPGEVTPGDSRMPAGTETV Proteasome subunit beta type-11 PSB11_HUMAN A5LHX3 MSIMSYNGGAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYTLMSMVANLLYEKRFGPYYTEPVIAGLDPKTFKPFICSLDLIGCPMVTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLFETISQAMLNAVDRDAVSGMGVIVHIIEKDKITTRTLKARMD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QZ9,8QYO,8QYN,8QYM,8QYL,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,9U7R,9U3L,9RKZ,9QVX,9MBQ,9MBP,9HMN,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7B12,7AWE,6XMJ,6WJN,6WJD,6R70,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5T0J,5T0I,5T0H,5T0G,5T0C,5A0Q,4R67,4R3O,22MM,8YVP,8YPK,6TU3,3UNH,3UNF,3UNE,3UNB,8QYS Proteasome subunit beta type-3 PSB3_HUMAN P49720 P31147 Q0P6J7 Q96E27 MEAFLGSRSGLWAGGPAPGQFYRIPSTPDSFMDPASALYRGPITRTQNPMVTGTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNNSTMLGASGDYADFQYLKQVLGQMVIDEELLGDGHSYSPRAIHSWLTRAMYSRRSKMNPLWNTMVIGGYADGESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREVLEKQPVLSQTEARDLVERCMRVLYYRDARSYNRFQIATVTEKGVEIEGPLSTETNWDIAHMISGFE 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9BW4,9BV3,9BV2,9BV1,9BUI,8TM6,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YIZ,8YIY,8YIX,9RKZ,9HMN,8UD9,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,6AVO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,6XMJ,4R67,4R3O,6R70,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,7B12,7AWE,9QVX Proteasome subunit beta type-4 PSB4_HUMAN P28070 B2R9L3 P31148 Q5SZS5 Q6IBI4 Q969L6 MAAVSVYAPPVGGFSFDNCRRNAVLEADFAKRGYKLPKVRKTGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTANRMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAIAAGIFNDLGSGSNIDLCVISKNKLDFLRPYTVPNKKGTRLGRYRCEKGTTAVLTEKITPLEIEVLEETVQTMDTS 8QZ9,8QYN,8QYM,8QYL,8QYJ,9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8TM6,8TM5,8TM4,8QYO,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,9RKZ,9HMN,8UD9,8CVS,8CVR,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,9QVX,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O Proteasome subunit beta type-7 PSB7_HUMAN Q99436 B4E0P1 Q5TBG6 Q96AG8 Q9BWA7 51159634 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 A5LHX3/O14818/P20618/P25786/P25787/P25788/P25789/P28062/P28065/P28066/P28070/P28072/P28074/P40306/P49720/P49721/P60900/Q8TAA3/Q99436 Homo sapiens 68 ChEMBL 10.1016/j.bmcl.2005.02.013 10.7270/Q2CF9SVN 15780623 Momose, I; Umezawa, Y; Hirosawa, S; Iinuma, H; Ikeda, D 4/1/2005 8/23/2020 Numazu Bio-Medical Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000077&target=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 19 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 MALLDVCGAPRGQRPESALPVAGSGRRSDPGHYSFSMRSPELALPRGMQPTEFFQSLGGDGERNVQIEMAHGTTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAIAYATHRDSYSGGVVNMYHMKEDGWVKVESTDVSDLLHQYREANQ 6E5B,6AVO,7B12,7AWE Proteasome subunit beta type-8 PSB8_HUMAN P28062 B0UZC0 Q29824 Q5JNW6 Q5QNR8 Q96J48 MLRAGAPTGDLPRAGEVHTGTTIMAVEFDGGVVMGSDSRVSAGEAVVNRVFDKLSPLHERIYCALSGSAADAQAVADMAAYQLELHGIELEEPPLVLAAANVVRNISYKYREDLSAHLMVAGWDQREGGQVYGTLGGMLTRQPFAIGGSGSTFIYGYVDAAYKPGMSPEECRRFTTDAIALAMSRDGSSGGVIYLVTITAAGVDHRVILGNELPKFYDE 6E5B,7B12,7AWE,6AVO,8YVG,8YSX Proteasome subunit beta type-9 PSB9_HUMAN P28065 B0V0T1 Q16523 Q5JNW4 MAATLLAARGAGPAPAWGPEAFTPDWESREVSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDRIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAASLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTANALALAMERDGSSGGVIRLAAIAESGVERQVLLGDQIPKFAVATLPPA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,9RKZ,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6R70,9QVX,6XMJ,4R67,4R3O,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit beta type-6 PSB6_HUMAN P28072 Q96J55 MFRNQYDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSELAAHQKKILHVDNHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGARSQSARTYLERHMSEFMECNLNELVKHGLRALRETLPAEQDLTTKNVSIGIVGKDLEFTIYDDDDVSPFLEGLEERPQRKAQPAQPADEPAEKADEPMEH 9YUZ,9UG9,9UF8,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9VUG,9VUF,9VUE,9U7R,9U3L,9SZV,9SZT,9MBQ,9MBP,9HEU,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,7DRW,7DR7,7DR6,8YVG,8YSX,8QYS,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,5M32,9QVX Proteasome subunit alpha type-1 PSA1_HUMAN P25786 A8K400 Q53YE8 Q9BRV9 MAERGYSFSLTTFSPSGKLVQIEYALAAVAGGAPSVGIKAANGVVLATEKKQKSILYDERSVHKVEPITKHIGLVYSGMGPDYRVLVHRARKLAQQYYLVYQEPIPTAQLVQRVASVMQEYTQSGGVRPFGVSLLICGWNEGRPYLFQSDPSGAYFAWKATAMGKNYVNGKTFLEKRYNEDLELEDAIHTAILTLKESFEGQMTEDNIEVGICNEAGFRRLTPTEVKDYLAAIA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YVG,8YSX,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYS,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,9U7R,9U3L,9MBQ,9MBP,9HMN,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6XMJ,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,4R67,4R3O,22MM,1IRU,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,6R70,9QVX,7B12,7AWE Proteasome subunit alpha type-2 PSA2_HUMAN P25787 Q6ICS6 Q9BU45 MSSIGTGYDLSASTFSPDGRVFQVEYAMKAVENSSTAIGIRCKDGVVFGVEKLVLSKLYEEGSNKRLFNVDRHVGMAVAGLLADARSLADIAREEASNFRSNFGYNIPLKHLADRVAMYVHAYTLYSAVRPFGCSFMLGSYSVNDGAQLYMIDPSGVSYGYWGCAIGKARQAAKTEIEKLQMKEMTCRDIVKEVAKIIYIVHDEVKDKAFELELSWVGELTNGRHEIVPKDIREEAEKYAKESLKEEDESDDDNM 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7E55,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5DSV,5A0Q,9U7R,9U3L,9MBQ,9MBP,9HMN,8FZ6,8FZ5,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7DRW,7DR7,7DR6,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,1IRU,6TU3,6EPF,6EPE,6EPD,6EPC,8YVP,8YPK,3UNH,3UNF,3UNE,3UNB,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,8QYS,6R70,9QVX Proteasome subunit alpha type-3 PSA3_HUMAN P25788 B2RCK6 Q86U83 Q8N1D8 Q9BS70 MSRRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGEMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTRENGKTVIRVLKQKEVEQLIKKHEEEEAKAEREKKEKEQKEKDK 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,7AWE,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,6R70,8QYS,9QVX Proteasome subunit alpha type-4 PSA4_HUMAN P25789 D3DW86 Q53XP2 Q567Q5 Q8TBD1 MFLTRSEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKTLIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGEEDADPGAMSRPFGVALLFGGVDEKGPQLFHMDPSGTFVQCDARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKLNATNIELATVQPGQNFHMFTKEELEEVIKDI 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDI,9NKJ,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8O,9E8N,9E8L,9E8K,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YVP,8YVG,8YSX,8YPK,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QYO,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,22MM,8QZ9,8QYN,8QYM,8QYL,8QYJ,8QYS,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9QVX,6R70,7B12,7AWE Proteasome subunit alpha type-5 PSA5_HUMAN P28066 B2R8F6 B4E2V4 Q3T1C1 Q6IBF7 MSRGSSAGFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITENIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATAAGVKQTESTSFLEKKVKKKFDWTFEQTVETAITCLSTVLSIDFKPSEIEVGVVTVENPKFRILTEAEIDAHLVALAERD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6TU3,6RGQ,6REY,6KWY,6EPF,6EPE,6EPD,6EPC,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,6XMJ,6R70,4R67,4R3O,7B12,7AWE,9QVX,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit alpha type-6 PSA6_HUMAN P60900 B2R7J9 B4DQR4 B4DXJ9 P34062 Q6IB60 MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIGRGAKSVREFLEKNYTDEAIETDDLTIKLVIKALLEVVQSGGKNIELAVMRRDQSLKILNPEEIEKYVAEIEKEKEENEKKKQKKAS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,22MM,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7AWE,6R70,7B12,8QYS,9QVX Proteasome subunit alpha type-7 PSA7_HUMAN O14818 B2R515 Q5JXJ2 Q9BR53 Q9H4K5 Q9UEU8 MASRYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVCMAFAVLTIFIGLTADARVVINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDAIASDSEAIKLAIKALLEVVQSGGKNIELAIIRRNQPLKMFSAKEVELYVTEIEKEKEEAEKKKSKKSV Proteasome subunit alpha-type 8 PSMA8_HUMAN Q8TAA3 B0YJ75 Q8IVP4 Q8TA98 Q8TAA2 MLKPALEPRGGFSFENCQRNASLERVLPGLKVPHARKTGTTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATVTRILRQTLFRYQGHVGASLIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLLVEAVTAGILGDLGSGGNVDACVITKTGAKLLRTLSSPTEPVKRSGRYHFVPGTTAVLTQTVKPLTLELVEETVQAMEVE 6E5B,6AVO,7AWE Proteasome subunit beta type-10 PSB10_HUMAN P40306 B2R5J4 Q5U098 MALQDVCKWQSPDTQGPSPHLPRAGGWAVPRGCDPQTFLQIHGPRLAHGTTTLAFRFRHGVIAAADTRSSCGSYVACPASCKVIPVHQHLLGTTSGTSADCATWYRVLQRELRLRELREGQLPSVASAAKLLSAMMSQYRGLDLCVATALCGWDRSGPELFYVYSDGTRLQGDIFSVGSGSPYAYGVLDRGYRYDMSTQEAYALARCAVAHATHRDAYSGGSVDLFHVRESGWEHVSRSDACVLYVELQKLLEPEPEEDASHAHPEPATAHRAAEDRELSVGPGEVTPGDSRMPAGTETV Proteasome subunit beta type-11 PSB11_HUMAN A5LHX3 MSIMSYNGGAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYTLMSMVANLLYEKRFGPYYTEPVIAGLDPKTFKPFICSLDLIGCPMVTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLFETISQAMLNAVDRDAVSGMGVIVHIIEKDKITTRTLKARMD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QZ9,8QYO,8QYN,8QYM,8QYL,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,9U7R,9U3L,9RKZ,9QVX,9MBQ,9MBP,9HMN,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7B12,7AWE,6XMJ,6WJN,6WJD,6R70,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5T0J,5T0I,5T0H,5T0G,5T0C,5A0Q,4R67,4R3O,22MM,8YVP,8YPK,6TU3,3UNH,3UNF,3UNE,3UNB,8QYS Proteasome subunit beta type-3 PSB3_HUMAN P49720 P31147 Q0P6J7 Q96E27 MEAFLGSRSGLWAGGPAPGQFYRIPSTPDSFMDPASALYRGPITRTQNPMVTGTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNNSTMLGASGDYADFQYLKQVLGQMVIDEELLGDGHSYSPRAIHSWLTRAMYSRRSKMNPLWNTMVIGGYADGESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREVLEKQPVLSQTEARDLVERCMRVLYYRDARSYNRFQIATVTEKGVEIEGPLSTETNWDIAHMISGFE 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9BW4,9BV3,9BV2,9BV1,9BUI,8TM6,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YIZ,8YIY,8YIX,9RKZ,9HMN,8UD9,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,6AVO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,6XMJ,4R67,4R3O,6R70,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,7B12,7AWE,9QVX Proteasome subunit beta type-4 PSB4_HUMAN P28070 B2R9L3 P31148 Q5SZS5 Q6IBI4 Q969L6 MAAVSVYAPPVGGFSFDNCRRNAVLEADFAKRGYKLPKVRKTGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTANRMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAIAAGIFNDLGSGSNIDLCVISKNKLDFLRPYTVPNKKGTRLGRYRCEKGTTAVLTEKITPLEIEVLEETVQTMDTS 8QZ9,8QYN,8QYM,8QYL,8QYJ,9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8TM6,8TM5,8TM4,8QYO,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,9RKZ,9HMN,8UD9,8CVS,8CVR,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,9QVX,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O Proteasome subunit beta type-7 PSB7_HUMAN Q99436 B4E0P1 Q5TBG6 Q96AG8 Q9BWA7 50028847 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 120 ChEMBL 10.1021/jm00213a022 10.7270/Q26977R0 576620 Song, R; Qiao, W; He, J; Huang, J; Luo, Y; Yang, T 3/25/2021 4/18/2024 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 50029539 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 1080 ChEMBL 10.1021/jm00213a022 10.7270/Q26977R0 576620 Song, R; Qiao, W; He, J; Huang, J; Luo, Y; Yang, T 3/25/2021 4/18/2024 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 50029543 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 1.2 ChEMBL 10.1021/jm00213a022 10.7270/Q26977R0 576620 Song, R; Qiao, W; He, J; Huang, J; Luo, Y; Yang, T 3/25/2021 4/18/2024 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 50494739 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 37 ChEMBL 10.1016/j.bmcl.2016.04.067 10.7270/Q2N018GG 27158142 Yang, L; Wang, W; Sun, Q; Xu, F; Niu, Y; Wang, C; Liang, L; Xu, P 6/15/2016 8/25/2017 Peking University Health Science Center http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 50494751 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 44 ChEMBL 10.1016/j.bmcl.2016.04.067 10.7270/Q2N018GG 27158142 Yang, L; Wang, W; Sun, Q; Xu, F; Niu, Y; Wang, C; Liang, L; Xu, P 6/15/2016 8/25/2017 Peking University Health Science Center http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 50494763 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 52 ChEMBL 10.1016/j.bmcl.2016.04.067 10.7270/Q2N018GG 27158142 Yang, L; Wang, W; Sun, Q; Xu, F; Niu, Y; Wang, C; Liang, L; Xu, P 6/15/2016 8/25/2017 Peking University Health Science Center http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 50521882 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 1.4 ChEMBL 10.1016/j.ejmech.2016.05.049 10.7270/Q28C9Z6K 27318981 Di Giovanni, C; Ettari, R; Sarno, S; Rotondo, A; Bitto, A; Squadrito, F; Altavilla, D; Schirmeister, T; Novellino, E; Grasso, S; Zappalà, M; Lavecchia, A 10/4/2016 7/10/2018 University of Naples Federico Ii http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 50521890 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 22100 ChEMBL 10.1016/j.ejmech.2016.05.049 10.7270/Q28C9Z6K 27318981 Di Giovanni, C; Ettari, R; Sarno, S; Rotondo, A; Bitto, A; Squadrito, F; Altavilla, D; Schirmeister, T; Novellino, E; Grasso, S; Zappalà, M; Lavecchia, A 10/4/2016 7/10/2018 University of Naples Federico Ii http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 50521891 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 5520 ChEMBL 10.1016/j.ejmech.2016.05.049 10.7270/Q28C9Z6K 27318981 Di Giovanni, C; Ettari, R; Sarno, S; Rotondo, A; Bitto, A; Squadrito, F; Altavilla, D; Schirmeister, T; Novellino, E; Grasso, S; Zappalà, M; Lavecchia, A 10/4/2016 7/10/2018 University of Naples Federico Ii http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 50711335 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 25 ChEMBL 10.1016/j.ejmech.2016.11.024 10.7270/Q2Z03BDZ 27889629 Qin, JM; Huang, RZ; Yao, GY; Liao, ZX; Pan, YM; Wang, HS 1/27/2017 6/17/2019 Guangxi Normal University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51002658 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 470 ChEMBL 10.1021/jm058289o 10.7270/Q2FF3S0S 16686537 Rydzewski, RM; Burrill, L; Mendonca, R; Palmer, JT; Rice, M; Tahilramani, R; Bass, KE; Leung, L; Gjerstad, E; Janc, JW; Pan, L 5/11/2006 11/10/2009 Celera http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51002662 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 3.7 ChEMBL 10.1021/jm058289o 10.7270/Q2FF3S0S 16686537 Rydzewski, RM; Burrill, L; Mendonca, R; Palmer, JT; Rice, M; Tahilramani, R; Bass, KE; Leung, L; Gjerstad, E; Janc, JW; Pan, L 5/11/2006 11/10/2009 Celera http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51002664 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 330 ChEMBL 10.1021/jm058289o 10.7270/Q2FF3S0S 16686537 Rydzewski, RM; Burrill, L; Mendonca, R; Palmer, JT; Rice, M; Tahilramani, R; Bass, KE; Leung, L; Gjerstad, E; Janc, JW; Pan, L 5/11/2006 11/10/2009 Celera http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51087096 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 2100 ChEMBL 10.1016/j.ejmech.2013.11.009 10.7270/Q2222W81 24321833 Hasegawa, M; Yasuda, Y; Tanaka, M; Nakata, K; Umeda, E; Wang, Y; Watanabe, C; Uetake, S; Kunoh, T; Shionyu, M; Sasaki, R; Shiina, I; Mizukami, T 1/31/2014 7/25/2014 Institute of Bio-Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51087151 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 120 ChEMBL 10.1016/j.ejmech.2013.11.009 10.7270/Q2222W81 24321833 Hasegawa, M; Yasuda, Y; Tanaka, M; Nakata, K; Umeda, E; Wang, Y; Watanabe, C; Uetake, S; Kunoh, T; Shionyu, M; Sasaki, R; Shiina, I; Mizukami, T 1/31/2014 7/25/2014 Institute of Bio-Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51087152 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 11 ChEMBL 10.1016/j.ejmech.2013.11.009 10.7270/Q2222W81 24321833 Hasegawa, M; Yasuda, Y; Tanaka, M; Nakata, K; Umeda, E; Wang, Y; Watanabe, C; Uetake, S; Kunoh, T; Shionyu, M; Sasaki, R; Shiina, I; Mizukami, T 1/31/2014 7/25/2014 Institute of Bio-Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51110847 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 1.000000 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51110850 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 5520 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51110852 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 22100 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51110856 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 4.0 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51110862 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 130 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51110863 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 70 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51227585 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 1.2 ChEMBL 10.1016/j.bmc.2018.12.022 10.7270/Q2NP27P1 30581047 Pehere, AD; Nguyen, S; Garlick, SK; Wilson, DW; Hudson, I; Sykes, MJ; Morton, JD; Abell, AD 1/15/2019 2/18/2021 University of Adelaide http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51289132 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 1450 ChEMBL 10.1021/acsmedchemlett.9b00233 10.7270/Q2930XK7 31312413 Pacifico, S; Ferretti, V; Albanese, V; Fantinati, A; Gallerani, E; Nicoli, F; Gavioli, R; Zamberlan, F; Preti, D; Marastoni, M 7/11/2019 2/24/2021 University of Ferrara http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51289181 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 4590 ChEMBL 10.1021/acsmedchemlett.9b00233 10.7270/Q2930XK7 31312413 Pacifico, S; Ferretti, V; Albanese, V; Fantinati, A; Gallerani, E; Nicoli, F; Gavioli, R; Zamberlan, F; Preti, D; Marastoni, M 7/11/2019 2/24/2021 University of Ferrara http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51289196 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 7.0 ChEMBL 10.1021/acsmedchemlett.9b00233 10.7270/Q2930XK7 31312413 Pacifico, S; Ferretti, V; Albanese, V; Fantinati, A; Gallerani, E; Nicoli, F; Gavioli, R; Zamberlan, F; Preti, D; Marastoni, M 7/11/2019 2/24/2021 University of Ferrara http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51298902 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 30 ChEMBL 10.1016/j.bmc.2019.115161 10.7270/Q29W0JZJ 31732281 Uesugi, S; Honmura, Y; Nishiyama, M; Kusakabe, K; Tonouchi, A; Yamashita, T; Hashimoto, M; Kimura, KI 12/15/2019 2/25/2021 Iwate University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51298906 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 1600 ChEMBL 10.1016/j.bmc.2019.115161 10.7270/Q29W0JZJ 31732281 Uesugi, S; Honmura, Y; Nishiyama, M; Kusakabe, K; Tonouchi, A; Yamashita, T; Hashimoto, M; Kimura, KI 12/15/2019 2/25/2021 Iwate University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51298909 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 500 ChEMBL 10.1016/j.bmc.2019.115161 10.7270/Q29W0JZJ 31732281 Uesugi, S; Honmura, Y; Nishiyama, M; Kusakabe, K; Tonouchi, A; Yamashita, T; Hashimoto, M; Kimura, KI 12/15/2019 2/25/2021 Iwate University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51487773 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 22100 ChEMBL 10.7270/Q20R9TGT 34838650 Ettari, R; Iraci, N; Di Chio, C; Previti, S; Danzè, M; Zappalà, M 1/1/2022 6/23/2023 University of Messina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51487774 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 5520 ChEMBL 10.7270/Q20R9TGT 34838650 Ettari, R; Iraci, N; Di Chio, C; Previti, S; Danzè, M; Zappalà, M 1/1/2022 6/23/2023 University of Messina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51487775 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 1.4 ChEMBL 10.7270/Q20R9TGT 34838650 Ettari, R; Iraci, N; Di Chio, C; Previti, S; Danzè, M; Zappalà, M 1/1/2022 6/23/2023 University of Messina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51487776 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 130 ChEMBL 10.7270/Q20R9TGT 34838650 Ettari, R; Iraci, N; Di Chio, C; Previti, S; Danzè, M; Zappalà, M 1/1/2022 6/23/2023 University of Messina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51487777 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 1.000000 ChEMBL 10.7270/Q20R9TGT 34838650 Ettari, R; Iraci, N; Di Chio, C; Previti, S; Danzè, M; Zappalà, M 1/1/2022 6/23/2023 University of Messina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51159619 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 A5LHX3/O14818/P20618/P25786/P25787/P25788/P25789/P28062/P28065/P28066/P28070/P28072/P28074/P40306/P49720/P49721/P60900/Q8TAA3/Q99436 Homo sapiens 4500 ChEMBL 10.1016/j.bmcl.2005.02.013 10.7270/Q2CF9SVN 15780623 Momose, I; Umezawa, Y; Hirosawa, S; Iinuma, H; Ikeda, D 4/1/2005 8/23/2020 Numazu Bio-Medical Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000077&target=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 19 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 MALLDVCGAPRGQRPESALPVAGSGRRSDPGHYSFSMRSPELALPRGMQPTEFFQSLGGDGERNVQIEMAHGTTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAIAYATHRDSYSGGVVNMYHMKEDGWVKVESTDVSDLLHQYREANQ 6E5B,6AVO,7B12,7AWE Proteasome subunit beta type-8 PSB8_HUMAN P28062 B0UZC0 Q29824 Q5JNW6 Q5QNR8 Q96J48 MLRAGAPTGDLPRAGEVHTGTTIMAVEFDGGVVMGSDSRVSAGEAVVNRVFDKLSPLHERIYCALSGSAADAQAVADMAAYQLELHGIELEEPPLVLAAANVVRNISYKYREDLSAHLMVAGWDQREGGQVYGTLGGMLTRQPFAIGGSGSTFIYGYVDAAYKPGMSPEECRRFTTDAIALAMSRDGSSGGVIYLVTITAAGVDHRVILGNELPKFYDE 6E5B,7B12,7AWE,6AVO,8YVG,8YSX Proteasome subunit beta type-9 PSB9_HUMAN P28065 B0V0T1 Q16523 Q5JNW4 MAATLLAARGAGPAPAWGPEAFTPDWESREVSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDRIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAASLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTANALALAMERDGSSGGVIRLAAIAESGVERQVLLGDQIPKFAVATLPPA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,9RKZ,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6R70,9QVX,6XMJ,4R67,4R3O,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit beta type-6 PSB6_HUMAN P28072 Q96J55 MFRNQYDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSELAAHQKKILHVDNHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGARSQSARTYLERHMSEFMECNLNELVKHGLRALRETLPAEQDLTTKNVSIGIVGKDLEFTIYDDDDVSPFLEGLEERPQRKAQPAQPADEPAEKADEPMEH 9YUZ,9UG9,9UF8,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9VUG,9VUF,9VUE,9U7R,9U3L,9SZV,9SZT,9MBQ,9MBP,9HEU,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,7DRW,7DR7,7DR6,8YVG,8YSX,8QYS,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,5M32,9QVX Proteasome subunit alpha type-1 PSA1_HUMAN P25786 A8K400 Q53YE8 Q9BRV9 MAERGYSFSLTTFSPSGKLVQIEYALAAVAGGAPSVGIKAANGVVLATEKKQKSILYDERSVHKVEPITKHIGLVYSGMGPDYRVLVHRARKLAQQYYLVYQEPIPTAQLVQRVASVMQEYTQSGGVRPFGVSLLICGWNEGRPYLFQSDPSGAYFAWKATAMGKNYVNGKTFLEKRYNEDLELEDAIHTAILTLKESFEGQMTEDNIEVGICNEAGFRRLTPTEVKDYLAAIA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YVG,8YSX,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYS,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,9U7R,9U3L,9MBQ,9MBP,9HMN,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6XMJ,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,4R67,4R3O,22MM,1IRU,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,6R70,9QVX,7B12,7AWE Proteasome subunit alpha type-2 PSA2_HUMAN P25787 Q6ICS6 Q9BU45 MSSIGTGYDLSASTFSPDGRVFQVEYAMKAVENSSTAIGIRCKDGVVFGVEKLVLSKLYEEGSNKRLFNVDRHVGMAVAGLLADARSLADIAREEASNFRSNFGYNIPLKHLADRVAMYVHAYTLYSAVRPFGCSFMLGSYSVNDGAQLYMIDPSGVSYGYWGCAIGKARQAAKTEIEKLQMKEMTCRDIVKEVAKIIYIVHDEVKDKAFELELSWVGELTNGRHEIVPKDIREEAEKYAKESLKEEDESDDDNM 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7E55,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5DSV,5A0Q,9U7R,9U3L,9MBQ,9MBP,9HMN,8FZ6,8FZ5,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7DRW,7DR7,7DR6,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,1IRU,6TU3,6EPF,6EPE,6EPD,6EPC,8YVP,8YPK,3UNH,3UNF,3UNE,3UNB,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,8QYS,6R70,9QVX Proteasome subunit alpha type-3 PSA3_HUMAN P25788 B2RCK6 Q86U83 Q8N1D8 Q9BS70 MSRRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGEMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTRENGKTVIRVLKQKEVEQLIKKHEEEEAKAEREKKEKEQKEKDK 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,7AWE,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,6R70,8QYS,9QVX Proteasome subunit alpha type-4 PSA4_HUMAN P25789 D3DW86 Q53XP2 Q567Q5 Q8TBD1 MFLTRSEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKTLIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGEEDADPGAMSRPFGVALLFGGVDEKGPQLFHMDPSGTFVQCDARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKLNATNIELATVQPGQNFHMFTKEELEEVIKDI 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDI,9NKJ,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8O,9E8N,9E8L,9E8K,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YVP,8YVG,8YSX,8YPK,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QYO,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,22MM,8QZ9,8QYN,8QYM,8QYL,8QYJ,8QYS,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9QVX,6R70,7B12,7AWE Proteasome subunit alpha type-5 PSA5_HUMAN P28066 B2R8F6 B4E2V4 Q3T1C1 Q6IBF7 MSRGSSAGFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITENIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATAAGVKQTESTSFLEKKVKKKFDWTFEQTVETAITCLSTVLSIDFKPSEIEVGVVTVENPKFRILTEAEIDAHLVALAERD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6TU3,6RGQ,6REY,6KWY,6EPF,6EPE,6EPD,6EPC,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,6XMJ,6R70,4R67,4R3O,7B12,7AWE,9QVX,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit alpha type-6 PSA6_HUMAN P60900 B2R7J9 B4DQR4 B4DXJ9 P34062 Q6IB60 MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIGRGAKSVREFLEKNYTDEAIETDDLTIKLVIKALLEVVQSGGKNIELAVMRRDQSLKILNPEEIEKYVAEIEKEKEENEKKKQKKAS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,22MM,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7AWE,6R70,7B12,8QYS,9QVX Proteasome subunit alpha type-7 PSA7_HUMAN O14818 B2R515 Q5JXJ2 Q9BR53 Q9H4K5 Q9UEU8 MASRYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVCMAFAVLTIFIGLTADARVVINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDAIASDSEAIKLAIKALLEVVQSGGKNIELAIIRRNQPLKMFSAKEVELYVTEIEKEKEEAEKKKSKKSV Proteasome subunit alpha-type 8 PSMA8_HUMAN Q8TAA3 B0YJ75 Q8IVP4 Q8TA98 Q8TAA2 MLKPALEPRGGFSFENCQRNASLERVLPGLKVPHARKTGTTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATVTRILRQTLFRYQGHVGASLIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLLVEAVTAGILGDLGSGGNVDACVITKTGAKLLRTLSSPTEPVKRSGRYHFVPGTTAVLTQTVKPLTLELVEETVQAMEVE 6E5B,6AVO,7AWE Proteasome subunit beta type-10 PSB10_HUMAN P40306 B2R5J4 Q5U098 MALQDVCKWQSPDTQGPSPHLPRAGGWAVPRGCDPQTFLQIHGPRLAHGTTTLAFRFRHGVIAAADTRSSCGSYVACPASCKVIPVHQHLLGTTSGTSADCATWYRVLQRELRLRELREGQLPSVASAAKLLSAMMSQYRGLDLCVATALCGWDRSGPELFYVYSDGTRLQGDIFSVGSGSPYAYGVLDRGYRYDMSTQEAYALARCAVAHATHRDAYSGGSVDLFHVRESGWEHVSRSDACVLYVELQKLLEPEPEEDASHAHPEPATAHRAAEDRELSVGPGEVTPGDSRMPAGTETV Proteasome subunit beta type-11 PSB11_HUMAN A5LHX3 MSIMSYNGGAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYTLMSMVANLLYEKRFGPYYTEPVIAGLDPKTFKPFICSLDLIGCPMVTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLFETISQAMLNAVDRDAVSGMGVIVHIIEKDKITTRTLKARMD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QZ9,8QYO,8QYN,8QYM,8QYL,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,9U7R,9U3L,9RKZ,9QVX,9MBQ,9MBP,9HMN,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7B12,7AWE,6XMJ,6WJN,6WJD,6R70,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5T0J,5T0I,5T0H,5T0G,5T0C,5A0Q,4R67,4R3O,22MM,8YVP,8YPK,6TU3,3UNH,3UNF,3UNE,3UNB,8QYS Proteasome subunit beta type-3 PSB3_HUMAN P49720 P31147 Q0P6J7 Q96E27 MEAFLGSRSGLWAGGPAPGQFYRIPSTPDSFMDPASALYRGPITRTQNPMVTGTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNNSTMLGASGDYADFQYLKQVLGQMVIDEELLGDGHSYSPRAIHSWLTRAMYSRRSKMNPLWNTMVIGGYADGESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREVLEKQPVLSQTEARDLVERCMRVLYYRDARSYNRFQIATVTEKGVEIEGPLSTETNWDIAHMISGFE 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9BW4,9BV3,9BV2,9BV1,9BUI,8TM6,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YIZ,8YIY,8YIX,9RKZ,9HMN,8UD9,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,6AVO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,6XMJ,4R67,4R3O,6R70,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,7B12,7AWE,9QVX Proteasome subunit beta type-4 PSB4_HUMAN P28070 B2R9L3 P31148 Q5SZS5 Q6IBI4 Q969L6 MAAVSVYAPPVGGFSFDNCRRNAVLEADFAKRGYKLPKVRKTGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTANRMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAIAAGIFNDLGSGSNIDLCVISKNKLDFLRPYTVPNKKGTRLGRYRCEKGTTAVLTEKITPLEIEVLEETVQTMDTS 8QZ9,8QYN,8QYM,8QYL,8QYJ,9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8TM6,8TM5,8TM4,8QYO,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,9RKZ,9HMN,8UD9,8CVS,8CVR,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,9QVX,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O Proteasome subunit beta type-7 PSB7_HUMAN Q99436 B4E0P1 Q5TBG6 Q96AG8 Q9BWA7 51159624 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 A5LHX3/O14818/P20618/P25786/P25787/P25788/P25789/P28062/P28065/P28066/P28070/P28072/P28074/P40306/P49720/P49721/P60900/Q8TAA3/Q99436 Homo sapiens 1400 ChEMBL 10.1016/j.bmcl.2005.02.013 10.7270/Q2CF9SVN 15780623 Momose, I; Umezawa, Y; Hirosawa, S; Iinuma, H; Ikeda, D 4/1/2005 8/23/2020 Numazu Bio-Medical Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000077&target=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 19 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 MALLDVCGAPRGQRPESALPVAGSGRRSDPGHYSFSMRSPELALPRGMQPTEFFQSLGGDGERNVQIEMAHGTTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAIAYATHRDSYSGGVVNMYHMKEDGWVKVESTDVSDLLHQYREANQ 6E5B,6AVO,7B12,7AWE Proteasome subunit beta type-8 PSB8_HUMAN P28062 B0UZC0 Q29824 Q5JNW6 Q5QNR8 Q96J48 MLRAGAPTGDLPRAGEVHTGTTIMAVEFDGGVVMGSDSRVSAGEAVVNRVFDKLSPLHERIYCALSGSAADAQAVADMAAYQLELHGIELEEPPLVLAAANVVRNISYKYREDLSAHLMVAGWDQREGGQVYGTLGGMLTRQPFAIGGSGSTFIYGYVDAAYKPGMSPEECRRFTTDAIALAMSRDGSSGGVIYLVTITAAGVDHRVILGNELPKFYDE 6E5B,7B12,7AWE,6AVO,8YVG,8YSX Proteasome subunit beta type-9 PSB9_HUMAN P28065 B0V0T1 Q16523 Q5JNW4 MAATLLAARGAGPAPAWGPEAFTPDWESREVSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDRIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAASLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTANALALAMERDGSSGGVIRLAAIAESGVERQVLLGDQIPKFAVATLPPA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,9RKZ,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6R70,9QVX,6XMJ,4R67,4R3O,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit beta type-6 PSB6_HUMAN P28072 Q96J55 MFRNQYDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSELAAHQKKILHVDNHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGARSQSARTYLERHMSEFMECNLNELVKHGLRALRETLPAEQDLTTKNVSIGIVGKDLEFTIYDDDDVSPFLEGLEERPQRKAQPAQPADEPAEKADEPMEH 9YUZ,9UG9,9UF8,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9VUG,9VUF,9VUE,9U7R,9U3L,9SZV,9SZT,9MBQ,9MBP,9HEU,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,7DRW,7DR7,7DR6,8YVG,8YSX,8QYS,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,5M32,9QVX Proteasome subunit alpha type-1 PSA1_HUMAN P25786 A8K400 Q53YE8 Q9BRV9 MAERGYSFSLTTFSPSGKLVQIEYALAAVAGGAPSVGIKAANGVVLATEKKQKSILYDERSVHKVEPITKHIGLVYSGMGPDYRVLVHRARKLAQQYYLVYQEPIPTAQLVQRVASVMQEYTQSGGVRPFGVSLLICGWNEGRPYLFQSDPSGAYFAWKATAMGKNYVNGKTFLEKRYNEDLELEDAIHTAILTLKESFEGQMTEDNIEVGICNEAGFRRLTPTEVKDYLAAIA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YVG,8YSX,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYS,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,9U7R,9U3L,9MBQ,9MBP,9HMN,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6XMJ,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,4R67,4R3O,22MM,1IRU,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,6R70,9QVX,7B12,7AWE Proteasome subunit alpha type-2 PSA2_HUMAN P25787 Q6ICS6 Q9BU45 MSSIGTGYDLSASTFSPDGRVFQVEYAMKAVENSSTAIGIRCKDGVVFGVEKLVLSKLYEEGSNKRLFNVDRHVGMAVAGLLADARSLADIAREEASNFRSNFGYNIPLKHLADRVAMYVHAYTLYSAVRPFGCSFMLGSYSVNDGAQLYMIDPSGVSYGYWGCAIGKARQAAKTEIEKLQMKEMTCRDIVKEVAKIIYIVHDEVKDKAFELELSWVGELTNGRHEIVPKDIREEAEKYAKESLKEEDESDDDNM 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7E55,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5DSV,5A0Q,9U7R,9U3L,9MBQ,9MBP,9HMN,8FZ6,8FZ5,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7DRW,7DR7,7DR6,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,1IRU,6TU3,6EPF,6EPE,6EPD,6EPC,8YVP,8YPK,3UNH,3UNF,3UNE,3UNB,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,8QYS,6R70,9QVX Proteasome subunit alpha type-3 PSA3_HUMAN P25788 B2RCK6 Q86U83 Q8N1D8 Q9BS70 MSRRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGEMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTRENGKTVIRVLKQKEVEQLIKKHEEEEAKAEREKKEKEQKEKDK 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,7AWE,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,6R70,8QYS,9QVX Proteasome subunit alpha type-4 PSA4_HUMAN P25789 D3DW86 Q53XP2 Q567Q5 Q8TBD1 MFLTRSEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKTLIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGEEDADPGAMSRPFGVALLFGGVDEKGPQLFHMDPSGTFVQCDARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKLNATNIELATVQPGQNFHMFTKEELEEVIKDI 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDI,9NKJ,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8O,9E8N,9E8L,9E8K,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YVP,8YVG,8YSX,8YPK,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QYO,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,22MM,8QZ9,8QYN,8QYM,8QYL,8QYJ,8QYS,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9QVX,6R70,7B12,7AWE Proteasome subunit alpha type-5 PSA5_HUMAN P28066 B2R8F6 B4E2V4 Q3T1C1 Q6IBF7 MSRGSSAGFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITENIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATAAGVKQTESTSFLEKKVKKKFDWTFEQTVETAITCLSTVLSIDFKPSEIEVGVVTVENPKFRILTEAEIDAHLVALAERD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6TU3,6RGQ,6REY,6KWY,6EPF,6EPE,6EPD,6EPC,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,6XMJ,6R70,4R67,4R3O,7B12,7AWE,9QVX,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit alpha type-6 PSA6_HUMAN P60900 B2R7J9 B4DQR4 B4DXJ9 P34062 Q6IB60 MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIGRGAKSVREFLEKNYTDEAIETDDLTIKLVIKALLEVVQSGGKNIELAVMRRDQSLKILNPEEIEKYVAEIEKEKEENEKKKQKKAS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,22MM,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7AWE,6R70,7B12,8QYS,9QVX Proteasome subunit alpha type-7 PSA7_HUMAN O14818 B2R515 Q5JXJ2 Q9BR53 Q9H4K5 Q9UEU8 MASRYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVCMAFAVLTIFIGLTADARVVINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDAIASDSEAIKLAIKALLEVVQSGGKNIELAIIRRNQPLKMFSAKEVELYVTEIEKEKEEAEKKKSKKSV Proteasome subunit alpha-type 8 PSMA8_HUMAN Q8TAA3 B0YJ75 Q8IVP4 Q8TA98 Q8TAA2 MLKPALEPRGGFSFENCQRNASLERVLPGLKVPHARKTGTTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATVTRILRQTLFRYQGHVGASLIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLLVEAVTAGILGDLGSGGNVDACVITKTGAKLLRTLSSPTEPVKRSGRYHFVPGTTAVLTQTVKPLTLELVEETVQAMEVE 6E5B,6AVO,7AWE Proteasome subunit beta type-10 PSB10_HUMAN P40306 B2R5J4 Q5U098 MALQDVCKWQSPDTQGPSPHLPRAGGWAVPRGCDPQTFLQIHGPRLAHGTTTLAFRFRHGVIAAADTRSSCGSYVACPASCKVIPVHQHLLGTTSGTSADCATWYRVLQRELRLRELREGQLPSVASAAKLLSAMMSQYRGLDLCVATALCGWDRSGPELFYVYSDGTRLQGDIFSVGSGSPYAYGVLDRGYRYDMSTQEAYALARCAVAHATHRDAYSGGSVDLFHVRESGWEHVSRSDACVLYVELQKLLEPEPEEDASHAHPEPATAHRAAEDRELSVGPGEVTPGDSRMPAGTETV Proteasome subunit beta type-11 PSB11_HUMAN A5LHX3 MSIMSYNGGAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYTLMSMVANLLYEKRFGPYYTEPVIAGLDPKTFKPFICSLDLIGCPMVTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLFETISQAMLNAVDRDAVSGMGVIVHIIEKDKITTRTLKARMD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QZ9,8QYO,8QYN,8QYM,8QYL,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,9U7R,9U3L,9RKZ,9QVX,9MBQ,9MBP,9HMN,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7B12,7AWE,6XMJ,6WJN,6WJD,6R70,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5T0J,5T0I,5T0H,5T0G,5T0C,5A0Q,4R67,4R3O,22MM,8YVP,8YPK,6TU3,3UNH,3UNF,3UNE,3UNB,8QYS Proteasome subunit beta type-3 PSB3_HUMAN P49720 P31147 Q0P6J7 Q96E27 MEAFLGSRSGLWAGGPAPGQFYRIPSTPDSFMDPASALYRGPITRTQNPMVTGTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNNSTMLGASGDYADFQYLKQVLGQMVIDEELLGDGHSYSPRAIHSWLTRAMYSRRSKMNPLWNTMVIGGYADGESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREVLEKQPVLSQTEARDLVERCMRVLYYRDARSYNRFQIATVTEKGVEIEGPLSTETNWDIAHMISGFE 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9BW4,9BV3,9BV2,9BV1,9BUI,8TM6,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YIZ,8YIY,8YIX,9RKZ,9HMN,8UD9,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,6AVO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,6XMJ,4R67,4R3O,6R70,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,7B12,7AWE,9QVX Proteasome subunit beta type-4 PSB4_HUMAN P28070 B2R9L3 P31148 Q5SZS5 Q6IBI4 Q969L6 MAAVSVYAPPVGGFSFDNCRRNAVLEADFAKRGYKLPKVRKTGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTANRMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAIAAGIFNDLGSGSNIDLCVISKNKLDFLRPYTVPNKKGTRLGRYRCEKGTTAVLTEKITPLEIEVLEETVQTMDTS 8QZ9,8QYN,8QYM,8QYL,8QYJ,9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8TM6,8TM5,8TM4,8QYO,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,9RKZ,9HMN,8UD9,8CVS,8CVR,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,9QVX,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O Proteasome subunit beta type-7 PSB7_HUMAN Q99436 B4E0P1 Q5TBG6 Q96AG8 Q9BWA7 51159634 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 A5LHX3/O14818/P20618/P25786/P25787/P25788/P25789/P28062/P28065/P28066/P28070/P28072/P28074/P40306/P49720/P49721/P60900/Q8TAA3/Q99436 Homo sapiens 68 ChEMBL 10.1016/j.bmcl.2005.02.013 10.7270/Q2CF9SVN 15780623 Momose, I; Umezawa, Y; Hirosawa, S; Iinuma, H; Ikeda, D 4/1/2005 8/23/2020 Numazu Bio-Medical Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000077&target=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 19 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 MALLDVCGAPRGQRPESALPVAGSGRRSDPGHYSFSMRSPELALPRGMQPTEFFQSLGGDGERNVQIEMAHGTTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAIAYATHRDSYSGGVVNMYHMKEDGWVKVESTDVSDLLHQYREANQ 6E5B,6AVO,7B12,7AWE Proteasome subunit beta type-8 PSB8_HUMAN P28062 B0UZC0 Q29824 Q5JNW6 Q5QNR8 Q96J48 MLRAGAPTGDLPRAGEVHTGTTIMAVEFDGGVVMGSDSRVSAGEAVVNRVFDKLSPLHERIYCALSGSAADAQAVADMAAYQLELHGIELEEPPLVLAAANVVRNISYKYREDLSAHLMVAGWDQREGGQVYGTLGGMLTRQPFAIGGSGSTFIYGYVDAAYKPGMSPEECRRFTTDAIALAMSRDGSSGGVIYLVTITAAGVDHRVILGNELPKFYDE 6E5B,7B12,7AWE,6AVO,8YVG,8YSX Proteasome subunit beta type-9 PSB9_HUMAN P28065 B0V0T1 Q16523 Q5JNW4 MAATLLAARGAGPAPAWGPEAFTPDWESREVSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDRIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAASLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTANALALAMERDGSSGGVIRLAAIAESGVERQVLLGDQIPKFAVATLPPA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,9RKZ,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6R70,9QVX,6XMJ,4R67,4R3O,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit beta type-6 PSB6_HUMAN P28072 Q96J55 MFRNQYDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSELAAHQKKILHVDNHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGARSQSARTYLERHMSEFMECNLNELVKHGLRALRETLPAEQDLTTKNVSIGIVGKDLEFTIYDDDDVSPFLEGLEERPQRKAQPAQPADEPAEKADEPMEH 9YUZ,9UG9,9UF8,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9VUG,9VUF,9VUE,9U7R,9U3L,9SZV,9SZT,9MBQ,9MBP,9HEU,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,7DRW,7DR7,7DR6,8YVG,8YSX,8QYS,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,5M32,9QVX Proteasome subunit alpha type-1 PSA1_HUMAN P25786 A8K400 Q53YE8 Q9BRV9 MAERGYSFSLTTFSPSGKLVQIEYALAAVAGGAPSVGIKAANGVVLATEKKQKSILYDERSVHKVEPITKHIGLVYSGMGPDYRVLVHRARKLAQQYYLVYQEPIPTAQLVQRVASVMQEYTQSGGVRPFGVSLLICGWNEGRPYLFQSDPSGAYFAWKATAMGKNYVNGKTFLEKRYNEDLELEDAIHTAILTLKESFEGQMTEDNIEVGICNEAGFRRLTPTEVKDYLAAIA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YVG,8YSX,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYS,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,9U7R,9U3L,9MBQ,9MBP,9HMN,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6XMJ,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,4R67,4R3O,22MM,1IRU,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,6R70,9QVX,7B12,7AWE Proteasome subunit alpha type-2 PSA2_HUMAN P25787 Q6ICS6 Q9BU45 MSSIGTGYDLSASTFSPDGRVFQVEYAMKAVENSSTAIGIRCKDGVVFGVEKLVLSKLYEEGSNKRLFNVDRHVGMAVAGLLADARSLADIAREEASNFRSNFGYNIPLKHLADRVAMYVHAYTLYSAVRPFGCSFMLGSYSVNDGAQLYMIDPSGVSYGYWGCAIGKARQAAKTEIEKLQMKEMTCRDIVKEVAKIIYIVHDEVKDKAFELELSWVGELTNGRHEIVPKDIREEAEKYAKESLKEEDESDDDNM 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7E55,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5DSV,5A0Q,9U7R,9U3L,9MBQ,9MBP,9HMN,8FZ6,8FZ5,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7DRW,7DR7,7DR6,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,1IRU,6TU3,6EPF,6EPE,6EPD,6EPC,8YVP,8YPK,3UNH,3UNF,3UNE,3UNB,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,8QYS,6R70,9QVX Proteasome subunit alpha type-3 PSA3_HUMAN P25788 B2RCK6 Q86U83 Q8N1D8 Q9BS70 MSRRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGEMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTRENGKTVIRVLKQKEVEQLIKKHEEEEAKAEREKKEKEQKEKDK 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,7AWE,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,6R70,8QYS,9QVX Proteasome subunit alpha type-4 PSA4_HUMAN P25789 D3DW86 Q53XP2 Q567Q5 Q8TBD1 MFLTRSEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKTLIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGEEDADPGAMSRPFGVALLFGGVDEKGPQLFHMDPSGTFVQCDARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKLNATNIELATVQPGQNFHMFTKEELEEVIKDI 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDI,9NKJ,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8O,9E8N,9E8L,9E8K,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YVP,8YVG,8YSX,8YPK,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QYO,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,22MM,8QZ9,8QYN,8QYM,8QYL,8QYJ,8QYS,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9QVX,6R70,7B12,7AWE Proteasome subunit alpha type-5 PSA5_HUMAN P28066 B2R8F6 B4E2V4 Q3T1C1 Q6IBF7 MSRGSSAGFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITENIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATAAGVKQTESTSFLEKKVKKKFDWTFEQTVETAITCLSTVLSIDFKPSEIEVGVVTVENPKFRILTEAEIDAHLVALAERD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6TU3,6RGQ,6REY,6KWY,6EPF,6EPE,6EPD,6EPC,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,6XMJ,6R70,4R67,4R3O,7B12,7AWE,9QVX,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit alpha type-6 PSA6_HUMAN P60900 B2R7J9 B4DQR4 B4DXJ9 P34062 Q6IB60 MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIGRGAKSVREFLEKNYTDEAIETDDLTIKLVIKALLEVVQSGGKNIELAVMRRDQSLKILNPEEIEKYVAEIEKEKEENEKKKQKKAS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,22MM,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7AWE,6R70,7B12,8QYS,9QVX Proteasome subunit alpha type-7 PSA7_HUMAN O14818 B2R515 Q5JXJ2 Q9BR53 Q9H4K5 Q9UEU8 MASRYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVCMAFAVLTIFIGLTADARVVINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDAIASDSEAIKLAIKALLEVVQSGGKNIELAIIRRNQPLKMFSAKEVELYVTEIEKEKEEAEKKKSKKSV Proteasome subunit alpha-type 8 PSMA8_HUMAN Q8TAA3 B0YJ75 Q8IVP4 Q8TA98 Q8TAA2 MLKPALEPRGGFSFENCQRNASLERVLPGLKVPHARKTGTTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATVTRILRQTLFRYQGHVGASLIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLLVEAVTAGILGDLGSGGNVDACVITKTGAKLLRTLSSPTEPVKRSGRYHFVPGTTAVLTQTVKPLTLELVEETVQAMEVE 6E5B,6AVO,7AWE Proteasome subunit beta type-10 PSB10_HUMAN P40306 B2R5J4 Q5U098 MALQDVCKWQSPDTQGPSPHLPRAGGWAVPRGCDPQTFLQIHGPRLAHGTTTLAFRFRHGVIAAADTRSSCGSYVACPASCKVIPVHQHLLGTTSGTSADCATWYRVLQRELRLRELREGQLPSVASAAKLLSAMMSQYRGLDLCVATALCGWDRSGPELFYVYSDGTRLQGDIFSVGSGSPYAYGVLDRGYRYDMSTQEAYALARCAVAHATHRDAYSGGSVDLFHVRESGWEHVSRSDACVLYVELQKLLEPEPEEDASHAHPEPATAHRAAEDRELSVGPGEVTPGDSRMPAGTETV Proteasome subunit beta type-11 PSB11_HUMAN A5LHX3 MSIMSYNGGAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYTLMSMVANLLYEKRFGPYYTEPVIAGLDPKTFKPFICSLDLIGCPMVTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLFETISQAMLNAVDRDAVSGMGVIVHIIEKDKITTRTLKARMD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QZ9,8QYO,8QYN,8QYM,8QYL,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,9U7R,9U3L,9RKZ,9QVX,9MBQ,9MBP,9HMN,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7B12,7AWE,6XMJ,6WJN,6WJD,6R70,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5T0J,5T0I,5T0H,5T0G,5T0C,5A0Q,4R67,4R3O,22MM,8YVP,8YPK,6TU3,3UNH,3UNF,3UNE,3UNB,8QYS Proteasome subunit beta type-3 PSB3_HUMAN P49720 P31147 Q0P6J7 Q96E27 MEAFLGSRSGLWAGGPAPGQFYRIPSTPDSFMDPASALYRGPITRTQNPMVTGTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNNSTMLGASGDYADFQYLKQVLGQMVIDEELLGDGHSYSPRAIHSWLTRAMYSRRSKMNPLWNTMVIGGYADGESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREVLEKQPVLSQTEARDLVERCMRVLYYRDARSYNRFQIATVTEKGVEIEGPLSTETNWDIAHMISGFE 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9BW4,9BV3,9BV2,9BV1,9BUI,8TM6,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YIZ,8YIY,8YIX,9RKZ,9HMN,8UD9,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,6AVO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,6XMJ,4R67,4R3O,6R70,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,7B12,7AWE,9QVX Proteasome subunit beta type-4 PSB4_HUMAN P28070 B2R9L3 P31148 Q5SZS5 Q6IBI4 Q969L6 MAAVSVYAPPVGGFSFDNCRRNAVLEADFAKRGYKLPKVRKTGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTANRMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAIAAGIFNDLGSGSNIDLCVISKNKLDFLRPYTVPNKKGTRLGRYRCEKGTTAVLTEKITPLEIEVLEETVQTMDTS 8QZ9,8QYN,8QYM,8QYL,8QYJ,9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8TM6,8TM5,8TM4,8QYO,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,9RKZ,9HMN,8UD9,8CVS,8CVR,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,9QVX,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O Proteasome subunit beta type-7 PSB7_HUMAN Q99436 B4E0P1 Q5TBG6 Q96AG8 Q9BWA7 50028847 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 120 ChEMBL 10.1021/jm00213a022 10.7270/Q26977R0 576620 Song, R; Qiao, W; He, J; Huang, J; Luo, Y; Yang, T 3/25/2021 4/18/2024 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 50029539 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 1080 ChEMBL 10.1021/jm00213a022 10.7270/Q26977R0 576620 Song, R; Qiao, W; He, J; Huang, J; Luo, Y; Yang, T 3/25/2021 4/18/2024 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 50029543 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 1.2 ChEMBL 10.1021/jm00213a022 10.7270/Q26977R0 576620 Song, R; Qiao, W; He, J; Huang, J; Luo, Y; Yang, T 3/25/2021 4/18/2024 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 50494739 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 37 ChEMBL 10.1016/j.bmcl.2016.04.067 10.7270/Q2N018GG 27158142 Yang, L; Wang, W; Sun, Q; Xu, F; Niu, Y; Wang, C; Liang, L; Xu, P 6/15/2016 8/25/2017 Peking University Health Science Center http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 50494751 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 44 ChEMBL 10.1016/j.bmcl.2016.04.067 10.7270/Q2N018GG 27158142 Yang, L; Wang, W; Sun, Q; Xu, F; Niu, Y; Wang, C; Liang, L; Xu, P 6/15/2016 8/25/2017 Peking University Health Science Center http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 50494763 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 52 ChEMBL 10.1016/j.bmcl.2016.04.067 10.7270/Q2N018GG 27158142 Yang, L; Wang, W; Sun, Q; Xu, F; Niu, Y; Wang, C; Liang, L; Xu, P 6/15/2016 8/25/2017 Peking University Health Science Center http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 50521882 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 1.4 ChEMBL 10.1016/j.ejmech.2016.05.049 10.7270/Q28C9Z6K 27318981 Di Giovanni, C; Ettari, R; Sarno, S; Rotondo, A; Bitto, A; Squadrito, F; Altavilla, D; Schirmeister, T; Novellino, E; Grasso, S; Zappalà, M; Lavecchia, A 10/4/2016 7/10/2018 University of Naples Federico Ii http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 50521890 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 22100 ChEMBL 10.1016/j.ejmech.2016.05.049 10.7270/Q28C9Z6K 27318981 Di Giovanni, C; Ettari, R; Sarno, S; Rotondo, A; Bitto, A; Squadrito, F; Altavilla, D; Schirmeister, T; Novellino, E; Grasso, S; Zappalà, M; Lavecchia, A 10/4/2016 7/10/2018 University of Naples Federico Ii http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 50521891 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 5520 ChEMBL 10.1016/j.ejmech.2016.05.049 10.7270/Q28C9Z6K 27318981 Di Giovanni, C; Ettari, R; Sarno, S; Rotondo, A; Bitto, A; Squadrito, F; Altavilla, D; Schirmeister, T; Novellino, E; Grasso, S; Zappalà, M; Lavecchia, A 10/4/2016 7/10/2018 University of Naples Federico Ii http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 50711335 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 25 ChEMBL 10.1016/j.ejmech.2016.11.024 10.7270/Q2Z03BDZ 27889629 Qin, JM; Huang, RZ; Yao, GY; Liao, ZX; Pan, YM; Wang, HS 1/27/2017 6/17/2019 Guangxi Normal University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51002658 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 470 ChEMBL 10.1021/jm058289o 10.7270/Q2FF3S0S 16686537 Rydzewski, RM; Burrill, L; Mendonca, R; Palmer, JT; Rice, M; Tahilramani, R; Bass, KE; Leung, L; Gjerstad, E; Janc, JW; Pan, L 5/11/2006 11/10/2009 Celera http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51002662 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 3.7 ChEMBL 10.1021/jm058289o 10.7270/Q2FF3S0S 16686537 Rydzewski, RM; Burrill, L; Mendonca, R; Palmer, JT; Rice, M; Tahilramani, R; Bass, KE; Leung, L; Gjerstad, E; Janc, JW; Pan, L 5/11/2006 11/10/2009 Celera http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51002664 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 330 ChEMBL 10.1021/jm058289o 10.7270/Q2FF3S0S 16686537 Rydzewski, RM; Burrill, L; Mendonca, R; Palmer, JT; Rice, M; Tahilramani, R; Bass, KE; Leung, L; Gjerstad, E; Janc, JW; Pan, L 5/11/2006 11/10/2009 Celera http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51087096 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 2100 ChEMBL 10.1016/j.ejmech.2013.11.009 10.7270/Q2222W81 24321833 Hasegawa, M; Yasuda, Y; Tanaka, M; Nakata, K; Umeda, E; Wang, Y; Watanabe, C; Uetake, S; Kunoh, T; Shionyu, M; Sasaki, R; Shiina, I; Mizukami, T 1/31/2014 7/25/2014 Institute of Bio-Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51087151 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 120 ChEMBL 10.1016/j.ejmech.2013.11.009 10.7270/Q2222W81 24321833 Hasegawa, M; Yasuda, Y; Tanaka, M; Nakata, K; Umeda, E; Wang, Y; Watanabe, C; Uetake, S; Kunoh, T; Shionyu, M; Sasaki, R; Shiina, I; Mizukami, T 1/31/2014 7/25/2014 Institute of Bio-Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51087152 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 11 ChEMBL 10.1016/j.ejmech.2013.11.009 10.7270/Q2222W81 24321833 Hasegawa, M; Yasuda, Y; Tanaka, M; Nakata, K; Umeda, E; Wang, Y; Watanabe, C; Uetake, S; Kunoh, T; Shionyu, M; Sasaki, R; Shiina, I; Mizukami, T 1/31/2014 7/25/2014 Institute of Bio-Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51110847 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 1.000000 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51110850 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 5520 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51110852 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 22100 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51110856 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 4.0 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51110862 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 130 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51110863 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 70 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51227585 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 1.2 ChEMBL 10.1016/j.bmc.2018.12.022 10.7270/Q2NP27P1 30581047 Pehere, AD; Nguyen, S; Garlick, SK; Wilson, DW; Hudson, I; Sykes, MJ; Morton, JD; Abell, AD 1/15/2019 2/18/2021 University of Adelaide http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51289132 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 1450 ChEMBL 10.1021/acsmedchemlett.9b00233 10.7270/Q2930XK7 31312413 Pacifico, S; Ferretti, V; Albanese, V; Fantinati, A; Gallerani, E; Nicoli, F; Gavioli, R; Zamberlan, F; Preti, D; Marastoni, M 7/11/2019 2/24/2021 University of Ferrara http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51289181 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 4590 ChEMBL 10.1021/acsmedchemlett.9b00233 10.7270/Q2930XK7 31312413 Pacifico, S; Ferretti, V; Albanese, V; Fantinati, A; Gallerani, E; Nicoli, F; Gavioli, R; Zamberlan, F; Preti, D; Marastoni, M 7/11/2019 2/24/2021 University of Ferrara http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51289196 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 7.0 ChEMBL 10.1021/acsmedchemlett.9b00233 10.7270/Q2930XK7 31312413 Pacifico, S; Ferretti, V; Albanese, V; Fantinati, A; Gallerani, E; Nicoli, F; Gavioli, R; Zamberlan, F; Preti, D; Marastoni, M 7/11/2019 2/24/2021 University of Ferrara http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51298902 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 30 ChEMBL 10.1016/j.bmc.2019.115161 10.7270/Q29W0JZJ 31732281 Uesugi, S; Honmura, Y; Nishiyama, M; Kusakabe, K; Tonouchi, A; Yamashita, T; Hashimoto, M; Kimura, KI 12/15/2019 2/25/2021 Iwate University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51298906 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 1600 ChEMBL 10.1016/j.bmc.2019.115161 10.7270/Q29W0JZJ 31732281 Uesugi, S; Honmura, Y; Nishiyama, M; Kusakabe, K; Tonouchi, A; Yamashita, T; Hashimoto, M; Kimura, KI 12/15/2019 2/25/2021 Iwate University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51298909 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 500 ChEMBL 10.1016/j.bmc.2019.115161 10.7270/Q29W0JZJ 31732281 Uesugi, S; Honmura, Y; Nishiyama, M; Kusakabe, K; Tonouchi, A; Yamashita, T; Hashimoto, M; Kimura, KI 12/15/2019 2/25/2021 Iwate University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51487773 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 22100 ChEMBL 10.7270/Q20R9TGT 34838650 Ettari, R; Iraci, N; Di Chio, C; Previti, S; Danzè, M; Zappalà, M 1/1/2022 6/23/2023 University of Messina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51487774 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 5520 ChEMBL 10.7270/Q20R9TGT 34838650 Ettari, R; Iraci, N; Di Chio, C; Previti, S; Danzè, M; Zappalà, M 1/1/2022 6/23/2023 University of Messina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51487775 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 1.4 ChEMBL 10.7270/Q20R9TGT 34838650 Ettari, R; Iraci, N; Di Chio, C; Previti, S; Danzè, M; Zappalà, M 1/1/2022 6/23/2023 University of Messina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51487776 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 130 ChEMBL 10.7270/Q20R9TGT 34838650 Ettari, R; Iraci, N; Di Chio, C; Previti, S; Danzè, M; Zappalà, M 1/1/2022 6/23/2023 University of Messina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51487777 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 1.000000 ChEMBL 10.7270/Q20R9TGT 34838650 Ettari, R; Iraci, N; Di Chio, C; Previti, S; Danzè, M; Zappalà, M 1/1/2022 6/23/2023 University of Messina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51159619 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 A5LHX3/O14818/P20618/P25786/P25787/P25788/P25789/P28062/P28065/P28066/P28070/P28072/P28074/P40306/P49720/P49721/P60900/Q8TAA3/Q99436 Homo sapiens 4500 ChEMBL 10.1016/j.bmcl.2005.02.013 10.7270/Q2CF9SVN 15780623 Momose, I; Umezawa, Y; Hirosawa, S; Iinuma, H; Ikeda, D 4/1/2005 8/23/2020 Numazu Bio-Medical Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000077&target=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 19 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 MALLDVCGAPRGQRPESALPVAGSGRRSDPGHYSFSMRSPELALPRGMQPTEFFQSLGGDGERNVQIEMAHGTTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAIAYATHRDSYSGGVVNMYHMKEDGWVKVESTDVSDLLHQYREANQ 6E5B,6AVO,7B12,7AWE Proteasome subunit beta type-8 PSB8_HUMAN P28062 B0UZC0 Q29824 Q5JNW6 Q5QNR8 Q96J48 MLRAGAPTGDLPRAGEVHTGTTIMAVEFDGGVVMGSDSRVSAGEAVVNRVFDKLSPLHERIYCALSGSAADAQAVADMAAYQLELHGIELEEPPLVLAAANVVRNISYKYREDLSAHLMVAGWDQREGGQVYGTLGGMLTRQPFAIGGSGSTFIYGYVDAAYKPGMSPEECRRFTTDAIALAMSRDGSSGGVIYLVTITAAGVDHRVILGNELPKFYDE 6E5B,7B12,7AWE,6AVO,8YVG,8YSX Proteasome subunit beta type-9 PSB9_HUMAN P28065 B0V0T1 Q16523 Q5JNW4 MAATLLAARGAGPAPAWGPEAFTPDWESREVSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDRIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAASLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTANALALAMERDGSSGGVIRLAAIAESGVERQVLLGDQIPKFAVATLPPA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,9RKZ,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6R70,9QVX,6XMJ,4R67,4R3O,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit beta type-6 PSB6_HUMAN P28072 Q96J55 MFRNQYDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSELAAHQKKILHVDNHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGARSQSARTYLERHMSEFMECNLNELVKHGLRALRETLPAEQDLTTKNVSIGIVGKDLEFTIYDDDDVSPFLEGLEERPQRKAQPAQPADEPAEKADEPMEH 9YUZ,9UG9,9UF8,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9VUG,9VUF,9VUE,9U7R,9U3L,9SZV,9SZT,9MBQ,9MBP,9HEU,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,7DRW,7DR7,7DR6,8YVG,8YSX,8QYS,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,5M32,9QVX Proteasome subunit alpha type-1 PSA1_HUMAN P25786 A8K400 Q53YE8 Q9BRV9 MAERGYSFSLTTFSPSGKLVQIEYALAAVAGGAPSVGIKAANGVVLATEKKQKSILYDERSVHKVEPITKHIGLVYSGMGPDYRVLVHRARKLAQQYYLVYQEPIPTAQLVQRVASVMQEYTQSGGVRPFGVSLLICGWNEGRPYLFQSDPSGAYFAWKATAMGKNYVNGKTFLEKRYNEDLELEDAIHTAILTLKESFEGQMTEDNIEVGICNEAGFRRLTPTEVKDYLAAIA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YVG,8YSX,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYS,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,9U7R,9U3L,9MBQ,9MBP,9HMN,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6XMJ,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,4R67,4R3O,22MM,1IRU,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,6R70,9QVX,7B12,7AWE Proteasome subunit alpha type-2 PSA2_HUMAN P25787 Q6ICS6 Q9BU45 MSSIGTGYDLSASTFSPDGRVFQVEYAMKAVENSSTAIGIRCKDGVVFGVEKLVLSKLYEEGSNKRLFNVDRHVGMAVAGLLADARSLADIAREEASNFRSNFGYNIPLKHLADRVAMYVHAYTLYSAVRPFGCSFMLGSYSVNDGAQLYMIDPSGVSYGYWGCAIGKARQAAKTEIEKLQMKEMTCRDIVKEVAKIIYIVHDEVKDKAFELELSWVGELTNGRHEIVPKDIREEAEKYAKESLKEEDESDDDNM 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7E55,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5DSV,5A0Q,9U7R,9U3L,9MBQ,9MBP,9HMN,8FZ6,8FZ5,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7DRW,7DR7,7DR6,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,1IRU,6TU3,6EPF,6EPE,6EPD,6EPC,8YVP,8YPK,3UNH,3UNF,3UNE,3UNB,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,8QYS,6R70,9QVX Proteasome subunit alpha type-3 PSA3_HUMAN P25788 B2RCK6 Q86U83 Q8N1D8 Q9BS70 MSRRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGEMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTRENGKTVIRVLKQKEVEQLIKKHEEEEAKAEREKKEKEQKEKDK 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,7AWE,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,6R70,8QYS,9QVX Proteasome subunit alpha type-4 PSA4_HUMAN P25789 D3DW86 Q53XP2 Q567Q5 Q8TBD1 MFLTRSEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKTLIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGEEDADPGAMSRPFGVALLFGGVDEKGPQLFHMDPSGTFVQCDARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKLNATNIELATVQPGQNFHMFTKEELEEVIKDI 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDI,9NKJ,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8O,9E8N,9E8L,9E8K,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YVP,8YVG,8YSX,8YPK,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QYO,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,22MM,8QZ9,8QYN,8QYM,8QYL,8QYJ,8QYS,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9QVX,6R70,7B12,7AWE Proteasome subunit alpha type-5 PSA5_HUMAN P28066 B2R8F6 B4E2V4 Q3T1C1 Q6IBF7 MSRGSSAGFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITENIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATAAGVKQTESTSFLEKKVKKKFDWTFEQTVETAITCLSTVLSIDFKPSEIEVGVVTVENPKFRILTEAEIDAHLVALAERD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6TU3,6RGQ,6REY,6KWY,6EPF,6EPE,6EPD,6EPC,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,6XMJ,6R70,4R67,4R3O,7B12,7AWE,9QVX,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit alpha type-6 PSA6_HUMAN P60900 B2R7J9 B4DQR4 B4DXJ9 P34062 Q6IB60 MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIGRGAKSVREFLEKNYTDEAIETDDLTIKLVIKALLEVVQSGGKNIELAVMRRDQSLKILNPEEIEKYVAEIEKEKEENEKKKQKKAS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,22MM,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7AWE,6R70,7B12,8QYS,9QVX Proteasome subunit alpha type-7 PSA7_HUMAN O14818 B2R515 Q5JXJ2 Q9BR53 Q9H4K5 Q9UEU8 MASRYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVCMAFAVLTIFIGLTADARVVINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDAIASDSEAIKLAIKALLEVVQSGGKNIELAIIRRNQPLKMFSAKEVELYVTEIEKEKEEAEKKKSKKSV Proteasome subunit alpha-type 8 PSMA8_HUMAN Q8TAA3 B0YJ75 Q8IVP4 Q8TA98 Q8TAA2 MLKPALEPRGGFSFENCQRNASLERVLPGLKVPHARKTGTTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATVTRILRQTLFRYQGHVGASLIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLLVEAVTAGILGDLGSGGNVDACVITKTGAKLLRTLSSPTEPVKRSGRYHFVPGTTAVLTQTVKPLTLELVEETVQAMEVE 6E5B,6AVO,7AWE Proteasome subunit beta type-10 PSB10_HUMAN P40306 B2R5J4 Q5U098 MALQDVCKWQSPDTQGPSPHLPRAGGWAVPRGCDPQTFLQIHGPRLAHGTTTLAFRFRHGVIAAADTRSSCGSYVACPASCKVIPVHQHLLGTTSGTSADCATWYRVLQRELRLRELREGQLPSVASAAKLLSAMMSQYRGLDLCVATALCGWDRSGPELFYVYSDGTRLQGDIFSVGSGSPYAYGVLDRGYRYDMSTQEAYALARCAVAHATHRDAYSGGSVDLFHVRESGWEHVSRSDACVLYVELQKLLEPEPEEDASHAHPEPATAHRAAEDRELSVGPGEVTPGDSRMPAGTETV Proteasome subunit beta type-11 PSB11_HUMAN A5LHX3 MSIMSYNGGAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYTLMSMVANLLYEKRFGPYYTEPVIAGLDPKTFKPFICSLDLIGCPMVTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLFETISQAMLNAVDRDAVSGMGVIVHIIEKDKITTRTLKARMD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QZ9,8QYO,8QYN,8QYM,8QYL,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,9U7R,9U3L,9RKZ,9QVX,9MBQ,9MBP,9HMN,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7B12,7AWE,6XMJ,6WJN,6WJD,6R70,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5T0J,5T0I,5T0H,5T0G,5T0C,5A0Q,4R67,4R3O,22MM,8YVP,8YPK,6TU3,3UNH,3UNF,3UNE,3UNB,8QYS Proteasome subunit beta type-3 PSB3_HUMAN P49720 P31147 Q0P6J7 Q96E27 MEAFLGSRSGLWAGGPAPGQFYRIPSTPDSFMDPASALYRGPITRTQNPMVTGTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNNSTMLGASGDYADFQYLKQVLGQMVIDEELLGDGHSYSPRAIHSWLTRAMYSRRSKMNPLWNTMVIGGYADGESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREVLEKQPVLSQTEARDLVERCMRVLYYRDARSYNRFQIATVTEKGVEIEGPLSTETNWDIAHMISGFE 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9BW4,9BV3,9BV2,9BV1,9BUI,8TM6,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YIZ,8YIY,8YIX,9RKZ,9HMN,8UD9,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,6AVO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,6XMJ,4R67,4R3O,6R70,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,7B12,7AWE,9QVX Proteasome subunit beta type-4 PSB4_HUMAN P28070 B2R9L3 P31148 Q5SZS5 Q6IBI4 Q969L6 MAAVSVYAPPVGGFSFDNCRRNAVLEADFAKRGYKLPKVRKTGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTANRMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAIAAGIFNDLGSGSNIDLCVISKNKLDFLRPYTVPNKKGTRLGRYRCEKGTTAVLTEKITPLEIEVLEETVQTMDTS 8QZ9,8QYN,8QYM,8QYL,8QYJ,9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8TM6,8TM5,8TM4,8QYO,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,9RKZ,9HMN,8UD9,8CVS,8CVR,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,9QVX,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O Proteasome subunit beta type-7 PSB7_HUMAN Q99436 B4E0P1 Q5TBG6 Q96AG8 Q9BWA7 51159624 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 A5LHX3/O14818/P20618/P25786/P25787/P25788/P25789/P28062/P28065/P28066/P28070/P28072/P28074/P40306/P49720/P49721/P60900/Q8TAA3/Q99436 Homo sapiens 1400 ChEMBL 10.1016/j.bmcl.2005.02.013 10.7270/Q2CF9SVN 15780623 Momose, I; Umezawa, Y; Hirosawa, S; Iinuma, H; Ikeda, D 4/1/2005 8/23/2020 Numazu Bio-Medical Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000077&target=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 19 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 MALLDVCGAPRGQRPESALPVAGSGRRSDPGHYSFSMRSPELALPRGMQPTEFFQSLGGDGERNVQIEMAHGTTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAIAYATHRDSYSGGVVNMYHMKEDGWVKVESTDVSDLLHQYREANQ 6E5B,6AVO,7B12,7AWE Proteasome subunit beta type-8 PSB8_HUMAN P28062 B0UZC0 Q29824 Q5JNW6 Q5QNR8 Q96J48 MLRAGAPTGDLPRAGEVHTGTTIMAVEFDGGVVMGSDSRVSAGEAVVNRVFDKLSPLHERIYCALSGSAADAQAVADMAAYQLELHGIELEEPPLVLAAANVVRNISYKYREDLSAHLMVAGWDQREGGQVYGTLGGMLTRQPFAIGGSGSTFIYGYVDAAYKPGMSPEECRRFTTDAIALAMSRDGSSGGVIYLVTITAAGVDHRVILGNELPKFYDE 6E5B,7B12,7AWE,6AVO,8YVG,8YSX Proteasome subunit beta type-9 PSB9_HUMAN P28065 B0V0T1 Q16523 Q5JNW4 MAATLLAARGAGPAPAWGPEAFTPDWESREVSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDRIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAASLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTANALALAMERDGSSGGVIRLAAIAESGVERQVLLGDQIPKFAVATLPPA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,9RKZ,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6R70,9QVX,6XMJ,4R67,4R3O,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit beta type-6 PSB6_HUMAN P28072 Q96J55 MFRNQYDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSELAAHQKKILHVDNHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGARSQSARTYLERHMSEFMECNLNELVKHGLRALRETLPAEQDLTTKNVSIGIVGKDLEFTIYDDDDVSPFLEGLEERPQRKAQPAQPADEPAEKADEPMEH 9YUZ,9UG9,9UF8,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9VUG,9VUF,9VUE,9U7R,9U3L,9SZV,9SZT,9MBQ,9MBP,9HEU,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,7DRW,7DR7,7DR6,8YVG,8YSX,8QYS,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,5M32,9QVX Proteasome subunit alpha type-1 PSA1_HUMAN P25786 A8K400 Q53YE8 Q9BRV9 MAERGYSFSLTTFSPSGKLVQIEYALAAVAGGAPSVGIKAANGVVLATEKKQKSILYDERSVHKVEPITKHIGLVYSGMGPDYRVLVHRARKLAQQYYLVYQEPIPTAQLVQRVASVMQEYTQSGGVRPFGVSLLICGWNEGRPYLFQSDPSGAYFAWKATAMGKNYVNGKTFLEKRYNEDLELEDAIHTAILTLKESFEGQMTEDNIEVGICNEAGFRRLTPTEVKDYLAAIA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YVG,8YSX,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYS,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,9U7R,9U3L,9MBQ,9MBP,9HMN,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6XMJ,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,4R67,4R3O,22MM,1IRU,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,6R70,9QVX,7B12,7AWE Proteasome subunit alpha type-2 PSA2_HUMAN P25787 Q6ICS6 Q9BU45 MSSIGTGYDLSASTFSPDGRVFQVEYAMKAVENSSTAIGIRCKDGVVFGVEKLVLSKLYEEGSNKRLFNVDRHVGMAVAGLLADARSLADIAREEASNFRSNFGYNIPLKHLADRVAMYVHAYTLYSAVRPFGCSFMLGSYSVNDGAQLYMIDPSGVSYGYWGCAIGKARQAAKTEIEKLQMKEMTCRDIVKEVAKIIYIVHDEVKDKAFELELSWVGELTNGRHEIVPKDIREEAEKYAKESLKEEDESDDDNM 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7E55,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5DSV,5A0Q,9U7R,9U3L,9MBQ,9MBP,9HMN,8FZ6,8FZ5,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7DRW,7DR7,7DR6,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,1IRU,6TU3,6EPF,6EPE,6EPD,6EPC,8YVP,8YPK,3UNH,3UNF,3UNE,3UNB,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,8QYS,6R70,9QVX Proteasome subunit alpha type-3 PSA3_HUMAN P25788 B2RCK6 Q86U83 Q8N1D8 Q9BS70 MSRRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGEMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTRENGKTVIRVLKQKEVEQLIKKHEEEEAKAEREKKEKEQKEKDK 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,7AWE,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,6R70,8QYS,9QVX Proteasome subunit alpha type-4 PSA4_HUMAN P25789 D3DW86 Q53XP2 Q567Q5 Q8TBD1 MFLTRSEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKTLIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGEEDADPGAMSRPFGVALLFGGVDEKGPQLFHMDPSGTFVQCDARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKLNATNIELATVQPGQNFHMFTKEELEEVIKDI 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDI,9NKJ,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8O,9E8N,9E8L,9E8K,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YVP,8YVG,8YSX,8YPK,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QYO,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,22MM,8QZ9,8QYN,8QYM,8QYL,8QYJ,8QYS,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9QVX,6R70,7B12,7AWE Proteasome subunit alpha type-5 PSA5_HUMAN P28066 B2R8F6 B4E2V4 Q3T1C1 Q6IBF7 MSRGSSAGFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITENIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATAAGVKQTESTSFLEKKVKKKFDWTFEQTVETAITCLSTVLSIDFKPSEIEVGVVTVENPKFRILTEAEIDAHLVALAERD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6TU3,6RGQ,6REY,6KWY,6EPF,6EPE,6EPD,6EPC,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,6XMJ,6R70,4R67,4R3O,7B12,7AWE,9QVX,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit alpha type-6 PSA6_HUMAN P60900 B2R7J9 B4DQR4 B4DXJ9 P34062 Q6IB60 MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIGRGAKSVREFLEKNYTDEAIETDDLTIKLVIKALLEVVQSGGKNIELAVMRRDQSLKILNPEEIEKYVAEIEKEKEENEKKKQKKAS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,22MM,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7AWE,6R70,7B12,8QYS,9QVX Proteasome subunit alpha type-7 PSA7_HUMAN O14818 B2R515 Q5JXJ2 Q9BR53 Q9H4K5 Q9UEU8 MASRYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVCMAFAVLTIFIGLTADARVVINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDAIASDSEAIKLAIKALLEVVQSGGKNIELAIIRRNQPLKMFSAKEVELYVTEIEKEKEEAEKKKSKKSV Proteasome subunit alpha-type 8 PSMA8_HUMAN Q8TAA3 B0YJ75 Q8IVP4 Q8TA98 Q8TAA2 MLKPALEPRGGFSFENCQRNASLERVLPGLKVPHARKTGTTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATVTRILRQTLFRYQGHVGASLIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLLVEAVTAGILGDLGSGGNVDACVITKTGAKLLRTLSSPTEPVKRSGRYHFVPGTTAVLTQTVKPLTLELVEETVQAMEVE 6E5B,6AVO,7AWE Proteasome subunit beta type-10 PSB10_HUMAN P40306 B2R5J4 Q5U098 MALQDVCKWQSPDTQGPSPHLPRAGGWAVPRGCDPQTFLQIHGPRLAHGTTTLAFRFRHGVIAAADTRSSCGSYVACPASCKVIPVHQHLLGTTSGTSADCATWYRVLQRELRLRELREGQLPSVASAAKLLSAMMSQYRGLDLCVATALCGWDRSGPELFYVYSDGTRLQGDIFSVGSGSPYAYGVLDRGYRYDMSTQEAYALARCAVAHATHRDAYSGGSVDLFHVRESGWEHVSRSDACVLYVELQKLLEPEPEEDASHAHPEPATAHRAAEDRELSVGPGEVTPGDSRMPAGTETV Proteasome subunit beta type-11 PSB11_HUMAN A5LHX3 MSIMSYNGGAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYTLMSMVANLLYEKRFGPYYTEPVIAGLDPKTFKPFICSLDLIGCPMVTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLFETISQAMLNAVDRDAVSGMGVIVHIIEKDKITTRTLKARMD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QZ9,8QYO,8QYN,8QYM,8QYL,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,9U7R,9U3L,9RKZ,9QVX,9MBQ,9MBP,9HMN,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7B12,7AWE,6XMJ,6WJN,6WJD,6R70,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5T0J,5T0I,5T0H,5T0G,5T0C,5A0Q,4R67,4R3O,22MM,8YVP,8YPK,6TU3,3UNH,3UNF,3UNE,3UNB,8QYS Proteasome subunit beta type-3 PSB3_HUMAN P49720 P31147 Q0P6J7 Q96E27 MEAFLGSRSGLWAGGPAPGQFYRIPSTPDSFMDPASALYRGPITRTQNPMVTGTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNNSTMLGASGDYADFQYLKQVLGQMVIDEELLGDGHSYSPRAIHSWLTRAMYSRRSKMNPLWNTMVIGGYADGESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREVLEKQPVLSQTEARDLVERCMRVLYYRDARSYNRFQIATVTEKGVEIEGPLSTETNWDIAHMISGFE 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9BW4,9BV3,9BV2,9BV1,9BUI,8TM6,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YIZ,8YIY,8YIX,9RKZ,9HMN,8UD9,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,6AVO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,6XMJ,4R67,4R3O,6R70,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,7B12,7AWE,9QVX Proteasome subunit beta type-4 PSB4_HUMAN P28070 B2R9L3 P31148 Q5SZS5 Q6IBI4 Q969L6 MAAVSVYAPPVGGFSFDNCRRNAVLEADFAKRGYKLPKVRKTGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTANRMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAIAAGIFNDLGSGSNIDLCVISKNKLDFLRPYTVPNKKGTRLGRYRCEKGTTAVLTEKITPLEIEVLEETVQTMDTS 8QZ9,8QYN,8QYM,8QYL,8QYJ,9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8TM6,8TM5,8TM4,8QYO,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,9RKZ,9HMN,8UD9,8CVS,8CVR,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,9QVX,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O Proteasome subunit beta type-7 PSB7_HUMAN Q99436 B4E0P1 Q5TBG6 Q96AG8 Q9BWA7 51159634 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 A5LHX3/O14818/P20618/P25786/P25787/P25788/P25789/P28062/P28065/P28066/P28070/P28072/P28074/P40306/P49720/P49721/P60900/Q8TAA3/Q99436 Homo sapiens 68 ChEMBL 10.1016/j.bmcl.2005.02.013 10.7270/Q2CF9SVN 15780623 Momose, I; Umezawa, Y; Hirosawa, S; Iinuma, H; Ikeda, D 4/1/2005 8/23/2020 Numazu Bio-Medical Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000077&target=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 19 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 MALLDVCGAPRGQRPESALPVAGSGRRSDPGHYSFSMRSPELALPRGMQPTEFFQSLGGDGERNVQIEMAHGTTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAIAYATHRDSYSGGVVNMYHMKEDGWVKVESTDVSDLLHQYREANQ 6E5B,6AVO,7B12,7AWE Proteasome subunit beta type-8 PSB8_HUMAN P28062 B0UZC0 Q29824 Q5JNW6 Q5QNR8 Q96J48 MLRAGAPTGDLPRAGEVHTGTTIMAVEFDGGVVMGSDSRVSAGEAVVNRVFDKLSPLHERIYCALSGSAADAQAVADMAAYQLELHGIELEEPPLVLAAANVVRNISYKYREDLSAHLMVAGWDQREGGQVYGTLGGMLTRQPFAIGGSGSTFIYGYVDAAYKPGMSPEECRRFTTDAIALAMSRDGSSGGVIYLVTITAAGVDHRVILGNELPKFYDE 6E5B,7B12,7AWE,6AVO,8YVG,8YSX Proteasome subunit beta type-9 PSB9_HUMAN P28065 B0V0T1 Q16523 Q5JNW4 MAATLLAARGAGPAPAWGPEAFTPDWESREVSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDRIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAASLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTANALALAMERDGSSGGVIRLAAIAESGVERQVLLGDQIPKFAVATLPPA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,9RKZ,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6R70,9QVX,6XMJ,4R67,4R3O,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit beta type-6 PSB6_HUMAN P28072 Q96J55 MFRNQYDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSELAAHQKKILHVDNHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGARSQSARTYLERHMSEFMECNLNELVKHGLRALRETLPAEQDLTTKNVSIGIVGKDLEFTIYDDDDVSPFLEGLEERPQRKAQPAQPADEPAEKADEPMEH 9YUZ,9UG9,9UF8,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9VUG,9VUF,9VUE,9U7R,9U3L,9SZV,9SZT,9MBQ,9MBP,9HEU,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,7DRW,7DR7,7DR6,8YVG,8YSX,8QYS,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,5M32,9QVX Proteasome subunit alpha type-1 PSA1_HUMAN P25786 A8K400 Q53YE8 Q9BRV9 MAERGYSFSLTTFSPSGKLVQIEYALAAVAGGAPSVGIKAANGVVLATEKKQKSILYDERSVHKVEPITKHIGLVYSGMGPDYRVLVHRARKLAQQYYLVYQEPIPTAQLVQRVASVMQEYTQSGGVRPFGVSLLICGWNEGRPYLFQSDPSGAYFAWKATAMGKNYVNGKTFLEKRYNEDLELEDAIHTAILTLKESFEGQMTEDNIEVGICNEAGFRRLTPTEVKDYLAAIA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YVG,8YSX,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYS,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,9U7R,9U3L,9MBQ,9MBP,9HMN,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6XMJ,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,4R67,4R3O,22MM,1IRU,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,6R70,9QVX,7B12,7AWE Proteasome subunit alpha type-2 PSA2_HUMAN P25787 Q6ICS6 Q9BU45 MSSIGTGYDLSASTFSPDGRVFQVEYAMKAVENSSTAIGIRCKDGVVFGVEKLVLSKLYEEGSNKRLFNVDRHVGMAVAGLLADARSLADIAREEASNFRSNFGYNIPLKHLADRVAMYVHAYTLYSAVRPFGCSFMLGSYSVNDGAQLYMIDPSGVSYGYWGCAIGKARQAAKTEIEKLQMKEMTCRDIVKEVAKIIYIVHDEVKDKAFELELSWVGELTNGRHEIVPKDIREEAEKYAKESLKEEDESDDDNM 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7E55,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5DSV,5A0Q,9U7R,9U3L,9MBQ,9MBP,9HMN,8FZ6,8FZ5,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7DRW,7DR7,7DR6,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,1IRU,6TU3,6EPF,6EPE,6EPD,6EPC,8YVP,8YPK,3UNH,3UNF,3UNE,3UNB,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,8QYS,6R70,9QVX Proteasome subunit alpha type-3 PSA3_HUMAN P25788 B2RCK6 Q86U83 Q8N1D8 Q9BS70 MSRRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGEMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTRENGKTVIRVLKQKEVEQLIKKHEEEEAKAEREKKEKEQKEKDK 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,7AWE,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,6R70,8QYS,9QVX Proteasome subunit alpha type-4 PSA4_HUMAN P25789 D3DW86 Q53XP2 Q567Q5 Q8TBD1 MFLTRSEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKTLIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGEEDADPGAMSRPFGVALLFGGVDEKGPQLFHMDPSGTFVQCDARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKLNATNIELATVQPGQNFHMFTKEELEEVIKDI 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDI,9NKJ,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8O,9E8N,9E8L,9E8K,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YVP,8YVG,8YSX,8YPK,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QYO,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,22MM,8QZ9,8QYN,8QYM,8QYL,8QYJ,8QYS,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9QVX,6R70,7B12,7AWE Proteasome subunit alpha type-5 PSA5_HUMAN P28066 B2R8F6 B4E2V4 Q3T1C1 Q6IBF7 MSRGSSAGFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITENIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATAAGVKQTESTSFLEKKVKKKFDWTFEQTVETAITCLSTVLSIDFKPSEIEVGVVTVENPKFRILTEAEIDAHLVALAERD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6TU3,6RGQ,6REY,6KWY,6EPF,6EPE,6EPD,6EPC,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,6XMJ,6R70,4R67,4R3O,7B12,7AWE,9QVX,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit alpha type-6 PSA6_HUMAN P60900 B2R7J9 B4DQR4 B4DXJ9 P34062 Q6IB60 MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIGRGAKSVREFLEKNYTDEAIETDDLTIKLVIKALLEVVQSGGKNIELAVMRRDQSLKILNPEEIEKYVAEIEKEKEENEKKKQKKAS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,22MM,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7AWE,6R70,7B12,8QYS,9QVX Proteasome subunit alpha type-7 PSA7_HUMAN O14818 B2R515 Q5JXJ2 Q9BR53 Q9H4K5 Q9UEU8 MASRYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVCMAFAVLTIFIGLTADARVVINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDAIASDSEAIKLAIKALLEVVQSGGKNIELAIIRRNQPLKMFSAKEVELYVTEIEKEKEEAEKKKSKKSV Proteasome subunit alpha-type 8 PSMA8_HUMAN Q8TAA3 B0YJ75 Q8IVP4 Q8TA98 Q8TAA2 MLKPALEPRGGFSFENCQRNASLERVLPGLKVPHARKTGTTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATVTRILRQTLFRYQGHVGASLIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLLVEAVTAGILGDLGSGGNVDACVITKTGAKLLRTLSSPTEPVKRSGRYHFVPGTTAVLTQTVKPLTLELVEETVQAMEVE 6E5B,6AVO,7AWE Proteasome subunit beta type-10 PSB10_HUMAN P40306 B2R5J4 Q5U098 MALQDVCKWQSPDTQGPSPHLPRAGGWAVPRGCDPQTFLQIHGPRLAHGTTTLAFRFRHGVIAAADTRSSCGSYVACPASCKVIPVHQHLLGTTSGTSADCATWYRVLQRELRLRELREGQLPSVASAAKLLSAMMSQYRGLDLCVATALCGWDRSGPELFYVYSDGTRLQGDIFSVGSGSPYAYGVLDRGYRYDMSTQEAYALARCAVAHATHRDAYSGGSVDLFHVRESGWEHVSRSDACVLYVELQKLLEPEPEEDASHAHPEPATAHRAAEDRELSVGPGEVTPGDSRMPAGTETV Proteasome subunit beta type-11 PSB11_HUMAN A5LHX3 MSIMSYNGGAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYTLMSMVANLLYEKRFGPYYTEPVIAGLDPKTFKPFICSLDLIGCPMVTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLFETISQAMLNAVDRDAVSGMGVIVHIIEKDKITTRTLKARMD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QZ9,8QYO,8QYN,8QYM,8QYL,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,9U7R,9U3L,9RKZ,9QVX,9MBQ,9MBP,9HMN,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7B12,7AWE,6XMJ,6WJN,6WJD,6R70,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5T0J,5T0I,5T0H,5T0G,5T0C,5A0Q,4R67,4R3O,22MM,8YVP,8YPK,6TU3,3UNH,3UNF,3UNE,3UNB,8QYS Proteasome subunit beta type-3 PSB3_HUMAN P49720 P31147 Q0P6J7 Q96E27 MEAFLGSRSGLWAGGPAPGQFYRIPSTPDSFMDPASALYRGPITRTQNPMVTGTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNNSTMLGASGDYADFQYLKQVLGQMVIDEELLGDGHSYSPRAIHSWLTRAMYSRRSKMNPLWNTMVIGGYADGESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREVLEKQPVLSQTEARDLVERCMRVLYYRDARSYNRFQIATVTEKGVEIEGPLSTETNWDIAHMISGFE 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9BW4,9BV3,9BV2,9BV1,9BUI,8TM6,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YIZ,8YIY,8YIX,9RKZ,9HMN,8UD9,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,6AVO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,6XMJ,4R67,4R3O,6R70,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,7B12,7AWE,9QVX Proteasome subunit beta type-4 PSB4_HUMAN P28070 B2R9L3 P31148 Q5SZS5 Q6IBI4 Q969L6 MAAVSVYAPPVGGFSFDNCRRNAVLEADFAKRGYKLPKVRKTGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTANRMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAIAAGIFNDLGSGSNIDLCVISKNKLDFLRPYTVPNKKGTRLGRYRCEKGTTAVLTEKITPLEIEVLEETVQTMDTS 8QZ9,8QYN,8QYM,8QYL,8QYJ,9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8TM6,8TM5,8TM4,8QYO,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,9RKZ,9HMN,8UD9,8CVS,8CVR,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,9QVX,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O Proteasome subunit beta type-7 PSB7_HUMAN Q99436 B4E0P1 Q5TBG6 Q96AG8 Q9BWA7 50028847 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 120 ChEMBL 10.1021/jm00213a022 10.7270/Q26977R0 576620 Song, R; Qiao, W; He, J; Huang, J; Luo, Y; Yang, T 3/25/2021 4/18/2024 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 50029539 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 1080 ChEMBL 10.1021/jm00213a022 10.7270/Q26977R0 576620 Song, R; Qiao, W; He, J; Huang, J; Luo, Y; Yang, T 3/25/2021 4/18/2024 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 50029543 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 1.2 ChEMBL 10.1021/jm00213a022 10.7270/Q26977R0 576620 Song, R; Qiao, W; He, J; Huang, J; Luo, Y; Yang, T 3/25/2021 4/18/2024 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 50494739 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 37 ChEMBL 10.1016/j.bmcl.2016.04.067 10.7270/Q2N018GG 27158142 Yang, L; Wang, W; Sun, Q; Xu, F; Niu, Y; Wang, C; Liang, L; Xu, P 6/15/2016 8/25/2017 Peking University Health Science Center http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 50494751 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 44 ChEMBL 10.1016/j.bmcl.2016.04.067 10.7270/Q2N018GG 27158142 Yang, L; Wang, W; Sun, Q; Xu, F; Niu, Y; Wang, C; Liang, L; Xu, P 6/15/2016 8/25/2017 Peking University Health Science Center http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 50494763 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 52 ChEMBL 10.1016/j.bmcl.2016.04.067 10.7270/Q2N018GG 27158142 Yang, L; Wang, W; Sun, Q; Xu, F; Niu, Y; Wang, C; Liang, L; Xu, P 6/15/2016 8/25/2017 Peking University Health Science Center http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 50521882 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 1.4 ChEMBL 10.1016/j.ejmech.2016.05.049 10.7270/Q28C9Z6K 27318981 Di Giovanni, C; Ettari, R; Sarno, S; Rotondo, A; Bitto, A; Squadrito, F; Altavilla, D; Schirmeister, T; Novellino, E; Grasso, S; Zappalà, M; Lavecchia, A 10/4/2016 7/10/2018 University of Naples Federico Ii http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 50521890 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 22100 ChEMBL 10.1016/j.ejmech.2016.05.049 10.7270/Q28C9Z6K 27318981 Di Giovanni, C; Ettari, R; Sarno, S; Rotondo, A; Bitto, A; Squadrito, F; Altavilla, D; Schirmeister, T; Novellino, E; Grasso, S; Zappalà, M; Lavecchia, A 10/4/2016 7/10/2018 University of Naples Federico Ii http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 50521891 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 5520 ChEMBL 10.1016/j.ejmech.2016.05.049 10.7270/Q28C9Z6K 27318981 Di Giovanni, C; Ettari, R; Sarno, S; Rotondo, A; Bitto, A; Squadrito, F; Altavilla, D; Schirmeister, T; Novellino, E; Grasso, S; Zappalà, M; Lavecchia, A 10/4/2016 7/10/2018 University of Naples Federico Ii http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 50711335 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 25 ChEMBL 10.1016/j.ejmech.2016.11.024 10.7270/Q2Z03BDZ 27889629 Qin, JM; Huang, RZ; Yao, GY; Liao, ZX; Pan, YM; Wang, HS 1/27/2017 6/17/2019 Guangxi Normal University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51002658 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 470 ChEMBL 10.1021/jm058289o 10.7270/Q2FF3S0S 16686537 Rydzewski, RM; Burrill, L; Mendonca, R; Palmer, JT; Rice, M; Tahilramani, R; Bass, KE; Leung, L; Gjerstad, E; Janc, JW; Pan, L 5/11/2006 11/10/2009 Celera http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51002662 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 3.7 ChEMBL 10.1021/jm058289o 10.7270/Q2FF3S0S 16686537 Rydzewski, RM; Burrill, L; Mendonca, R; Palmer, JT; Rice, M; Tahilramani, R; Bass, KE; Leung, L; Gjerstad, E; Janc, JW; Pan, L 5/11/2006 11/10/2009 Celera http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51002664 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 330 ChEMBL 10.1021/jm058289o 10.7270/Q2FF3S0S 16686537 Rydzewski, RM; Burrill, L; Mendonca, R; Palmer, JT; Rice, M; Tahilramani, R; Bass, KE; Leung, L; Gjerstad, E; Janc, JW; Pan, L 5/11/2006 11/10/2009 Celera http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51087096 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 2100 ChEMBL 10.1016/j.ejmech.2013.11.009 10.7270/Q2222W81 24321833 Hasegawa, M; Yasuda, Y; Tanaka, M; Nakata, K; Umeda, E; Wang, Y; Watanabe, C; Uetake, S; Kunoh, T; Shionyu, M; Sasaki, R; Shiina, I; Mizukami, T 1/31/2014 7/25/2014 Institute of Bio-Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51087151 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 120 ChEMBL 10.1016/j.ejmech.2013.11.009 10.7270/Q2222W81 24321833 Hasegawa, M; Yasuda, Y; Tanaka, M; Nakata, K; Umeda, E; Wang, Y; Watanabe, C; Uetake, S; Kunoh, T; Shionyu, M; Sasaki, R; Shiina, I; Mizukami, T 1/31/2014 7/25/2014 Institute of Bio-Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51087152 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 11 ChEMBL 10.1016/j.ejmech.2013.11.009 10.7270/Q2222W81 24321833 Hasegawa, M; Yasuda, Y; Tanaka, M; Nakata, K; Umeda, E; Wang, Y; Watanabe, C; Uetake, S; Kunoh, T; Shionyu, M; Sasaki, R; Shiina, I; Mizukami, T 1/31/2014 7/25/2014 Institute of Bio-Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51110847 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 1.000000 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51110850 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 5520 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51110852 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 22100 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51110856 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 4.0 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51110862 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 130 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51110863 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 70 ChEMBL 10.1016/j.bmcl.2017.12.053 10.7270/Q29W0J2W 29292224 n/a 12/28/2018 8/15/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51227585 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 1.2 ChEMBL 10.1016/j.bmc.2018.12.022 10.7270/Q2NP27P1 30581047 Pehere, AD; Nguyen, S; Garlick, SK; Wilson, DW; Hudson, I; Sykes, MJ; Morton, JD; Abell, AD 1/15/2019 2/18/2021 University of Adelaide http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51289132 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 1450 ChEMBL 10.1021/acsmedchemlett.9b00233 10.7270/Q2930XK7 31312413 Pacifico, S; Ferretti, V; Albanese, V; Fantinati, A; Gallerani, E; Nicoli, F; Gavioli, R; Zamberlan, F; Preti, D; Marastoni, M 7/11/2019 2/24/2021 University of Ferrara http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51289181 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 4590 ChEMBL 10.1021/acsmedchemlett.9b00233 10.7270/Q2930XK7 31312413 Pacifico, S; Ferretti, V; Albanese, V; Fantinati, A; Gallerani, E; Nicoli, F; Gavioli, R; Zamberlan, F; Preti, D; Marastoni, M 7/11/2019 2/24/2021 University of Ferrara http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51289196 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 7.0 ChEMBL 10.1021/acsmedchemlett.9b00233 10.7270/Q2930XK7 31312413 Pacifico, S; Ferretti, V; Albanese, V; Fantinati, A; Gallerani, E; Nicoli, F; Gavioli, R; Zamberlan, F; Preti, D; Marastoni, M 7/11/2019 2/24/2021 University of Ferrara http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51298902 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 30 ChEMBL 10.1016/j.bmc.2019.115161 10.7270/Q29W0JZJ 31732281 Uesugi, S; Honmura, Y; Nishiyama, M; Kusakabe, K; Tonouchi, A; Yamashita, T; Hashimoto, M; Kimura, KI 12/15/2019 2/25/2021 Iwate University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51298906 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 1600 ChEMBL 10.1016/j.bmc.2019.115161 10.7270/Q29W0JZJ 31732281 Uesugi, S; Honmura, Y; Nishiyama, M; Kusakabe, K; Tonouchi, A; Yamashita, T; Hashimoto, M; Kimura, KI 12/15/2019 2/25/2021 Iwate University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51298909 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 500 ChEMBL 10.1016/j.bmc.2019.115161 10.7270/Q29W0JZJ 31732281 Uesugi, S; Honmura, Y; Nishiyama, M; Kusakabe, K; Tonouchi, A; Yamashita, T; Hashimoto, M; Kimura, KI 12/15/2019 2/25/2021 Iwate University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51487773 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 22100 ChEMBL 10.7270/Q20R9TGT 34838650 Ettari, R; Iraci, N; Di Chio, C; Previti, S; Danzè, M; Zappalà, M 1/1/2022 6/23/2023 University of Messina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51487774 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 5520 ChEMBL 10.7270/Q20R9TGT 34838650 Ettari, R; Iraci, N; Di Chio, C; Previti, S; Danzè, M; Zappalà, M 1/1/2022 6/23/2023 University of Messina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51487775 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-5 Homo sapiens 1.4 ChEMBL 10.7270/Q20R9TGT 34838650 Ettari, R; Iraci, N; Di Chio, C; Previti, S; Danzè, M; Zappalà, M 1/1/2022 6/23/2023 University of Messina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6277&target=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-5&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 51487776 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-1 Homo sapiens 130 ChEMBL 10.7270/Q20R9TGT 34838650 Ettari, R; Iraci, N; Di Chio, C; Previti, S; Danzè, M; Zappalà, M 1/1/2022 6/23/2023 University of Messina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003479&target=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-1&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 51487777 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 Proteasome subunit beta type-2 Homo sapiens 1.000000 ChEMBL 10.7270/Q20R9TGT 34838650 Ettari, R; Iraci, N; Di Chio, C; Previti, S; Danzè, M; Zappalà, M 1/1/2022 6/23/2023 University of Messina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003459&target=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=Proteasome+subunit+beta+type-2&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 1 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 51159619 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 A5LHX3/O14818/P20618/P25786/P25787/P25788/P25789/P28062/P28065/P28066/P28070/P28072/P28074/P40306/P49720/P49721/P60900/Q8TAA3/Q99436 Homo sapiens 4500 ChEMBL 10.1016/j.bmcl.2005.02.013 10.7270/Q2CF9SVN 15780623 Momose, I; Umezawa, Y; Hirosawa, S; Iinuma, H; Ikeda, D 4/1/2005 8/23/2020 Numazu Bio-Medical Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000077&target=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 19 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 MALLDVCGAPRGQRPESALPVAGSGRRSDPGHYSFSMRSPELALPRGMQPTEFFQSLGGDGERNVQIEMAHGTTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAIAYATHRDSYSGGVVNMYHMKEDGWVKVESTDVSDLLHQYREANQ 6E5B,6AVO,7B12,7AWE Proteasome subunit beta type-8 PSB8_HUMAN P28062 B0UZC0 Q29824 Q5JNW6 Q5QNR8 Q96J48 MLRAGAPTGDLPRAGEVHTGTTIMAVEFDGGVVMGSDSRVSAGEAVVNRVFDKLSPLHERIYCALSGSAADAQAVADMAAYQLELHGIELEEPPLVLAAANVVRNISYKYREDLSAHLMVAGWDQREGGQVYGTLGGMLTRQPFAIGGSGSTFIYGYVDAAYKPGMSPEECRRFTTDAIALAMSRDGSSGGVIYLVTITAAGVDHRVILGNELPKFYDE 6E5B,7B12,7AWE,6AVO,8YVG,8YSX Proteasome subunit beta type-9 PSB9_HUMAN P28065 B0V0T1 Q16523 Q5JNW4 MAATLLAARGAGPAPAWGPEAFTPDWESREVSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDRIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAASLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTANALALAMERDGSSGGVIRLAAIAESGVERQVLLGDQIPKFAVATLPPA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,9RKZ,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6R70,9QVX,6XMJ,4R67,4R3O,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit beta type-6 PSB6_HUMAN P28072 Q96J55 MFRNQYDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSELAAHQKKILHVDNHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGARSQSARTYLERHMSEFMECNLNELVKHGLRALRETLPAEQDLTTKNVSIGIVGKDLEFTIYDDDDVSPFLEGLEERPQRKAQPAQPADEPAEKADEPMEH 9YUZ,9UG9,9UF8,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9VUG,9VUF,9VUE,9U7R,9U3L,9SZV,9SZT,9MBQ,9MBP,9HEU,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,7DRW,7DR7,7DR6,8YVG,8YSX,8QYS,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,5M32,9QVX Proteasome subunit alpha type-1 PSA1_HUMAN P25786 A8K400 Q53YE8 Q9BRV9 MAERGYSFSLTTFSPSGKLVQIEYALAAVAGGAPSVGIKAANGVVLATEKKQKSILYDERSVHKVEPITKHIGLVYSGMGPDYRVLVHRARKLAQQYYLVYQEPIPTAQLVQRVASVMQEYTQSGGVRPFGVSLLICGWNEGRPYLFQSDPSGAYFAWKATAMGKNYVNGKTFLEKRYNEDLELEDAIHTAILTLKESFEGQMTEDNIEVGICNEAGFRRLTPTEVKDYLAAIA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YVG,8YSX,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYS,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,9U7R,9U3L,9MBQ,9MBP,9HMN,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6XMJ,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,4R67,4R3O,22MM,1IRU,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,6R70,9QVX,7B12,7AWE Proteasome subunit alpha type-2 PSA2_HUMAN P25787 Q6ICS6 Q9BU45 MSSIGTGYDLSASTFSPDGRVFQVEYAMKAVENSSTAIGIRCKDGVVFGVEKLVLSKLYEEGSNKRLFNVDRHVGMAVAGLLADARSLADIAREEASNFRSNFGYNIPLKHLADRVAMYVHAYTLYSAVRPFGCSFMLGSYSVNDGAQLYMIDPSGVSYGYWGCAIGKARQAAKTEIEKLQMKEMTCRDIVKEVAKIIYIVHDEVKDKAFELELSWVGELTNGRHEIVPKDIREEAEKYAKESLKEEDESDDDNM 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7E55,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5DSV,5A0Q,9U7R,9U3L,9MBQ,9MBP,9HMN,8FZ6,8FZ5,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7DRW,7DR7,7DR6,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,1IRU,6TU3,6EPF,6EPE,6EPD,6EPC,8YVP,8YPK,3UNH,3UNF,3UNE,3UNB,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,8QYS,6R70,9QVX Proteasome subunit alpha type-3 PSA3_HUMAN P25788 B2RCK6 Q86U83 Q8N1D8 Q9BS70 MSRRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGEMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTRENGKTVIRVLKQKEVEQLIKKHEEEEAKAEREKKEKEQKEKDK 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,7AWE,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,6R70,8QYS,9QVX Proteasome subunit alpha type-4 PSA4_HUMAN P25789 D3DW86 Q53XP2 Q567Q5 Q8TBD1 MFLTRSEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKTLIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGEEDADPGAMSRPFGVALLFGGVDEKGPQLFHMDPSGTFVQCDARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKLNATNIELATVQPGQNFHMFTKEELEEVIKDI 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDI,9NKJ,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8O,9E8N,9E8L,9E8K,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YVP,8YVG,8YSX,8YPK,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QYO,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,22MM,8QZ9,8QYN,8QYM,8QYL,8QYJ,8QYS,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9QVX,6R70,7B12,7AWE Proteasome subunit alpha type-5 PSA5_HUMAN P28066 B2R8F6 B4E2V4 Q3T1C1 Q6IBF7 MSRGSSAGFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITENIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATAAGVKQTESTSFLEKKVKKKFDWTFEQTVETAITCLSTVLSIDFKPSEIEVGVVTVENPKFRILTEAEIDAHLVALAERD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6TU3,6RGQ,6REY,6KWY,6EPF,6EPE,6EPD,6EPC,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,6XMJ,6R70,4R67,4R3O,7B12,7AWE,9QVX,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit alpha type-6 PSA6_HUMAN P60900 B2R7J9 B4DQR4 B4DXJ9 P34062 Q6IB60 MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIGRGAKSVREFLEKNYTDEAIETDDLTIKLVIKALLEVVQSGGKNIELAVMRRDQSLKILNPEEIEKYVAEIEKEKEENEKKKQKKAS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,22MM,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7AWE,6R70,7B12,8QYS,9QVX Proteasome subunit alpha type-7 PSA7_HUMAN O14818 B2R515 Q5JXJ2 Q9BR53 Q9H4K5 Q9UEU8 MASRYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVCMAFAVLTIFIGLTADARVVINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDAIASDSEAIKLAIKALLEVVQSGGKNIELAIIRRNQPLKMFSAKEVELYVTEIEKEKEEAEKKKSKKSV Proteasome subunit alpha-type 8 PSMA8_HUMAN Q8TAA3 B0YJ75 Q8IVP4 Q8TA98 Q8TAA2 MLKPALEPRGGFSFENCQRNASLERVLPGLKVPHARKTGTTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATVTRILRQTLFRYQGHVGASLIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLLVEAVTAGILGDLGSGGNVDACVITKTGAKLLRTLSSPTEPVKRSGRYHFVPGTTAVLTQTVKPLTLELVEETVQAMEVE 6E5B,6AVO,7AWE Proteasome subunit beta type-10 PSB10_HUMAN P40306 B2R5J4 Q5U098 MALQDVCKWQSPDTQGPSPHLPRAGGWAVPRGCDPQTFLQIHGPRLAHGTTTLAFRFRHGVIAAADTRSSCGSYVACPASCKVIPVHQHLLGTTSGTSADCATWYRVLQRELRLRELREGQLPSVASAAKLLSAMMSQYRGLDLCVATALCGWDRSGPELFYVYSDGTRLQGDIFSVGSGSPYAYGVLDRGYRYDMSTQEAYALARCAVAHATHRDAYSGGSVDLFHVRESGWEHVSRSDACVLYVELQKLLEPEPEEDASHAHPEPATAHRAAEDRELSVGPGEVTPGDSRMPAGTETV Proteasome subunit beta type-11 PSB11_HUMAN A5LHX3 MSIMSYNGGAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYTLMSMVANLLYEKRFGPYYTEPVIAGLDPKTFKPFICSLDLIGCPMVTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLFETISQAMLNAVDRDAVSGMGVIVHIIEKDKITTRTLKARMD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QZ9,8QYO,8QYN,8QYM,8QYL,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,9U7R,9U3L,9RKZ,9QVX,9MBQ,9MBP,9HMN,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7B12,7AWE,6XMJ,6WJN,6WJD,6R70,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5T0J,5T0I,5T0H,5T0G,5T0C,5A0Q,4R67,4R3O,22MM,8YVP,8YPK,6TU3,3UNH,3UNF,3UNE,3UNB,8QYS Proteasome subunit beta type-3 PSB3_HUMAN P49720 P31147 Q0P6J7 Q96E27 MEAFLGSRSGLWAGGPAPGQFYRIPSTPDSFMDPASALYRGPITRTQNPMVTGTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNNSTMLGASGDYADFQYLKQVLGQMVIDEELLGDGHSYSPRAIHSWLTRAMYSRRSKMNPLWNTMVIGGYADGESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREVLEKQPVLSQTEARDLVERCMRVLYYRDARSYNRFQIATVTEKGVEIEGPLSTETNWDIAHMISGFE 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9BW4,9BV3,9BV2,9BV1,9BUI,8TM6,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YIZ,8YIY,8YIX,9RKZ,9HMN,8UD9,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,6AVO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,6XMJ,4R67,4R3O,6R70,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,7B12,7AWE,9QVX Proteasome subunit beta type-4 PSB4_HUMAN P28070 B2R9L3 P31148 Q5SZS5 Q6IBI4 Q969L6 MAAVSVYAPPVGGFSFDNCRRNAVLEADFAKRGYKLPKVRKTGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTANRMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAIAAGIFNDLGSGSNIDLCVISKNKLDFLRPYTVPNKKGTRLGRYRCEKGTTAVLTEKITPLEIEVLEETVQTMDTS 8QZ9,8QYN,8QYM,8QYL,8QYJ,9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8TM6,8TM5,8TM4,8QYO,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,9RKZ,9HMN,8UD9,8CVS,8CVR,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,9QVX,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O Proteasome subunit beta type-7 PSB7_HUMAN Q99436 B4E0P1 Q5TBG6 Q96AG8 Q9BWA7 51159624 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 A5LHX3/O14818/P20618/P25786/P25787/P25788/P25789/P28062/P28065/P28066/P28070/P28072/P28074/P40306/P49720/P49721/P60900/Q8TAA3/Q99436 Homo sapiens 1400 ChEMBL 10.1016/j.bmcl.2005.02.013 10.7270/Q2CF9SVN 15780623 Momose, I; Umezawa, Y; Hirosawa, S; Iinuma, H; Ikeda, D 4/1/2005 8/23/2020 Numazu Bio-Medical Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000077&target=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 19 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 MALLDVCGAPRGQRPESALPVAGSGRRSDPGHYSFSMRSPELALPRGMQPTEFFQSLGGDGERNVQIEMAHGTTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAIAYATHRDSYSGGVVNMYHMKEDGWVKVESTDVSDLLHQYREANQ 6E5B,6AVO,7B12,7AWE Proteasome subunit beta type-8 PSB8_HUMAN P28062 B0UZC0 Q29824 Q5JNW6 Q5QNR8 Q96J48 MLRAGAPTGDLPRAGEVHTGTTIMAVEFDGGVVMGSDSRVSAGEAVVNRVFDKLSPLHERIYCALSGSAADAQAVADMAAYQLELHGIELEEPPLVLAAANVVRNISYKYREDLSAHLMVAGWDQREGGQVYGTLGGMLTRQPFAIGGSGSTFIYGYVDAAYKPGMSPEECRRFTTDAIALAMSRDGSSGGVIYLVTITAAGVDHRVILGNELPKFYDE 6E5B,7B12,7AWE,6AVO,8YVG,8YSX Proteasome subunit beta type-9 PSB9_HUMAN P28065 B0V0T1 Q16523 Q5JNW4 MAATLLAARGAGPAPAWGPEAFTPDWESREVSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDRIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAASLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTANALALAMERDGSSGGVIRLAAIAESGVERQVLLGDQIPKFAVATLPPA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,9RKZ,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6R70,9QVX,6XMJ,4R67,4R3O,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit beta type-6 PSB6_HUMAN P28072 Q96J55 MFRNQYDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSELAAHQKKILHVDNHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGARSQSARTYLERHMSEFMECNLNELVKHGLRALRETLPAEQDLTTKNVSIGIVGKDLEFTIYDDDDVSPFLEGLEERPQRKAQPAQPADEPAEKADEPMEH 9YUZ,9UG9,9UF8,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9VUG,9VUF,9VUE,9U7R,9U3L,9SZV,9SZT,9MBQ,9MBP,9HEU,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,7DRW,7DR7,7DR6,8YVG,8YSX,8QYS,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,5M32,9QVX Proteasome subunit alpha type-1 PSA1_HUMAN P25786 A8K400 Q53YE8 Q9BRV9 MAERGYSFSLTTFSPSGKLVQIEYALAAVAGGAPSVGIKAANGVVLATEKKQKSILYDERSVHKVEPITKHIGLVYSGMGPDYRVLVHRARKLAQQYYLVYQEPIPTAQLVQRVASVMQEYTQSGGVRPFGVSLLICGWNEGRPYLFQSDPSGAYFAWKATAMGKNYVNGKTFLEKRYNEDLELEDAIHTAILTLKESFEGQMTEDNIEVGICNEAGFRRLTPTEVKDYLAAIA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YVG,8YSX,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYS,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,9U7R,9U3L,9MBQ,9MBP,9HMN,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6XMJ,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,4R67,4R3O,22MM,1IRU,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,6R70,9QVX,7B12,7AWE Proteasome subunit alpha type-2 PSA2_HUMAN P25787 Q6ICS6 Q9BU45 MSSIGTGYDLSASTFSPDGRVFQVEYAMKAVENSSTAIGIRCKDGVVFGVEKLVLSKLYEEGSNKRLFNVDRHVGMAVAGLLADARSLADIAREEASNFRSNFGYNIPLKHLADRVAMYVHAYTLYSAVRPFGCSFMLGSYSVNDGAQLYMIDPSGVSYGYWGCAIGKARQAAKTEIEKLQMKEMTCRDIVKEVAKIIYIVHDEVKDKAFELELSWVGELTNGRHEIVPKDIREEAEKYAKESLKEEDESDDDNM 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7E55,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5DSV,5A0Q,9U7R,9U3L,9MBQ,9MBP,9HMN,8FZ6,8FZ5,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7DRW,7DR7,7DR6,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,1IRU,6TU3,6EPF,6EPE,6EPD,6EPC,8YVP,8YPK,3UNH,3UNF,3UNE,3UNB,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,8QYS,6R70,9QVX Proteasome subunit alpha type-3 PSA3_HUMAN P25788 B2RCK6 Q86U83 Q8N1D8 Q9BS70 MSRRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGEMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTRENGKTVIRVLKQKEVEQLIKKHEEEEAKAEREKKEKEQKEKDK 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,7AWE,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,6R70,8QYS,9QVX Proteasome subunit alpha type-4 PSA4_HUMAN P25789 D3DW86 Q53XP2 Q567Q5 Q8TBD1 MFLTRSEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKTLIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGEEDADPGAMSRPFGVALLFGGVDEKGPQLFHMDPSGTFVQCDARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKLNATNIELATVQPGQNFHMFTKEELEEVIKDI 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDI,9NKJ,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8O,9E8N,9E8L,9E8K,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YVP,8YVG,8YSX,8YPK,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QYO,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,22MM,8QZ9,8QYN,8QYM,8QYL,8QYJ,8QYS,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9QVX,6R70,7B12,7AWE Proteasome subunit alpha type-5 PSA5_HUMAN P28066 B2R8F6 B4E2V4 Q3T1C1 Q6IBF7 MSRGSSAGFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITENIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATAAGVKQTESTSFLEKKVKKKFDWTFEQTVETAITCLSTVLSIDFKPSEIEVGVVTVENPKFRILTEAEIDAHLVALAERD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6TU3,6RGQ,6REY,6KWY,6EPF,6EPE,6EPD,6EPC,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,6XMJ,6R70,4R67,4R3O,7B12,7AWE,9QVX,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit alpha type-6 PSA6_HUMAN P60900 B2R7J9 B4DQR4 B4DXJ9 P34062 Q6IB60 MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIGRGAKSVREFLEKNYTDEAIETDDLTIKLVIKALLEVVQSGGKNIELAVMRRDQSLKILNPEEIEKYVAEIEKEKEENEKKKQKKAS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,22MM,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7AWE,6R70,7B12,8QYS,9QVX Proteasome subunit alpha type-7 PSA7_HUMAN O14818 B2R515 Q5JXJ2 Q9BR53 Q9H4K5 Q9UEU8 MASRYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVCMAFAVLTIFIGLTADARVVINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDAIASDSEAIKLAIKALLEVVQSGGKNIELAIIRRNQPLKMFSAKEVELYVTEIEKEKEEAEKKKSKKSV Proteasome subunit alpha-type 8 PSMA8_HUMAN Q8TAA3 B0YJ75 Q8IVP4 Q8TA98 Q8TAA2 MLKPALEPRGGFSFENCQRNASLERVLPGLKVPHARKTGTTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATVTRILRQTLFRYQGHVGASLIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLLVEAVTAGILGDLGSGGNVDACVITKTGAKLLRTLSSPTEPVKRSGRYHFVPGTTAVLTQTVKPLTLELVEETVQAMEVE 6E5B,6AVO,7AWE Proteasome subunit beta type-10 PSB10_HUMAN P40306 B2R5J4 Q5U098 MALQDVCKWQSPDTQGPSPHLPRAGGWAVPRGCDPQTFLQIHGPRLAHGTTTLAFRFRHGVIAAADTRSSCGSYVACPASCKVIPVHQHLLGTTSGTSADCATWYRVLQRELRLRELREGQLPSVASAAKLLSAMMSQYRGLDLCVATALCGWDRSGPELFYVYSDGTRLQGDIFSVGSGSPYAYGVLDRGYRYDMSTQEAYALARCAVAHATHRDAYSGGSVDLFHVRESGWEHVSRSDACVLYVELQKLLEPEPEEDASHAHPEPATAHRAAEDRELSVGPGEVTPGDSRMPAGTETV Proteasome subunit beta type-11 PSB11_HUMAN A5LHX3 MSIMSYNGGAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYTLMSMVANLLYEKRFGPYYTEPVIAGLDPKTFKPFICSLDLIGCPMVTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLFETISQAMLNAVDRDAVSGMGVIVHIIEKDKITTRTLKARMD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QZ9,8QYO,8QYN,8QYM,8QYL,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,9U7R,9U3L,9RKZ,9QVX,9MBQ,9MBP,9HMN,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7B12,7AWE,6XMJ,6WJN,6WJD,6R70,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5T0J,5T0I,5T0H,5T0G,5T0C,5A0Q,4R67,4R3O,22MM,8YVP,8YPK,6TU3,3UNH,3UNF,3UNE,3UNB,8QYS Proteasome subunit beta type-3 PSB3_HUMAN P49720 P31147 Q0P6J7 Q96E27 MEAFLGSRSGLWAGGPAPGQFYRIPSTPDSFMDPASALYRGPITRTQNPMVTGTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNNSTMLGASGDYADFQYLKQVLGQMVIDEELLGDGHSYSPRAIHSWLTRAMYSRRSKMNPLWNTMVIGGYADGESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREVLEKQPVLSQTEARDLVERCMRVLYYRDARSYNRFQIATVTEKGVEIEGPLSTETNWDIAHMISGFE 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9BW4,9BV3,9BV2,9BV1,9BUI,8TM6,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YIZ,8YIY,8YIX,9RKZ,9HMN,8UD9,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,6AVO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,6XMJ,4R67,4R3O,6R70,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,7B12,7AWE,9QVX Proteasome subunit beta type-4 PSB4_HUMAN P28070 B2R9L3 P31148 Q5SZS5 Q6IBI4 Q969L6 MAAVSVYAPPVGGFSFDNCRRNAVLEADFAKRGYKLPKVRKTGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTANRMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAIAAGIFNDLGSGSNIDLCVISKNKLDFLRPYTVPNKKGTRLGRYRCEKGTTAVLTEKITPLEIEVLEETVQTMDTS 8QZ9,8QYN,8QYM,8QYL,8QYJ,9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8TM6,8TM5,8TM4,8QYO,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,9RKZ,9HMN,8UD9,8CVS,8CVR,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,9QVX,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O Proteasome subunit beta type-7 PSB7_HUMAN Q99436 B4E0P1 Q5TBG6 Q96AG8 Q9BWA7 51159634 CC(C)C[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1 InChI=1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33) TZYWCYJVHRLUCT-UHFFFAOYSA-N 50069985 {1-[(S)-(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::benzyloxycarbonyl-Leu-Leu-leucinal::benzyl(S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-H::{1-[1-(1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::Z-L-leu-L-leu-L-leu-H::benzyl (S)-4-methyl-1-((S)-4-methyl-1-((S)-4-methyl-1-oxopentan-2-ylamino)-1-oxopentan-2-ylamino)-1-oxopentan-2-ylcarbamate::Z-Leu-Leu-Leu-al::Cbz-L-leu-L-leu-L-leu-CHO::{(S)-1-[(S)-1-((S)-1-Formyl-3-methyl-butylcarbamoyl)-3-methyl-butylcarbamoyl]-3-methyl-butyl}-carbamic acid benzyl ester::MG-132::(S)-4-methyl-2-(3-phenyl-propionylamino)-pentanoic acid [(S)-1-((S)-1-formyl-3-methyl-butylcarbamoyl)-3-methyl-butyl]-amide::CHEMBL64925::MG-13 A5LHX3/O14818/P20618/P25786/P25787/P25788/P25789/P28062/P28065/P28066/P28070/P28072/P28074/P40306/P49720/P49721/P60900/Q8TAA3/Q99436 Homo sapiens 68 ChEMBL 10.1016/j.bmcl.2005.02.013 10.7270/Q2CF9SVN 15780623 Momose, I; Umezawa, Y; Hirosawa, S; Iinuma, H; Ikeda, D 4/1/2005 8/23/2020 Numazu Bio-Medical Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50069985 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000077&target=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50069985&enzyme=A5LHX3%2FO14818%2FP20618%2FP25786%2FP25787%2FP25788%2FP25789%2FP28062%2FP28065%2FP28066%2FP28070%2FP28072%2FP28074%2FP40306%2FP49720%2FP49721%2FP60900%2FQ8TAA3%2FQ99436&column=ki&startPg=0&Increment=50&submit=Search LDZ 22MM,4G4S,8CVR,8CVS,8CVT,9MBP,9MBQ,9NKF,9NKG,9NKJ,9U3L,9U7R 462382 103963944 CHEMBL64925 19 MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,8QYS,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9RKZ,9QVX Proteasome subunit beta type-5 PSB5_HUMAN P28074 B2R4N9 B4DUM9 D3DS43 E9PAV2 Q16242 Q6PEW2 Q7Z3B5 Q86T01 Q9TNN9 MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRIIDKNGIHDLDNISFPKQGS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9U7R,9U3L,9SZV,9SZT,9RKZ,9NKJ,9NKI,9NKG,9NKF,9MBQ,9MBP,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QYO,8QYM,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6WJD,6RGQ,6REY,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,6KWY,6E5B,6AVO,5T0J,5T0I,5T0H,5T0G,5T0C,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5A0Q,22MM,1IRU,8QZ9,8QYN,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,8QYS,7B12,7AWE,9QVX,6R70,5M32 Proteasome subunit beta type-2 PSB2_HUMAN P49721 D3DPS0 P31145 Q9BWZ9 MLSSTAMYSAPGRDLGMEPHRAAGPLQLRFSPYVFNGGTILAIAGEDFAIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLSLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVSLRKD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8QZ9,8QYO,8QYN,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YVP,8YPK,9RKZ,9HMN,8UD9,8AZK,7V5M,7V5G,7PG9,7LXV,7B12,7AWE,6XMJ,6WJN,6RGQ,6REY,6R70,6AVO,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,4R67,4R3O,1IRU,9QVX,8QYS Proteasome subunit beta type-1 PSB1_HUMAN P20618 B5BU76 Q9BWA8 MALLDVCGAPRGQRPESALPVAGSGRRSDPGHYSFSMRSPELALPRGMQPTEFFQSLGGDGERNVQIEMAHGTTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAIAYATHRDSYSGGVVNMYHMKEDGWVKVESTDVSDLLHQYREANQ 6E5B,6AVO,7B12,7AWE Proteasome subunit beta type-8 PSB8_HUMAN P28062 B0UZC0 Q29824 Q5JNW6 Q5QNR8 Q96J48 MLRAGAPTGDLPRAGEVHTGTTIMAVEFDGGVVMGSDSRVSAGEAVVNRVFDKLSPLHERIYCALSGSAADAQAVADMAAYQLELHGIELEEPPLVLAAANVVRNISYKYREDLSAHLMVAGWDQREGGQVYGTLGGMLTRQPFAIGGSGSTFIYGYVDAAYKPGMSPEECRRFTTDAIALAMSRDGSSGGVIYLVTITAAGVDHRVILGNELPKFYDE 6E5B,7B12,7AWE,6AVO,8YVG,8YSX Proteasome subunit beta type-9 PSB9_HUMAN P28065 B0V0T1 Q16523 Q5JNW4 MAATLLAARGAGPAPAWGPEAFTPDWESREVSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDRIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAASLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTANALALAMERDGSSGGVIRLAAIAESGVERQVLLGDQIPKFAVATLPPA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8TM6,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,9RKZ,9HMN,8UD9,8CVS,8CVR,8AZK,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,1IRU,6R70,9QVX,6XMJ,4R67,4R3O,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit beta type-6 PSB6_HUMAN P28072 Q96J55 MFRNQYDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSELAAHQKKILHVDNHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGARSQSARTYLERHMSEFMECNLNELVKHGLRALRETLPAEQDLTTKNVSIGIVGKDLEFTIYDDDDVSPFLEGLEERPQRKAQPAQPADEPAEKADEPMEH 9YUZ,9UG9,9UF8,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9VUG,9VUF,9VUE,9U7R,9U3L,9SZV,9SZT,9MBQ,9MBP,9HEU,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8FZ6,8FZ5,7DRW,7DR7,7DR6,8YVG,8YSX,8QYS,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,5M32,9QVX Proteasome subunit alpha type-1 PSA1_HUMAN P25786 A8K400 Q53YE8 Q9BRV9 MAERGYSFSLTTFSPSGKLVQIEYALAAVAGGAPSVGIKAANGVVLATEKKQKSILYDERSVHKVEPITKHIGLVYSGMGPDYRVLVHRARKLAQQYYLVYQEPIPTAQLVQRVASVMQEYTQSGGVRPFGVSLLICGWNEGRPYLFQSDPSGAYFAWKATAMGKNYVNGKTFLEKRYNEDLELEDAIHTAILTLKESFEGQMTEDNIEVGICNEAGFRRLTPTEVKDYLAAIA 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YVG,8YSX,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYS,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,9U7R,9U3L,9MBQ,9MBP,9HMN,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6XMJ,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,4R67,4R3O,22MM,1IRU,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,6R70,9QVX,7B12,7AWE Proteasome subunit alpha type-2 PSA2_HUMAN P25787 Q6ICS6 Q9BU45 MSSIGTGYDLSASTFSPDGRVFQVEYAMKAVENSSTAIGIRCKDGVVFGVEKLVLSKLYEEGSNKRLFNVDRHVGMAVAGLLADARSLADIAREEASNFRSNFGYNIPLKHLADRVAMYVHAYTLYSAVRPFGCSFMLGSYSVNDGAQLYMIDPSGVSYGYWGCAIGKARQAAKTEIEKLQMKEMTCRDIVKEVAKIIYIVHDEVKDKAFELELSWVGELTNGRHEIVPKDIREEAEKYAKESLKEEDESDDDNM 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7E55,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5DSV,5A0Q,9U7R,9U3L,9MBQ,9MBP,9HMN,8FZ6,8FZ5,8AZK,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7DRW,7DR7,7DR6,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,1IRU,6TU3,6EPF,6EPE,6EPD,6EPC,8YVP,8YPK,3UNH,3UNF,3UNE,3UNB,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,7AWE,8QYS,6R70,9QVX Proteasome subunit alpha type-3 PSA3_HUMAN P25788 B2RCK6 Q86U83 Q8N1D8 Q9BS70 MSRRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGEMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTRENGKTVIRVLKQKEVEQLIKKHEEEEAKAEREKKEKEQKEKDK 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,7AWE,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7B12,6R70,8QYS,9QVX Proteasome subunit alpha type-4 PSA4_HUMAN P25789 D3DW86 Q53XP2 Q567Q5 Q8TBD1 MFLTRSEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDAHIGCAMSGLIADAKTLIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGEEDADPGAMSRPFGVALLFGGVDEKGPQLFHMDPSGTFVQCDARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLIILKQVMEEKLNATNIELATVQPGQNFHMFTKEELEEVIKDI 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDI,9NKJ,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8O,9E8N,9E8L,9E8K,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YVP,8YVG,8YSX,8YPK,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QYO,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,3UNH,3UNF,3UNE,3UNB,22MM,8QZ9,8QYN,8QYM,8QYL,8QYJ,8QYS,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,9QVX,6R70,7B12,7AWE Proteasome subunit alpha type-5 PSA5_HUMAN P28066 B2R8F6 B4E2V4 Q3T1C1 Q6IBF7 MSRGSSAGFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITENIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATAAGVKQTESTSFLEKKVKKKFDWTFEQTVETAITCLSTVLSIDFKPSEIEVGVVTVENPKFRILTEAEIDAHLVALAERD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDL,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8FZ6,8FZ5,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,7DRW,7DR7,7DR6,6TU3,6RGQ,6REY,6KWY,6EPF,6EPE,6EPD,6EPC,6E5B,6AVO,5M32,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,6XMJ,6R70,4R67,4R3O,7B12,7AWE,9QVX,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO Proteasome subunit alpha type-6 PSA6_HUMAN P60900 B2R7J9 B4DQR4 B4DXJ9 P34062 Q6IB60 MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIGRGAKSVREFLEKNYTDEAIETDDLTIKLVIKALLEVVQSGGKNIELAVMRRDQSLKILNPEEIEKYVAEIEKEKEENEKKKQKKAS 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9RKZ,9QOO,9QON,9PF1,9PDN,9PDI,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HMN,9HEU,9E8Q,9E8O,9E8N,9E8L,9E8K,9E8J,9E8I,9E8H,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8UD9,8TM6,8TM5,8TM4,8TM3,8QZ9,8QYO,8QYN,8QYM,8QYL,8QYJ,8K0G,8JTI,8JRT,8JRI,8CXB,8CVT,8CVS,8CVR,8BZL,8AZK,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5LN3,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,5GJR,5GJQ,5A0Q,22MM,1IRU,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,6XMJ,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O,7AWE,6R70,7B12,8QYS,9QVX Proteasome subunit alpha type-7 PSA7_HUMAN O14818 B2R515 Q5JXJ2 Q9BR53 Q9H4K5 Q9UEU8 MASRYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIRGTNIVVLGVEKKSVAKLQDERTVRKICALDDHVCMAFAVLTIFIGLTADARVVINRARVECQSHKLTVEDPVTVEYITRFIATLKQKYTQSNGRRPFGISALIVGFDDDGISRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTEDAIASDSEAIKLAIKALLEVVQSGGKNIELAIIRRNQPLKMFSAKEVELYVTEIEKEKEEAEKKKSKKSV Proteasome subunit alpha-type 8 PSMA8_HUMAN Q8TAA3 B0YJ75 Q8IVP4 Q8TA98 Q8TAA2 MLKPALEPRGGFSFENCQRNASLERVLPGLKVPHARKTGTTIAGLVFQDGVILGADTRATNDSVVADKSCEKIHFIAPKIYCCGAGVAADAEMTTRMVASKMELHALSTGREPRVATVTRILRQTLFRYQGHVGASLIVGGVDLTGPQLYGVHPHGSYSRLPFTALGSGQDAALAVLEDRFQPNMTLEAAQGLLVEAVTAGILGDLGSGGNVDACVITKTGAKLLRTLSSPTEPVKRSGRYHFVPGTTAVLTQTVKPLTLELVEETVQAMEVE 6E5B,6AVO,7AWE Proteasome subunit beta type-10 PSB10_HUMAN P40306 B2R5J4 Q5U098 MALQDVCKWQSPDTQGPSPHLPRAGGWAVPRGCDPQTFLQIHGPRLAHGTTTLAFRFRHGVIAAADTRSSCGSYVACPASCKVIPVHQHLLGTTSGTSADCATWYRVLQRELRLRELREGQLPSVASAAKLLSAMMSQYRGLDLCVATALCGWDRSGPELFYVYSDGTRLQGDIFSVGSGSPYAYGVLDRGYRYDMSTQEAYALARCAVAHATHRDAYSGGSVDLFHVRESGWEHVSRSDACVLYVELQKLLEPEPEEDASHAHPEPATAHRAAEDRELSVGPGEVTPGDSRMPAGTETV Proteasome subunit beta type-11 PSB11_HUMAN A5LHX3 MSIMSYNGGAVMAMKGKNCVAIAADRRFGIQAQMVTTDFQKIFPMGDRLYIGLAGLATDVQTVAQRLKFRLNLYELKEGRQIKPYTLMSMVANLLYEKRFGPYYTEPVIAGLDPKTFKPFICSLDLIGCPMVTDDFVVSGTCAEQMYGMCESLWEPNMDPDHLFETISQAMLNAVDRDAVSGMGVIVHIIEKDKITTRTLKARMD 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8UD9,8TM6,8TM5,8TM4,8QZ9,8QYO,8QYN,8QYM,8QYL,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7V5M,7V5G,7PG9,7NHT,7NAQ,7NAP,7NAO,7NAN,7LXV,6RGQ,6REY,6KWY,6E5B,6AVO,5M32,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5L4G,9U7R,9U3L,9RKZ,9QVX,9MBQ,9MBP,9HMN,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,7B12,7AWE,6XMJ,6WJN,6WJD,6R70,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,5T0J,5T0I,5T0H,5T0G,5T0C,5A0Q,4R67,4R3O,22MM,8YVP,8YPK,6TU3,3UNH,3UNF,3UNE,3UNB,8QYS Proteasome subunit beta type-3 PSB3_HUMAN P49720 P31147 Q0P6J7 Q96E27 MEAFLGSRSGLWAGGPAPGQFYRIPSTPDSFMDPASALYRGPITRTQNPMVTGTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNNSTMLGASGDYADFQYLKQVLGQMVIDEELLGDGHSYSPRAIHSWLTRAMYSRRSKMNPLWNTMVIGGYADGESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREVLEKQPVLSQTEARDLVERCMRVLYYRDARSYNRFQIATVTEKGVEIEGPLSTETNWDIAHMISGFE 9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9BW4,9BV3,9BV2,9BV1,9BUI,8TM6,8CXB,8CVT,8CVS,8CVR,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,6E5B,5M32,5L4G,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8YIZ,8YIY,8YIX,9RKZ,9HMN,8UD9,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,6AVO,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,6XMJ,4R67,4R3O,6R70,6WJN,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,7B12,7AWE,9QVX Proteasome subunit beta type-4 PSB4_HUMAN P28070 B2R9L3 P31148 Q5SZS5 Q6IBI4 Q969L6 MAAVSVYAPPVGGFSFDNCRRNAVLEADFAKRGYKLPKVRKTGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTANRMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAIAAGIFNDLGSGSNIDLCVISKNKLDFLRPYTVPNKKGTRLGRYRCEKGTTAVLTEKITPLEIEVLEETVQTMDTS 8QZ9,8QYN,8QYM,8QYL,8QYJ,9YUZ,9VUG,9VUF,9VUE,9UG9,9UF8,9SZV,9SZT,9NKJ,9NKI,9NKG,9NKF,9M2W,9K5E,9K5D,9K5C,9K5B,9K5A,9K59,9K58,9K57,9K56,9K55,9K54,9K53,9K51,9K50,9K4Z,9K4Y,9K4X,9K4W,9K4V,9K4U,9K4T,9K4S,9K4R,9K4P,9K4O,9K4M,9K4L,9K4K,9K4J,9HEU,9E8Q,9E8O,9E8G,9BW4,9BV3,9BV2,9BV1,9BUI,8YIZ,8YIY,8YIX,8USC,8USB,8TM6,8TM5,8TM4,8QYO,8CXB,8CVT,8BZL,7W3M,7W3K,7W3J,7W3I,7W3H,7W3G,7W3F,7W3C,7W3B,7W3A,7W39,7W38,7W37,7NHT,7NAQ,7NAP,7NAO,7NAN,6KWY,5M32,9U7R,9U3L,9MBQ,9MBP,7QYB,7QYA,7QY7,7QXX,7QXW,7QXU,7QXP,7QXN,6WJD,6MSK,6MSJ,6MSH,6MSG,6MSE,6MSD,6MSB,5T0J,5T0I,5T0H,5T0G,5T0C,22MM,8QYS,9RKZ,9HMN,8UD9,8CVS,8CVR,7V5M,7V5G,7PG9,7LXV,6RGQ,6REY,5LF7,5LF6,5LF4,5LF3,5LF1,5LF0,5LEZ,5LEY,5LEX,5LE5,5A0Q,9QVX,6XMJ,6WJN,6R70,5VFU,5VFT,5VFS,5VFR,5VFQ,5VFP,5VFO,4R67,4R3O Proteasome subunit beta type-7 PSB7_HUMAN Q99436 B4E0P1 Q5TBG6 Q96AG8 Q9BWA7 51587422 CN1C(=O)N(C(=O)C12CCN(CC2)CC3CCOCC3)c4ccc(cc4)C(F)(F)F InChI=1S/C21H26F3N3O3/c1-25-19(29)27(17-4-2-16(3-5-17)21(22,23)24)18(28)20(25)8-10-26(11-9-20)14-15-6-12-30-13-7-15/h2-5,15H,6-14H2,1H3 PGRXOQYVDWCZAG-UHFFFAOYSA-N 50639125 CHEMBL5561666 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase Homo sapiens 106 ChEMBL 10.7270/Q26H4P1W 38470227 Dorel, R; Sun, D; Carruthers, N; Castanedo, GM; Ung, PM; Factor, DC; Li, T; Baumann, H; Janota, D; Pang, J; Salphati, L; Meklemburg, R; Korman, AJ; Harper, HE; Stubblefield, S; Payandeh, J; McHugh, D; Lang, BT; Tesar, PJ; Dere, E; Masureel, M; Adams, DJ; Volgraf, M; Braun, MG //0 10/11/2025 Genentech http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50639125 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50001269&target=3-beta-hydroxysteroid-Delta%288%29%2CDelta%287%29-isomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50639125&enzyme=3-beta-hydroxysteroid-Delta%288%29%2CDelta%287%29-isomerase&column=ki&startPg=0&Increment=50&submit=Search A1AEV 8W0S 171662249 519659528 1 MTTNAGPLHPYWPQHLRLDNFVPNDRPTWHILAGLFSVTGVLVVTTWLLSGRAAVVPLGTWRRLSLCWFAVCGFIHLVIEGWFVLYYEDLLGDQAFLSQLWKEYAKGDSRYILGDNFTVCMETITACLWGPLSLWVVIAFLRQHPLRFILQLVVSVGQIYGDVLYFLTEHRDGFQHGELGHPLYFWFYFVFMNALWLVLPGVLVLDAVKHLTHAQSTLDAKATKAKSKKN 8W0S,8W0R,6OHU,6OHT 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase EBP_HUMAN Q15125 Q6FGL3 Q6IBI9 50829495 CCN(CC)CCO[C@H]1CC[C@@]2([C@H]3CC[C@]4([C@H]([C@@H]3CC=C2C1)CCC4=O)C)C InChI=1S/C25H41NO2/c1-5-26(6-2)15-16-28-19-11-13-24(3)18(17-19)7-8-20-21-9-10-23(27)25(21,4)14-12-22(20)24/h7,19-22H,5-6,8-17H2,1-4H3 DMZCCFMMPHJWQY-UHFFFAOYSA-N 50170651 (3S,8R,9S,10R,13S,14S)-3-(2-Diethylamino-ethoxy)-10,13-dimethyl-1,2,3,4,7,8,9,10,11,12,13,14,15,16-tetradecahydro-cyclopenta[a]phenanthren-17-one::CHEMBL365141 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase Homo sapiens 2 ChEMBL 10.1021/jm049073+ 10.7270/Q2639QHB 16033255 Laggner, C; Schieferer, C; Fiechtner, B; Poles, G; Hoffmann, RD; Glossmann, H; Langer, T; Moebius, FF 7/21/2005 12/3/2012 University of Innsbruck http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50170651 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50001269&target=3-beta-hydroxysteroid-Delta%288%29%2CDelta%287%29-isomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50170651&enzyme=3-beta-hydroxysteroid-Delta%288%29%2CDelta%287%29-isomerase&column=ki&startPg=0&Increment=50&submit=Search MKM 6OHT 9954083 104057031 CHEMBL365141 1 MTTNAGPLHPYWPQHLRLDNFVPNDRPTWHILAGLFSVTGVLVVTTWLLSGRAAVVPLGTWRRLSLCWFAVCGFIHLVIEGWFVLYYEDLLGDQAFLSQLWKEYAKGDSRYILGDNFTVCMETITACLWGPLSLWVVIAFLRQHPLRFILQLVVSVGQIYGDVLYFLTEHRDGFQHGELGHPLYFWFYFVFMNALWLVLPGVLVLDAVKHLTHAQSTLDAKATKAKSKKN 8W0S,8W0R,6OHU,6OHT 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase EBP_HUMAN Q15125 Q6FGL3 Q6IBI9 50829426 CC/C(=C(\c1ccccc1)/c2ccc(cc2)OCCN(C)C)/c3ccccc3 InChI=1S/C26H29NO/c1-4-25(21-11-7-5-8-12-21)26(22-13-9-6-10-14-22)23-15-17-24(18-16-23)28-20-19-27(2)3/h5-18H,4,19-20H2,1-3H3 NKANXQFJJICGDU-UHFFFAOYSA-N 20607 (2-{4-[(1Z)-1,2-diphenylbut-1-en-1-yl]phenoxy}ethyl)dimethylamine::CHEMBL83::cid_2733526::FOSTRIECIN SODIUM::2-{4-[(1Z)-1,2-diphenylbut-1-en-1-yl]phenoxy}-N,N-dimethylethanamine::Tamoxifen, 7::Nolvadex::Tamoxifen::Tamoxifen (8)::NCGC00024928::med.21724, Compound Tamoxifen::US20240217988, Example Tamoxifen 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase Homo sapiens 5 ChEMBL 10.1021/jm049073+ 10.7270/Q2639QHB 16033255 Laggner, C; Schieferer, C; Fiechtner, B; Poles, G; Hoffmann, RD; Glossmann, H; Langer, T; Moebius, FF 7/21/2005 12/3/2012 University of Innsbruck http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=20607 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50001269&target=3-beta-hydroxysteroid-Delta%288%29%2CDelta%287%29-isomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=20607&enzyme=3-beta-hydroxysteroid-Delta%288%29%2CDelta%287%29-isomerase&column=ki&startPg=0&Increment=50&submit=Search CTX 1YA4,6OHU,6SXF 2733526 49688681 CHEMBL83 DB00675 C07108 1 MTTNAGPLHPYWPQHLRLDNFVPNDRPTWHILAGLFSVTGVLVVTTWLLSGRAAVVPLGTWRRLSLCWFAVCGFIHLVIEGWFVLYYEDLLGDQAFLSQLWKEYAKGDSRYILGDNFTVCMETITACLWGPLSLWVVIAFLRQHPLRFILQLVVSVGQIYGDVLYFLTEHRDGFQHGELGHPLYFWFYFVFMNALWLVLPGVLVLDAVKHLTHAQSTLDAKATKAKSKKN 8W0S,8W0R,6OHU,6OHT 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase EBP_HUMAN Q15125 Q6FGL3 Q6IBI9 50031878 CC/C(=C(\c1ccccc1)/c2ccc(cc2)OCCN(C)C)/c3ccccc3 InChI=1S/C26H29NO/c1-4-25(21-11-7-5-8-12-21)26(22-13-9-6-10-14-22)23-15-17-24(18-16-23)28-20-19-27(2)3/h5-18H,4,19-20H2,1-3H3 NKANXQFJJICGDU-UHFFFAOYSA-N 20607 (2-{4-[(1Z)-1,2-diphenylbut-1-en-1-yl]phenoxy}ethyl)dimethylamine::CHEMBL83::cid_2733526::FOSTRIECIN SODIUM::2-{4-[(1Z)-1,2-diphenylbut-1-en-1-yl]phenoxy}-N,N-dimethylethanamine::Tamoxifen, 7::Nolvadex::Tamoxifen::Tamoxifen (8)::NCGC00024928::med.21724, Compound Tamoxifen::US20240217988, Example Tamoxifen 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase/7-dehydrocholesterol reductase Homo sapiens 12 ChEMBL 10.1021/jm00121a035 10.7270/Q28K782T 2909731 Ruenitz, PC; Arrendale, RF; Schmidt, WF; Thompson, CB; Nanavati, NT 2/6/1989 11/10/2009 University of Georgia http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=20607 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000409&target=3-beta-hydroxysteroid-Delta%288%29%2CDelta%287%29-isomerase%2F7-dehydrocholesterol+reductase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=20607&enzyme=3-beta-hydroxysteroid-Delta%288%29%2CDelta%287%29-isomerase%2F7-dehydrocholesterol+reductase&column=ki&startPg=0&Increment=50&submit=Search CTX 1YA4,6OHU,6SXF 2733526 49688681 CHEMBL83 DB00675 C07108 2 MTTNAGPLHPYWPQHLRLDNFVPNDRPTWHILAGLFSVTGVLVVTTWLLSGRAAVVPLGTWRRLSLCWFAVCGFIHLVIEGWFVLYYEDLLGDQAFLSQLWKEYAKGDSRYILGDNFTVCMETITACLWGPLSLWVVIAFLRQHPLRFILQLVVSVGQIYGDVLYFLTEHRDGFQHGELGHPLYFWFYFVFMNALWLVLPGVLVLDAVKHLTHAQSTLDAKATKAKSKKN 8W0S,8W0R,6OHU,6OHT 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase EBP_HUMAN Q15125 Q6FGL3 Q6IBI9 MAAKSQPNIPKAKSLDGVTNDRTASQGQWGRAWEVDWFSLASVIFLLLFAPFIVYYFIMACDQYSCALTGPVVDIVTGHARLSDIWAKTPPITRKAAQLYTLWVTFQVLLYTSLPDFCHKFLPGYVGGIQEGAVTPAGVVNKYQINGLQAWLLTHLLWFANAHLLSWFSPTIIFDNWIPLLWCANILGYAVSTFAMVKGYFFPTSARDCKFTGNFFYNYMMGIEFNPRIGKWFDFKLFFNGRPGIVAWTLINLSFAAKQRELHSHVTNAMVLVNVLQAIYVIDFFWNETWYLKTIDICHDHFGWYLGWGDCVWLPYLYTLQGLYLVYHPVQLSTPHAVGVLLLGLVGYYIFRVANHQKDLFRRTDGRCLIWGRKPKVIECSYTSADGQRHHSKLLVSGFWGVARHFNYVGDLMGSLAYCLACGGGHLLPYFYIIYMAILLTHRCLRDEHRCASKYGRDWERYTAAVPYRLLPGIF 7-dehydrocholesterol reductase DHCR7_HUMAN Q9UBM7 B2R6Z2 O60492 O60717 7-dehydrocholesterol reductase A0A024R5F7_HUMAN A0A024R5F7 51587401 CN1c2ccc(cc2C(=O)C13CCN(CC3)CC4CCOCC4)C(F)(F)F InChI=1S/C20H25F3N2O2/c1-24-17-3-2-15(20(21,22)23)12-16(17)18(26)19(24)6-8-25(9-7-19)13-14-4-10-27-11-5-14/h2-3,12,14H,4-11,13H2,1H3 CEQWEVQYPPXCIW-UHFFFAOYSA-N 50639123 CHEMBL4636197 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase Homo sapiens 11 ChEMBL 10.7270/Q26H4P1W 38470227 Dorel, R; Sun, D; Carruthers, N; Castanedo, GM; Ung, PM; Factor, DC; Li, T; Baumann, H; Janota, D; Pang, J; Salphati, L; Meklemburg, R; Korman, AJ; Harper, HE; Stubblefield, S; Payandeh, J; McHugh, D; Lang, BT; Tesar, PJ; Dere, E; Masureel, M; Adams, DJ; Volgraf, M; Braun, MG //0 10/11/2025 Genentech http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50639123 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50001269&target=3-beta-hydroxysteroid-Delta%288%29%2CDelta%287%29-isomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50639123&enzyme=3-beta-hydroxysteroid-Delta%288%29%2CDelta%287%29-isomerase&column=ki&startPg=0&Increment=50&submit=Search A1AEU 8W0R 156013691 519659526 1 MTTNAGPLHPYWPQHLRLDNFVPNDRPTWHILAGLFSVTGVLVVTTWLLSGRAAVVPLGTWRRLSLCWFAVCGFIHLVIEGWFVLYYEDLLGDQAFLSQLWKEYAKGDSRYILGDNFTVCMETITACLWGPLSLWVVIAFLRQHPLRFILQLVVSVGQIYGDVLYFLTEHRDGFQHGELGHPLYFWFYFVFMNALWLVLPGVLVLDAVKHLTHAQSTLDAKATKAKSKKN 8W0S,8W0R,6OHU,6OHT 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase EBP_HUMAN Q15125 Q6FGL3 Q6IBI9 51587420 CN1c2ccc(cc2C(=O)C13CCN(CC3)CC4CCOCC4)C(F)(F)F InChI=1S/C20H25F3N2O2/c1-24-17-3-2-15(20(21,22)23)12-16(17)18(26)19(24)6-8-25(9-7-19)13-14-4-10-27-11-5-14/h2-3,12,14H,4-11,13H2,1H3 CEQWEVQYPPXCIW-UHFFFAOYSA-N 50639123 CHEMBL4636197 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase Homo sapiens 33 ChEMBL 10.7270/Q26H4P1W 38470227 Dorel, R; Sun, D; Carruthers, N; Castanedo, GM; Ung, PM; Factor, DC; Li, T; Baumann, H; Janota, D; Pang, J; Salphati, L; Meklemburg, R; Korman, AJ; Harper, HE; Stubblefield, S; Payandeh, J; McHugh, D; Lang, BT; Tesar, PJ; Dere, E; Masureel, M; Adams, DJ; Volgraf, M; Braun, MG //0 10/11/2025 Genentech http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50639123 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50001269&target=3-beta-hydroxysteroid-Delta%288%29%2CDelta%287%29-isomerase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50639123&enzyme=3-beta-hydroxysteroid-Delta%288%29%2CDelta%287%29-isomerase&column=ki&startPg=0&Increment=50&submit=Search A1AEU 8W0R 156013691 519659526 1 MTTNAGPLHPYWPQHLRLDNFVPNDRPTWHILAGLFSVTGVLVVTTWLLSGRAAVVPLGTWRRLSLCWFAVCGFIHLVIEGWFVLYYEDLLGDQAFLSQLWKEYAKGDSRYILGDNFTVCMETITACLWGPLSLWVVIAFLRQHPLRFILQLVVSVGQIYGDVLYFLTEHRDGFQHGELGHPLYFWFYFVFMNALWLVLPGVLVLDAVKHLTHAQSTLDAKATKAKSKKN 8W0S,8W0R,6OHU,6OHT 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase EBP_HUMAN Q15125 Q6FGL3 Q6IBI9 50337880 C(C(=O)O)C(CC(=O)O)(C(=O)O)O InChI=1S/C6H8O7/c7-3(8)1-6(13,5(11)12)2-4(9)10/h13H,1-2H2,(H,7,8)(H,9,10)(H,11,12) KRKNYBCHXYNGOX-UHFFFAOYSA-N 14672 cid_311::CITRIC ACID::2-hydroxypropane-1,2,3-tricarboxylic acid::Fragment 2::Citrate::CHEMBL1261::Citric Acid 3-dehydroquinate dehydratase Helicobacter pylori (strain ATCC 700392 / 26695) 2500 ChEMBL 10.1021/jm0505361 10.7270/Q27P8XZF 16480265 Robinson, DA; Stewart, KA; Price, NC; Chalk, PA; Coggins, JR; Lapthorn, AJ 2/16/2006 11/10/2009 University of Glasgow http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=14672 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003406&target=3-dehydroquinate+dehydratase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=14672&enzyme=3-dehydroquinate+dehydratase&column=ki&startPg=0&Increment=50&submit=Search CIT 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311 46515004 CHEMBL1261 C17263 1 MKILVIQGPNLNMLGHRDPRLYGMVTLDQIHEIMQTFVKQGNLDVELEFFQTNFEGEIIDKIQESVGSDYEGIIINPGAFSHTSIAIADAIMLAGKPVIEVHLTNIQAREEFRKNSYTGAACGGVIMGFGPLGYNMALMAMVNILAEMKAFQEAQKNNPNNPINNQK 2C57,4B6S,4B6R,2XDA,2XD9,2XB9,2WKS,2C4V,1J2Y 3-dehydroquinate dehydratase AROQ_HELPY Q48255 50337880 C(C(=O)O)C(CC(=O)O)(C(=O)O)O InChI=1S/C6H8O7/c7-3(8)1-6(13,5(11)12)2-4(9)10/h13H,1-2H2,(H,7,8)(H,9,10)(H,11,12) KRKNYBCHXYNGOX-UHFFFAOYSA-N 14672 cid_311::CITRIC ACID::2-hydroxypropane-1,2,3-tricarboxylic acid::Fragment 2::Citrate::CHEMBL1261::Citric Acid 3-dehydroquinate dehydratase Helicobacter pylori (strain ATCC 700392 / 26695) 2500 ChEMBL 10.1021/jm0505361 10.7270/Q27P8XZF 16480265 Robinson, DA; Stewart, KA; Price, NC; Chalk, PA; Coggins, JR; Lapthorn, AJ 2/16/2006 11/10/2009 University of Glasgow http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=14672 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003406&target=3-dehydroquinate+dehydratase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=14672&enzyme=3-dehydroquinate+dehydratase&column=ki&startPg=0&Increment=50&submit=Search CIT 10QF,1A59,1AFL,1AGR,1AJ8,1AZ2,1B1E,1B1I,1CTS,1CWV,1CXU,1CZ9,1D3B,1DMG,1DVP,1DYT,1E5K,1EAZ,1EKJ,1EMD,1EQD,1ERX,1F8R,1FQ0,1FUO,1FUQ,1FWR,1G1L,1GCZ,1GD0,1GI7,1GI8,1GI9,1GJ7,1GJ8,1GJ9,1GJA,1GJB,1GJC,1GJD,1GO6,1GPJ,1GPM,1GV7,1GVE,1H1L,1H4C,1H4D,1H4E,1H53,1HHC,1HHU,1HJJ,1HJL,1HQS,1HTO,1HTQ,1I2S,1I4K,1IXE,1J3N,1JCH,1JEO,1K4M,1K59,1K5B,1KMP,1KQ7,1KWM,1KXG,1L8D,1LF7,1LT7,1LT8,1M0S,1MAU,1MK0,1MLD,1MQO,1MRZ,1NML,1O3P,1O4L,1O5A,1O5B,1O5C,1OCY,1P2Z,1PCA,1PQ8,1Q0H,1QB7,1QB8,1QCC,1QMH,1R74,1RE0,1RE5,1REO,1RPQ,1RQ2,1RZ6,1SMK,1SS4,1T8T,1T9R,1T9Z,1TA0,1TET,1TF0,1TM1,1TM3,1TM4,1TM5,1TM7,1TMG,1TO1,1TO2,1TZX,1U11,1U6T,1UEJ,1UJP,1ULT,1UN4,1UN5,1US0,1UYP,1UZR,1V7R,1VBJ,1VKF,1VL1,1VMA,1W2T,1W8O,1WDI,1X96,1X98,1X9J,1XE8,1XF1,1XJB,1XJT,1XT3,1XVY,1Y1K,1Y33,1Y34,1Y3B,1Y3C,1Y3D,1Y3F,1Y48,1Y4A,1YFK,1YJX,1YKI,1YUL,1YUM,1YY7,1Z1E,1Z1F,1Z7X,1Z9T,1ZC2,1ZEA,1ZPD,1ZX4,28WB,2A6C,2ACS,2ACU,2AEX,2AGK,2AGT,2AL0,2ANG,2ASF,2AZT,2B5U,2BS3,2BS4,2C4V,2C6X,2C6Z,2C74,2C7P,2C7Q,2CAD,2CI1,2CI5,2CMD,2CSG,2CTS,2CZ5,2CZE,2CZQ,2D1C,2DC1,2DDF,2DTJ,2DX7,2EAA,2F2L,2F6U,2FQD,2FQE,2FQF,2FQG,2FUS,2FW0,2FW6,2FWP,2G88,2GBB,2GC9,2HAU,2HAV,2HD9,2HI9,2HJ0,2HJR,2I16,2I17,2I29,2I2B,2I2D,2I54,2I7F,2IL2,2IS5,2O2D,2OAF,2OKL,2OT4,2OWZ,2P3L,2P3O,2P41,2P6Z,2P7K,2P8I,2P9E,2PEV,2PF8,2PFH,2PG4,2PQF,2Q1X,2Q2H,2Q4G,2Q83,2QE9,2QEU,2QIK,2QL5,2QL7,2QL9,2QLB,2QLJ,2QPQ,2QVR,2QXW,2R2V,2R4I,2RDG,2RIJ,2V03,2V9M,2V9N,2VEK,2VEN,2VN8,2VNS,2VOH,2VQ3,2VUV,2VXY,2W03,2WC8,2WCQ,2WGV,2WK0,2WRS,2WVE,2X7I,2XB9,2XCU,2XIG,2XU2,2Y1P,2Y6K,2Y91,2Z02,2Z6W,2Z92,2ZNH,2ZQM,2ZWA,2ZZJ,2ZZK,3A56,3ALP,3B0C,3B0D,3B2Q,3BB5,3BCJ,3BDL,3BHD,3BJK,3BM3,3BSW,3BX9,3BXA,3BZM,3C5A,3C8D,3C8W,3C9H,3CBW,3CGG,3CH0,3CKJ,3CSW,3CTS,3CWM,3DAO,3DGE,3DRN,3E2R,3E4F,3E8R,3EDZ,3EJK,3ELG,3F2E,3F7C,3FRY,3G68,3GFT,3GHF,3GHR,3GHS,3GHT,3GHU,3GM5,3GNI,3GVE,3GZ7,3H4Y,3H55,3H97,3H99,3H9B,3H9C,3HBA,3HCH,3HH2,3HVS,3I09,3I43,3ITC,3ITJ,3JVU,3JVV,3K1L,3K49,3K6V,3KGQ,3KN3,3KX6,3L57,3L6T,3LB0,3LBO,3LD5,3LEP,3LFK,3LIF,3LMZ,3LQL,3LY1,3LZ3,3LZ5,3M4H,3M9Y,3MA8,3MFD,3MLP,3MMX,3MRG,3MWD,3MXU,3N27,3N3H,3N7Q,3NAT,3NNB,3NO2,3NOR,3NR3,3NUA,3OBH,3ODV,3OKW,3OM2,3ONB,3ONC,3OQ2,3P4E,3P6C,3P6L,3P98,3PG6,3PGY,3PKO,3PL2,3PMA,3PP2,3PPA,3PZN,3Q6K,3Q6P,3Q6T,3QAE,3QLB,3QNQ,3QSL,3QU2,3R12,3R69,3R7T,3RCM,3RJU,3RQI,3RXW,3RZA,3S64,3S6E,3S9K,3SBL,3SFP,3SK3,3SOI,3SOR,3SOS,3T42,3TB5,3TZT,3U02,3U1K,3U2C,3U2G,3U3L,3U3N,3U3U,3UWU,3V2I,3V7Q,3V7U,3V7W,3V7Y,3V80,3V85,3V8H,3V8M,3V8N,3V8P,3V8Q,3V8R,3VPD,3VYR,3WAM,3WCZ,3WL5,3WL6,3WL7,3WL8,3WN0,3WN1,3WN2,3WND,3WSF,3WSG,3WUZ,3WWC,3WWD,3WWP,3ZN4,4A2Y,4A3R,4A44,4A5R,4ACI,4AF5,4AIZ,4ANE,4AXD,4BGV,4BM1,4BVM,4BZE,4BZF,4BZG,4BZH,4BZQ,4BZX,4C2Y,4C2Z,4C8I,4CFP,4CMV,4CMW,4CNM,4CNN,4CON,4CSW,4D6A,4DA4,4DJH,4DO4,4DO5,4DO6,4DY6,4E1H,4EEL,4EF3,4ESW,4EU3,4EU7,4EUD,4F35,4F40,4F9O,4FDI,4FIN,4FOE,4FOI,4FPA,4FPB,4G5O,4G5Q,4G5R,4G5S,4GP7,4GPS,4GSJ,4GYP,4H0C,4H1X,4HAS,4HFV,4HG9,4HK8,4I4K,4I6K,4IL0,4IUW,4IVF,4J6O,4JBD,4JCA,4JGX,4JP3,4JPH,4JZ8,4JZ9,4K0W,4K3D,4K7G,4K8O,4KAE,4KAX,4KDY,4KL5,4KNN,4KYS,4L9M,4LC3,4LIK,4LKT,4LQB,4MDF,4MEV,4MH2,4MH3,4MHQ,4MKZ,4MM2,4MP6,4N18,4N3V,4N7C,4N7D,4N7W,4NX0,4NXK,4NZF,4O61,4O87,4O89,4OE9,4OI6,4OIK,4OLC,4OVY,4OWZ,4OXF,4PUW,4PUX,4PW2,4Q0T,4Q14,4Q17,4Q1O,4QBX,4QD4,4QJP,4QLC,4QNI,4QSJ,4QTP,4R03,4R29,4RGD,4RPF,4RU1,4RXU,4TWG,4U2A,4U31,4U36,4U3E,4UHQ,4UMD,4W6U,4WBD,4WCA,4WDD,4WGK,4WHN,4WLE,4WPK,4WRY,4WRZ,4WS2,4WS4,4WS6,4WUA,4WUI,4WXB,4X3N,4X3S,4X5V,4X6P,4XES,4XFR,4XG0,4XTM,4XTP,4XUZ,4Y03,4YGS,4YHC,4YPM,4YYY,4Z6A,4ZBE,4ZBL,4ZJB,4ZM1,4ZVE,5A1P,5A3L,5A3M,5A56,5A57,5A58,5A59,5A5A,5A8J,5A9I,5AE0,5AFE,5AWV,5B3R,5B3W,5BO8,5BQB,5BYG,5CIK,5CLG,5CLJ,5CLS,5COL,5CR4,5CUY,5CVT,5D77,5DB5,5DFT,5DHP,5DHQ,5DHR,5DHS,5DHT,5DHU,5DQN,5DWK,5DYH,5E2N,5E8E,5EFI,5EJI,5EOE,5EOG,5EOM,5EOO,5FAI,5FT4,5FYJ,5G2U,5GGE,5GK6,5GN0,5GO2,5GPQ,5GRE,5GRF,5GRI,5GUD,5H16,5H52,5H7X,5HDN,5II2,5IIK,5IIL,5IR0,5IXD,5J72,5JOC,5JOQ,5JOS,5K2O,5K5D,5KLP,5KLQ,5KV8,5L6Z,5LDH,5LGW,5LLA,5LLN,5LR8,5M2H,5MA5,5MAK,5MEJ,5MEW,5MHU,5MHV,5MHW,5MHX,5MHY,5MHZ,5MI1,5MI2,5MIA,5MIB,5MIC,5MID,5MIE,5MIG,5MLQ,5MSA,5MY8,5NC9,5NCD,5NE6,5NE7,5NEL,5NFF,5NFR,5NHX,5NIJ,5NKP,5NTG,5NVJ,5NXI,5O9A,5O9H,5OCO,5OCQ,5OCS,5OEY,5OGJ 311 46515004 CHEMBL1261 C17263 1 MKILVIQGPNLNMLGHRDPRLYGMVTLDQIHEIMQTFVKQGNLDVELEFFQTNFEGEIIDKIQESVGSDYEGIIINPGAFSHTSIAIADAIMLAGKPVIEVHLTNIQAREEFRKNSYTGAACGGVIMGFGPLGYNMALMAMVNILAEMKAFQEAQKNNPNNPINNQK 2C57,4B6S,4B6R,2XDA,2XD9,2XB9,2WKS,2C4V,1J2Y 3-dehydroquinate dehydratase AROQ_HELPY Q48255 51461538 CNC(=O)[C@H](CCc1ccccc1)NC(=O)[C@@H](c2cccs2)NC(=O)CNCc3ccc(cc3OC)OC InChI=1S/C28H34N4O5S/c1-29-27(34)22(14-11-19-8-5-4-6-9-19)31-28(35)26(24-10-7-15-38-24)32-25(33)18-30-17-20-12-13-21(36-2)16-23(20)37-3/h4-10,12-13,15-16,22,26,30H,11,14,17-18H2,1-3H3,(H,29,34)(H,31,35)(H,32,33) TUQBDKJHGPFTTD-UHFFFAOYSA-N 50589801 CHEMBL5208789 Glucose-induced degradation protein 4 homolog Homo sapiens 5400 ChEMBL 10.7270/Q2JD51RW 36117290 Chana, CK; Maisonneuve, P; Posternak, G; Grinberg, NGA; Poirson, J; Ona, SM; Ceccarelli, DF; Mader, P; St-Cyr, DJ; Pau, V; Kurinov, I; Tang, X; Deng, D; Cui, W; Su, W; Kuai, L; Soll, R; Tyers, M; Röst, HL; Batey, RA; Taipale, M; Gingras, AC; Sicheri, F 10/13/2022 6/18/2023 Lunenfeld-Tanenbaum Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50589801 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50001177&target=Glucose-induced+degradation+protein+4+homolog&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50589801&enzyme=Glucose-induced+degradation+protein+4+homolog&column=ki&startPg=0&Increment=50&submit=Search L6U 7U3J 165180701 482600653 1 MCARGQVGRGTQLRTGRPCSQVPGSRWRPERLLRRQRAGGRPSRPHPARARPGLSLPATLLGSRAAAAVPLPLPPALAPGDPAMPVRTECPPPAGASAASAASLIPPPPINTQQPGVATSLLYSGSKFRGHQKSKGNSYDVEVVLQHVDTGNSYLCGYLKIKGLTEEYPTLTTFFEGEIISKKHPFLTRKWDADEDVDRKHWGKFLAFYQYAKSFNSDDFDYEELKNGDYVFMRWKEQFLVPDHTIKDISGASFAGFYYICFQKSAASIEGYYYHRSSEWYQSLNLTHVPEHSAPIYEFR 7NSC,7Q4Y,6CCU,6CCR,7Q50,8V1P,8X7H,8X7G,7U3L,7U3K,7U3J,7U3I,7U3H,7U3G,7U3F,7U3E,7SLZ,6WZZ,6WZX,6CDG,6CDC,6CD9,6CD8,6CCT Glucose-induced degradation protein 4 homolog GID4_HUMAN Q8IVV7 Q8TEB5 Q9BW50 377286 C/C(=C\[C@@]1(C(=C(C(=O)S1)CCCCN=[N+]=[N-])O)C)/C=C InChI=1S/C14H19N3O2S/c1-4-10(2)9-14(3)12(18)11(13(19)20-14)7-5-6-8-16-17-15/h4,9,18H,1,5-8H2,2-3H3 YWCFDTCBMVZYIG-UHFFFAOYSA-N 214777 TLM18 3-oxoacyl-[acyl-carrier-protein] synthase 1 Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) 1.120e+5 8.5000 Curated from the literature by BindingDB 10.1074/jbc.M113.511436 10.7270/Q22F7M8D 24108128 aid1802452 Schiebel, J; Kapilashrami, K; Fekete, A; Bommineni, GR; Schaefer, CM; Mueller, MJ; Tonge, PJ; Kisker, C 11/22/2013 3/1/2017 University of Wuerzburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=214777 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5359&target=3-oxoacyl-%5Bacyl-carrier-protein%5D+synthase+1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=214777&enzyme=3-oxoacyl-%5Bacyl-carrier-protein%5D+synthase+1&column=ki&startPg=0&Increment=50&submit=Search 7RD 4C71 78225991 329965654 1 MSQPSTANGGFPSVVVTAVTATTSISPDIESTWKGLLAGESGIHALEDEFVTKWDLAVKIGGHLKDPVDSHMGRLDMRRMSYVQRMGKLLGGQLWESAGSPEVDPDRFAVVVGTGLGGAERIVESYDLMNAGGPRKVSPLAVQMIMPNGAAAVIGLQLGARAGVMTPVSACSSGSEAIAHAWRQIVMGDADVAVCGGVEGPIEALPIAAFSMMRAMSTRNDEPERASRPFDKDRDGFVFGEAGALMLIETEEHAKARGAKPLARLLGAGITSDAFHMVAPAADGVRAGRAMTRSLELAGLSPADIDHVNAHGTATPIGDAAEANAIRVAGCDQAAVYAPKSALGHSIGAVGALESVLTVLTLRDGVIPPTLNYETPDPEIDLDVVAGEPRYGDYRYAVNNSFGFGGHNVALAFGRY 4C6V,4C6U,2WGE,2WGD,6Y2J,6Y2I,5LD8,6P9M,6P9L,6P9K 3-oxoacyl-[acyl-carrier-protein] synthase 1 KASA_MYCTU P9WQD9 L0T991 P63454 Q10524 377287 C/C(=C\[C@@]1(C(=C(C(=O)S1)CCCCN=[N+]=[N-])O)C)/C=C InChI=1S/C14H19N3O2S/c1-4-10(2)9-14(3)12(18)11(13(19)20-14)7-5-6-8-16-17-15/h4,9,18H,1,5-8H2,2-3H3 YWCFDTCBMVZYIG-UHFFFAOYSA-N 214777 TLM18 3-oxoacyl-[acyl-carrier-protein] synthase 1 [C171Q] Mycobacterium tuberculosis 3.840e+5 8.5000 Curated from the literature by BindingDB 10.1074/jbc.M113.511436 10.7270/Q22F7M8D 24108128 aid1802452 Schiebel, J; Kapilashrami, K; Fekete, A; Bommineni, GR; Schaefer, CM; Mueller, MJ; Tonge, PJ; Kisker, C 11/22/2013 3/1/2017 University of Wuerzburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=214777 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=9066&target=3-oxoacyl-%5Bacyl-carrier-protein%5D+synthase+1+%5BC171Q%5D&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=214777&enzyme=3-oxoacyl-%5Bacyl-carrier-protein%5D+synthase+1+%5BC171Q%5D&column=ki&startPg=0&Increment=50&submit=Search 7RD 4C71 78225991 329965654 1 MSQPSTANGGFPSVVVTAVTATTSISPDIESTWKGLLAGESGIHALEDEFVTKWDLAVKIGGHLKDPVDSHMGRLDMRRMSYVQRMGKLLGGQLWESAGSPEVDPDRFAVVVGTGLGGAERIVESYDLMNAGGPRKVSPLAVQMIMPNGAAAVIGLQLGARAGVMTPVSAQSSGSEAIAHAWRQIVMGDADVAVCGGVEGPIEALPIAAFSMMRAMSTRNDEPERASRPFDKDRDGFVFGEAGALMLIETEEHAKARGAKPLARLLGAGITSDAFHMVAPAADGVRAGRAMTRSLELAGLSPADIDHVNAHGTATPIGDAAEANAIRVAGCDQAAVYAPKSALGHSIGAVGALESVLTVLTLRDGVIPPTLNYETPDPEIDLDVVAGEPRYGDYRYAVNNSFGFGGHNVALAFGRY 4C73,4C72,4C71,4C70,4C6Z,4C6X,4C6W,2WGG,2WGF,5W2S,5W2Q,5W2P,5W2O,6Y2J,6Y2I,5LD8 3-oxoacyl-[acyl-carrier-protein] synthase 1 KASA_MYCTO P9WQD8 L0T991 P63454 Q10524 42821 CCN(CC)S(=O)(=O)c1cc(ccc1Br)C(=O)Nc2ccccc2C(=O)O InChI=1S/C18H19BrN2O5S/c1-3-21(4-2)27(25,26)16-11-12(9-10-14(16)19)17(22)20-15-8-6-5-7-13(15)18(23)24/h5-11H,3-4H2,1-2H3,(H,20,22)(H,23,24) VNOMZKMKBNFCMC-UHFFFAOYSA-N 23570 2-{[4-bromo-3-(diethylsulfamoyl)benzene]amido}benzoic acid::Diethylsulfonamide Derivative, 13a 3-oxoacyl-[acyl-carrier-protein] synthase 3 Enterococcus faecalis (strain ATCC 700802 / V583) 1600 7.0000 22.00 C Curated from the literature by BindingDB 10.1021/jm049141s 10.7270/Q22B8W9H 15743201 aid1798342 Nie, Z; Perretta, C; Lu, J; Su, Y; Margosiak, S; Gajiwala, KS; Cortez, J; Nikulin, V; Yager, KM; Appelt, K; Chu, S 3/10/2005 7/24/2008 Quorex Pharmaceuticals http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=23570 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2417&target=3-oxoacyl-%5Bacyl-carrier-protein%5D+synthase+3&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=23570&enzyme=3-oxoacyl-%5Bacyl-carrier-protein%5D+synthase+3&column=ki&startPg=0&Increment=50&submit=Search B82 1121782 50091831 DB07429 1 MKNYARISCTSRYVPENCVTNHQLSEMMDTSDEWIHSRTGISERRIVTQENTSDLCHQVAKQLLEKSGKQASEIDFILVATVTPDFNMPSVACQVQGAIGATEAFAFDISAACSGFVYALSMAEKLVLSGRYQTGLVIGGETFSKMLDWTDRSTAVLFGDGAAGVLIEAAETPHFLNEKLQADGQRWAALTSGYTINESPFYQGHKQASKTLQMEGRSIFDFAIKDVSQNILSLVTDETVDYLLLHQANVRIIDKIARKTKISREKFLTNMDKYGNTSAASIPILLDEAVENGTLILGSQQRVVLTGFGGGLTWGSLLLTL 3IL5 Beta-ketoacyl-[acyl-carrier-protein] synthase III FABH_ENTFA Q820T1 51007057 CCN(CC)S(=O)(=O)c1cc(ccc1Br)C(=O)Nc2ccccc2C(=O)O InChI=1S/C18H19BrN2O5S/c1-3-21(4-2)27(25,26)16-11-12(9-10-14(16)19)17(22)20-15-8-6-5-7-13(15)18(23)24/h5-11H,3-4H2,1-2H3,(H,20,22)(H,23,24) VNOMZKMKBNFCMC-UHFFFAOYSA-N 23570 2-{[4-bromo-3-(diethylsulfamoyl)benzene]amido}benzoic acid::Diethylsulfonamide Derivative, 13a 3-oxoacyl-[acyl-carrier-protein] synthase 3 Enterococcus faecalis (strain ATCC 700802 / V583) 1600 ChEMBL 10.1016/j.ejmech.2007.06.018 10.7270/Q2GQ700V 17707951 Singh, S; Soni, LK; Gupta, MK; Prabhakar, YS; Kaskhedikar, SG 5/9/2008 5/21/2013 Shri G.S. Institute of Technology and Science http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=23570 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2417&target=3-oxoacyl-%5Bacyl-carrier-protein%5D+synthase+3&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=23570&enzyme=3-oxoacyl-%5Bacyl-carrier-protein%5D+synthase+3&column=ki&startPg=0&Increment=50&submit=Search B82 3IL5 1121782 50091831 DB07429 1 MKNYARISCTSRYVPENCVTNHQLSEMMDTSDEWIHSRTGISERRIVTQENTSDLCHQVAKQLLEKSGKQASEIDFILVATVTPDFNMPSVACQVQGAIGATEAFAFDISAACSGFVYALSMAEKLVLSGRYQTGLVIGGETFSKMLDWTDRSTAVLFGDGAAGVLIEAAETPHFLNEKLQADGQRWAALTSGYTINESPFYQGHKQASKTLQMEGRSIFDFAIKDVSQNILSLVTDETVDYLLLHQANVRIIDKIARKTKISREKFLTNMDKYGNTSAASIPILLDEAVENGTLILGSQQRVVLTGFGGGLTWGSLLLTL 3IL5 Beta-ketoacyl-[acyl-carrier-protein] synthase III FABH_ENTFA Q820T1 51629000 C[C@@]12[C@@H]([C@@H](C[C@@H](O1)n3c4ccccc4c5c3c6n2c7ccccc7c6c8c5C(=O)NC8)NC)OC InChI=1S/C28H26N4O3/c1-28-26(34-3)17(29-2)12-20(35-28)31-18-10-6-4-8-14(18)22-23-16(13-30-27(23)33)21-15-9-5-7-11-19(15)32(28)25(21)24(22)31/h4-11,17,20,26,29H,12-13H2,1-3H3,(H,30,33) HKSZLNNOFSGOKW-UHFFFAOYSA-N 130909 US8822500, Stauro- sporine::US9920060, Staurosporine::US10683289, Example Staurosporine::US10927120, Compound staurosporine 3-phosphoinositide-dependent protein kinase 1 Homo sapiens 5.6 ChEMBL 10.7270/Q2KS6X8V 27784673 Deng, C; Lipstein, MR; Scotto, L; Jirau Serrano, XO; Mangone, MA; Li, S; Vendome, J; Hao, Y; Xu, X; Deng, SX; Realubit, RB; Tatonetti, NP; Karan, C; Lentzsch, S; Fruman, DA; Honig, B; Landry, DW; O'Connor, OA //0 10/13/2025 Center for Lymphoid Malignancies http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=130909 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1744&target=3-phosphoinositide-dependent+protein+kinase+1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=130909&enzyme=3-phosphoinositide-dependent+protein+kinase+1&column=ki&startPg=0&Increment=50&submit=Search STU 1AQ1,1BYG,1E8Z,1NVR,1NXK,1OKY,1Q3D,1QPD,1QPJ,1SM2,1SNU,1STC,1U59,1WVY,1XBC,1XJD,1YHS,2BUJ,2CLQ,2DQ7,2GCD,2HW7,2NRY,2OIC,2PZY,2YN8,2Z7R,3A4O,3A60,3A61,3A62,3BKB,3CBL,3CD3,3CKX,3D7T,3FME,3HMO,3LCS,3P86,3PPZ,3S95,3ZEW,4BF2,4C34,4CFE,4CFF,4CFH,4ERW,4EZ7,4FR4,4MVF,4QFG,4QFR,4QFS,4QMY,4RER,4REW,4RLO,4U97,4U9A,4YZC,5E8W,5E8X,5E8Y,5EZV,5ISO,5KQ5,5LOH,5NG2,5OOR,5T5T,5UFU,5VED,5WNL,6B1U,6B2E,6C9F,6C9G,6C9H,6C9J,6E4T,6E4U,6E4W,7AKO,7NVQ,8BIK,8E4T,8JPB,8JPC,8JPD,8S19,9DAI 5279 225157243 1 MARTTSQLYDAVPIQSSVVLCSCPSPSMVRTQTESSTPPGIPGGSRQGPAMDGTAAEPRPGAGSLQHAQPPPQPRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILEKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKLYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSALEYLHGKGIIHRDLKPENILLNEDMHIQITDFGTAKVLSPESKQARANSFVGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPFRAGNEYLIFQKIIKLEYDFPEKFFPKARDLVEKLLVLDATKRLGCEEMEGYGPLKAHPFFESVTWENLHQQTPPKLTAYLPAMSEDDEDCYGNYDNLLSQFGCMQVSSSSSSHSLSASDTGLPQRSGSNIEQYIHDLDSNSFELDLQFSEDEKRLLLEKQAGGNPWHQFVENNLILKMGPVDKRKGLFARRRQLLLTEGPHLYYVDPVNKVLKGEIPWSQELRPEAKNFKTFFVHTPNRTYYLMDPSGNAHKWCRKIQEVWRQRYQSHPDAAVQ 3QD4,3QD3,3QD0,3QCY,3QCX,3QCS,3QCQ,3IOP,3ION,2R7B,1UU8,1UU7,1UU3,1OKZ,1OKY,3SC1,3RWQ,3RWP,5HO8,5HO7,5HNG,5HKM,2XCH,3H9O,3NAY,3NAX,3NUN,1UVR,1H1W,1UU9,3NUY,3NUU,3NUS,2PE2,2PE1,2PE0,1Z5M,1W1H,1W1G,1W1D 3-phosphoinositide-dependent protein kinase 1 PDPK1_HUMAN O15530 H0Y4Z0 Q59EH6 Q6FI20 Q8IV52 Q9BRD5 30755 CC(C)(C(=O)N)C(=O)NCCCNc1c(cnc(n1)Nc2cccc(c2)NC(=O)N3CCCC3)Br InChI=1S/C23H31BrN8O3/c1-23(2,19(25)33)20(34)27-10-6-9-26-18-17(24)14-28-21(31-18)29-15-7-5-8-16(13-15)30-22(35)32-11-3-4-12-32/h5,7-8,13-14H,3-4,6,9-12H2,1-2H3,(H2,25,33)(H,27,34)(H,30,35)(H2,26,28,29,31) ZNSULAZTNWFKEW-UHFFFAOYSA-N 17053 N-(3-{[5-bromo-2-({3-[(pyrrolidin-1-ylcarbonyl)amino]phenyl}amino)pyrimidin-4-yl]amino}propyl)-2,2-dimethylpropanediamide::N-{3-[(5-bromo-2-{[3-(pyrrolidin-1-ylcarbonylamino)phenyl]amino}pyrimidin-4-yl)amino]propyl}-2,2-dimethylpropanediamide::BX-320 3-phosphoinositide-dependent protein kinase 1 Homo sapiens 39 7.2000 22.00 C Curated from the literature by BindingDB 10.1074/jbc.M501367200 10.7270/Q21Z42PW 15772071 aid1797580 Feldman, RI; Wu, JM; Polokoff, MA; Kochanny, MJ; Dinter, H; Zhu, D; Biroc, SL; Alicke, B; Bryant, J; Yuan, S; Buckman, BO; Lentz, D; Ferrer, M; Whitlow, M; Adler, M; Finster, S; Chang, Z; Arnaiz, DO 5/20/2005 8/2/2007 Berlex Biosciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=17053 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1744&target=3-phosphoinositide-dependent+protein+kinase+1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=17053&enzyme=3-phosphoinositide-dependent+protein+kinase+1&column=ki&startPg=0&Increment=50&submit=Search LI8 1Z5M 657138 46517283 1 MARTTSQLYDAVPIQSSVVLCSCPSPSMVRTQTESSTPPGIPGGSRQGPAMDGTAAEPRPGAGSLQHAQPPPQPRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILEKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKLYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSALEYLHGKGIIHRDLKPENILLNEDMHIQITDFGTAKVLSPESKQARANSFVGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPFRAGNEYLIFQKIIKLEYDFPEKFFPKARDLVEKLLVLDATKRLGCEEMEGYGPLKAHPFFESVTWENLHQQTPPKLTAYLPAMSEDDEDCYGNYDNLLSQFGCMQVSSSSSSHSLSASDTGLPQRSGSNIEQYIHDLDSNSFELDLQFSEDEKRLLLEKQAGGNPWHQFVENNLILKMGPVDKRKGLFARRRQLLLTEGPHLYYVDPVNKVLKGEIPWSQELRPEAKNFKTFFVHTPNRTYYLMDPSGNAHKWCRKIQEVWRQRYQSHPDAAVQ 3QD4,3QD3,3QD0,3QCY,3QCX,3QCS,3QCQ,3IOP,3ION,2R7B,1UU8,1UU7,1UU3,1OKZ,1OKY,3SC1,3RWQ,3RWP,5HO8,5HO7,5HNG,5HKM,2XCH,3H9O,3NAY,3NAX,3NUN,1UVR,1H1W,1UU9,3NUY,3NUU,3NUS,2PE2,2PE1,2PE0,1Z5M,1W1H,1W1G,1W1D 3-phosphoinositide-dependent protein kinase 1 PDPK1_HUMAN O15530 H0Y4Z0 Q59EH6 Q6FI20 Q8IV52 Q9BRD5 50500616 CC(C)(C(=O)N)C(=O)NCCCNc1c(cnc(n1)Nc2cccc(c2)NC(=O)N3CCCC3)Br InChI=1S/C23H31BrN8O3/c1-23(2,19(25)33)20(34)27-10-6-9-26-18-17(24)14-28-21(31-18)29-15-7-5-8-16(13-15)30-22(35)32-11-3-4-12-32/h5,7-8,13-14H,3-4,6,9-12H2,1-2H3,(H2,25,33)(H,27,34)(H,30,35)(H2,26,28,29,31) ZNSULAZTNWFKEW-UHFFFAOYSA-N 17053 N-(3-{[5-bromo-2-({3-[(pyrrolidin-1-ylcarbonyl)amino]phenyl}amino)pyrimidin-4-yl]amino}propyl)-2,2-dimethylpropanediamide::N-{3-[(5-bromo-2-{[3-(pyrrolidin-1-ylcarbonylamino)phenyl]amino}pyrimidin-4-yl)amino]propyl}-2,2-dimethylpropanediamide::BX-320 3-phosphoinositide-dependent protein kinase 1 Homo sapiens 39 ChEMBL 10.1016/j.bmcl.2016.05.005 10.7270/Q2M61N5R 27217002 Wucherer-Plietker, M; Merkul, E; Müller, TJ; Esdar, C; Knöchel, T; Heinrich, T; Buchstaller, HP; Greiner, H; Dorsch, D; Finsinger, D; Calderini, M; Bruge, D; Grädler, U 6/9/2016 9/18/2017 Merck http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=17053 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1744&target=3-phosphoinositide-dependent+protein+kinase+1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=17053&enzyme=3-phosphoinositide-dependent+protein+kinase+1&column=ki&startPg=0&Increment=50&submit=Search LI8 1Z5M 657138 46517283 1 MARTTSQLYDAVPIQSSVVLCSCPSPSMVRTQTESSTPPGIPGGSRQGPAMDGTAAEPRPGAGSLQHAQPPPQPRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILEKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKLYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSALEYLHGKGIIHRDLKPENILLNEDMHIQITDFGTAKVLSPESKQARANSFVGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPFRAGNEYLIFQKIIKLEYDFPEKFFPKARDLVEKLLVLDATKRLGCEEMEGYGPLKAHPFFESVTWENLHQQTPPKLTAYLPAMSEDDEDCYGNYDNLLSQFGCMQVSSSSSSHSLSASDTGLPQRSGSNIEQYIHDLDSNSFELDLQFSEDEKRLLLEKQAGGNPWHQFVENNLILKMGPVDKRKGLFARRRQLLLTEGPHLYYVDPVNKVLKGEIPWSQELRPEAKNFKTFFVHTPNRTYYLMDPSGNAHKWCRKIQEVWRQRYQSHPDAAVQ 3QD4,3QD3,3QD0,3QCY,3QCX,3QCS,3QCQ,3IOP,3ION,2R7B,1UU8,1UU7,1UU3,1OKZ,1OKY,3SC1,3RWQ,3RWP,5HO8,5HO7,5HNG,5HKM,2XCH,3H9O,3NAY,3NAX,3NUN,1UVR,1H1W,1UU9,3NUY,3NUU,3NUS,2PE2,2PE1,2PE0,1Z5M,1W1H,1W1G,1W1D 3-phosphoinositide-dependent protein kinase 1 PDPK1_HUMAN O15530 H0Y4Z0 Q59EH6 Q6FI20 Q8IV52 Q9BRD5 50709425 CC(C)(C(=O)N)C(=O)NCCCNc1c(cnc(n1)Nc2cccc(c2)NC(=O)N3CCCC3)Br InChI=1S/C23H31BrN8O3/c1-23(2,19(25)33)20(34)27-10-6-9-26-18-17(24)14-28-21(31-18)29-15-7-5-8-16(13-15)30-22(35)32-11-3-4-12-32/h5,7-8,13-14H,3-4,6,9-12H2,1-2H3,(H2,25,33)(H,27,34)(H,30,35)(H2,26,28,29,31) ZNSULAZTNWFKEW-UHFFFAOYSA-N 17053 N-(3-{[5-bromo-2-({3-[(pyrrolidin-1-ylcarbonyl)amino]phenyl}amino)pyrimidin-4-yl]amino}propyl)-2,2-dimethylpropanediamide::N-{3-[(5-bromo-2-{[3-(pyrrolidin-1-ylcarbonylamino)phenyl]amino}pyrimidin-4-yl)amino]propyl}-2,2-dimethylpropanediamide::BX-320 3-phosphoinositide-dependent protein kinase 1 Homo sapiens 39 ChEMBL 10.1016/j.bmcl.2011.11.006 10.7270/Q2N016ZX 22119465 Poulsen, A; Blanchard, S; Soh, CK; Lee, C; Williams, M; Wang, H; Dymock, B 12/30/2011 7/22/2012 S Bio http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=17053 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1744&target=3-phosphoinositide-dependent+protein+kinase+1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=17053&enzyme=3-phosphoinositide-dependent+protein+kinase+1&column=ki&startPg=0&Increment=50&submit=Search LI8 1Z5M 657138 46517283 1 MARTTSQLYDAVPIQSSVVLCSCPSPSMVRTQTESSTPPGIPGGSRQGPAMDGTAAEPRPGAGSLQHAQPPPQPRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILEKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKLYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSALEYLHGKGIIHRDLKPENILLNEDMHIQITDFGTAKVLSPESKQARANSFVGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPFRAGNEYLIFQKIIKLEYDFPEKFFPKARDLVEKLLVLDATKRLGCEEMEGYGPLKAHPFFESVTWENLHQQTPPKLTAYLPAMSEDDEDCYGNYDNLLSQFGCMQVSSSSSSHSLSASDTGLPQRSGSNIEQYIHDLDSNSFELDLQFSEDEKRLLLEKQAGGNPWHQFVENNLILKMGPVDKRKGLFARRRQLLLTEGPHLYYVDPVNKVLKGEIPWSQELRPEAKNFKTFFVHTPNRTYYLMDPSGNAHKWCRKIQEVWRQRYQSHPDAAVQ 3QD4,3QD3,3QD0,3QCY,3QCX,3QCS,3QCQ,3IOP,3ION,2R7B,1UU8,1UU7,1UU3,1OKZ,1OKY,3SC1,3RWQ,3RWP,5HO8,5HO7,5HNG,5HKM,2XCH,3H9O,3NAY,3NAX,3NUN,1UVR,1H1W,1UU9,3NUY,3NUU,3NUS,2PE2,2PE1,2PE0,1Z5M,1W1H,1W1G,1W1D 3-phosphoinositide-dependent protein kinase 1 PDPK1_HUMAN O15530 H0Y4Z0 Q59EH6 Q6FI20 Q8IV52 Q9BRD5 51055869 CC(C)(C(=O)N)C(=O)NCCCNc1c(cnc(n1)Nc2cccc(c2)NC(=O)N3CCCC3)Br InChI=1S/C23H31BrN8O3/c1-23(2,19(25)33)20(34)27-10-6-9-26-18-17(24)14-28-21(31-18)29-15-7-5-8-16(13-15)30-22(35)32-11-3-4-12-32/h5,7-8,13-14H,3-4,6,9-12H2,1-2H3,(H2,25,33)(H,27,34)(H,30,35)(H2,26,28,29,31) ZNSULAZTNWFKEW-UHFFFAOYSA-N 17053 N-(3-{[5-bromo-2-({3-[(pyrrolidin-1-ylcarbonyl)amino]phenyl}amino)pyrimidin-4-yl]amino}propyl)-2,2-dimethylpropanediamide::N-{3-[(5-bromo-2-{[3-(pyrrolidin-1-ylcarbonylamino)phenyl]amino}pyrimidin-4-yl)amino]propyl}-2,2-dimethylpropanediamide::BX-320 3-phosphoinositide-dependent protein kinase 1 Homo sapiens 30 ChEMBL 10.1021/jm4000227 10.7270/Q24Q7WCF 23448267 Medina, JR 4/11/2013 9/24/2013 Glaxosmithkline http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=17053 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1744&target=3-phosphoinositide-dependent+protein+kinase+1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=17053&enzyme=3-phosphoinositide-dependent+protein+kinase+1&column=ki&startPg=0&Increment=50&submit=Search LI8 1Z5M 657138 46517283 1 MARTTSQLYDAVPIQSSVVLCSCPSPSMVRTQTESSTPPGIPGGSRQGPAMDGTAAEPRPGAGSLQHAQPPPQPRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILEKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKLYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSALEYLHGKGIIHRDLKPENILLNEDMHIQITDFGTAKVLSPESKQARANSFVGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPFRAGNEYLIFQKIIKLEYDFPEKFFPKARDLVEKLLVLDATKRLGCEEMEGYGPLKAHPFFESVTWENLHQQTPPKLTAYLPAMSEDDEDCYGNYDNLLSQFGCMQVSSSSSSHSLSASDTGLPQRSGSNIEQYIHDLDSNSFELDLQFSEDEKRLLLEKQAGGNPWHQFVENNLILKMGPVDKRKGLFARRRQLLLTEGPHLYYVDPVNKVLKGEIPWSQELRPEAKNFKTFFVHTPNRTYYLMDPSGNAHKWCRKIQEVWRQRYQSHPDAAVQ 3QD4,3QD3,3QD0,3QCY,3QCX,3QCS,3QCQ,3IOP,3ION,2R7B,1UU8,1UU7,1UU3,1OKZ,1OKY,3SC1,3RWQ,3RWP,5HO8,5HO7,5HNG,5HKM,2XCH,3H9O,3NAY,3NAX,3NUN,1UVR,1H1W,1UU9,3NUY,3NUU,3NUS,2PE2,2PE1,2PE0,1Z5M,1W1H,1W1G,1W1D 3-phosphoinositide-dependent protein kinase 1 PDPK1_HUMAN O15530 H0Y4Z0 Q59EH6 Q6FI20 Q8IV52 Q9BRD5 30762 Cn1cc(c2c1cccc2)C3=C(C(=O)NC3=O)c4cn(c5c4cccc5)CCCN InChI=1S/C24H22N4O2/c1-27-13-17(15-7-2-4-9-19(15)27)21-22(24(30)26-23(21)29)18-14-28(12-6-11-25)20-10-5-3-8-16(18)20/h2-5,7-10,13-14H,6,11-12,25H2,1H3,(H,26,29,30) UQHKJRCFSLMWIA-UHFFFAOYSA-N 2695 Ro 31-7549::3-[1-(3-aminopropyl)-1H-indol-3-yl]-4-(1-methyl-1H-indol-3-yl)-2,5-dihydro-1H-pyrrole-2,5-dione::Bisindolylmaleimide VIII::Bisindolylmaleimide deriv. 2b::BIM-8::ROCHE screening, 49 3-phosphoinositide-dependent protein kinase 1 [51-359] Homo sapiens 1000 7.5000 30.00 C Curated from the literature by BindingDB 10.1016/j.str.2004.01.005 10.7270/Q2SJ1HV2 14962382 aid1797582 Komander, D; Kular, GS; Schüttelkopf, AW; Deak, M; Prakash, KR; Bain, J; Elliott, M; Garrido-Franco, M; Kozikowski, AP; Alessi, DR; van Aalten, DM 2/28/2004 8/2/2007 University of Dundee http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=2695 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=465&target=3-phosphoinositide-dependent+protein+kinase+1+%5B51-359%5D&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=2695&enzyme=3-phosphoinositide-dependent+protein+kinase+1+%5B51-359%5D&column=ki&startPg=0&Increment=50&submit=Search BI8 2VD5,1UVR 2403 8032458 DB01946 1 MDGTAAEPRPGAGSLQHAQPPPQPRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILEKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKLYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSALEYLHGKGIIHRDLKPENILLNEDMHIQITDFGTAKVLSPESKQARANSFVGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPFRAGNEYLIFQKIIKLEYDFPEKFFPKARDLVEKLLVLDATKRLGCEEMEGYGPLKAHPFFESVTWENLHQQTPPKLT 3RWP,1UU8,1UU7,1UU3,1OKZ,1OKY,5HO8,5HO7,5HNG,5HKM,2XCH,3SC1,3RWQ,3QD4,3QD3,3QD0,3QCY,3QCX,3QCS,3QCQ,3IOP,3ION,3H9O,2R7B,3NAY,3NAX,3NUN,1UVR,1H1W,1UU9,3NUY,3NUU,3NUS,2PE2,2PE1,2PE0,1Z5M 3-phosphoinositide-dependent protein kinase 1 PDPK1_HUMAN O15530 H0Y4Z0 Q59EH6 Q6FI20 Q8IV52 Q9BRD5 50500579 CSc1c(c(n(n1)C(=O)N)N)C(=O)N InChI=1S/C6H9N5O2S/c1-14-5-2(4(8)12)3(7)11(10-5)6(9)13/h7H2,1H3,(H2,8,12)(H2,9,13) TUVCBRIDRHWVLF-UHFFFAOYSA-N 50178295 CHEMBL3814512 3-phosphoinositide-dependent protein kinase 1 Homo sapiens 17000 ChEMBL 10.1016/j.bmcl.2016.05.005 10.7270/Q2M61N5R 27217002 Wucherer-Plietker, M; Merkul, E; Müller, TJ; Esdar, C; Knöchel, T; Heinrich, T; Buchstaller, HP; Greiner, H; Dorsch, D; Finsinger, D; Calderini, M; Bruge, D; Grädler, U 6/9/2016 9/18/2017 Merck http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50178295 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1744&target=3-phosphoinositide-dependent+protein+kinase+1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50178295&enzyme=3-phosphoinositide-dependent+protein+kinase+1&column=ki&startPg=0&Increment=50&submit=Search 63L 5HO7 119081690 346549405 CHEMBL3814512 1 MARTTSQLYDAVPIQSSVVLCSCPSPSMVRTQTESSTPPGIPGGSRQGPAMDGTAAEPRPGAGSLQHAQPPPQPRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILEKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKLYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSALEYLHGKGIIHRDLKPENILLNEDMHIQITDFGTAKVLSPESKQARANSFVGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPFRAGNEYLIFQKIIKLEYDFPEKFFPKARDLVEKLLVLDATKRLGCEEMEGYGPLKAHPFFESVTWENLHQQTPPKLTAYLPAMSEDDEDCYGNYDNLLSQFGCMQVSSSSSSHSLSASDTGLPQRSGSNIEQYIHDLDSNSFELDLQFSEDEKRLLLEKQAGGNPWHQFVENNLILKMGPVDKRKGLFARRRQLLLTEGPHLYYVDPVNKVLKGEIPWSQELRPEAKNFKTFFVHTPNRTYYLMDPSGNAHKWCRKIQEVWRQRYQSHPDAAVQ 3QD4,3QD3,3QD0,3QCY,3QCX,3QCS,3QCQ,3IOP,3ION,2R7B,1UU8,1UU7,1UU3,1OKZ,1OKY,3SC1,3RWQ,3RWP,5HO8,5HO7,5HNG,5HKM,2XCH,3H9O,3NAY,3NAX,3NUN,1UVR,1H1W,1UU9,3NUY,3NUU,3NUS,2PE2,2PE1,2PE0,1Z5M,1W1H,1W1G,1W1D 3-phosphoinositide-dependent protein kinase 1 PDPK1_HUMAN O15530 H0Y4Z0 Q59EH6 Q6FI20 Q8IV52 Q9BRD5 50711906 CC(C)n1cc(c2c1ncnc2N)C(=O)c3cncc(n3)NCCc4cccnc4 InChI=1S/C21H22N8O/c1-13(2)29-11-15(18-20(22)26-12-27-21(18)29)19(30)16-9-24-10-17(28-16)25-7-5-14-4-3-6-23-8-14/h3-4,6,8-13H,5,7H2,1-2H3,(H,25,28)(H2,22,26,27) WMUOCKJUZCEMCY-UHFFFAOYSA-N 50361647 CHEMBL1940244 3-phosphoinositide-dependent protein kinase 1 Homo sapiens 35 ChEMBL 10.1021/jm201019k 10.7270/Q23N23TV 22040023 Murphy, ST; Alton, G; Bailey, S; Baxi, SM; Burke, BJ; Chappie, TA; Ermolieff, J; Ferre, R; Greasley, S; Hickey, M; Humphrey, J; Kablaoui, N; Kath, J; Kazmirski, S; Kraus, M; Kupchinsky, S; Li, J; Lingardo, L; Marx, MA; Richter, D; Tanis, SP; Tran, K; Vernier, W; Xie, Z; Yin, MJ; Yu, XH 12/15/2011 7/22/2012 Pfizer http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50361647 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1744&target=3-phosphoinositide-dependent+protein+kinase+1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50361647&enzyme=3-phosphoinositide-dependent+protein+kinase+1&column=ki&startPg=0&Increment=50&submit=Search 3RW 3RWQ 53488414 136965709 CHEMBL1940244 1 MARTTSQLYDAVPIQSSVVLCSCPSPSMVRTQTESSTPPGIPGGSRQGPAMDGTAAEPRPGAGSLQHAQPPPQPRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILEKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKLYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSALEYLHGKGIIHRDLKPENILLNEDMHIQITDFGTAKVLSPESKQARANSFVGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPFRAGNEYLIFQKIIKLEYDFPEKFFPKARDLVEKLLVLDATKRLGCEEMEGYGPLKAHPFFESVTWENLHQQTPPKLTAYLPAMSEDDEDCYGNYDNLLSQFGCMQVSSSSSSHSLSASDTGLPQRSGSNIEQYIHDLDSNSFELDLQFSEDEKRLLLEKQAGGNPWHQFVENNLILKMGPVDKRKGLFARRRQLLLTEGPHLYYVDPVNKVLKGEIPWSQELRPEAKNFKTFFVHTPNRTYYLMDPSGNAHKWCRKIQEVWRQRYQSHPDAAVQ 3QD4,3QD3,3QD0,3QCY,3QCX,3QCS,3QCQ,3IOP,3ION,2R7B,1UU8,1UU7,1UU3,1OKZ,1OKY,3SC1,3RWQ,3RWP,5HO8,5HO7,5HNG,5HKM,2XCH,3H9O,3NAY,3NAX,3NUN,1UVR,1H1W,1UU9,3NUY,3NUU,3NUS,2PE2,2PE1,2PE0,1Z5M,1W1H,1W1G,1W1D 3-phosphoinositide-dependent protein kinase 1 PDPK1_HUMAN O15530 H0Y4Z0 Q59EH6 Q6FI20 Q8IV52 Q9BRD5 34067 Cc1c(ccc2c1nc(c3c2c4cc(c(cc4nc3)OC)OC)N)N InChI=1S/C19H18N4O2/c1-9-13(20)5-4-10-17-11-6-15(24-2)16(25-3)7-14(11)22-8-12(17)19(21)23-18(9)10/h4-8H,20H2,1-3H3,(H2,21,23) NVINUNQBDNEMSY-UHFFFAOYSA-N 19087 15,16-dimethoxy-6-methyl-8,12-diazatetracyclo[8.8.0.0^{2,7}.0^{13,18}]octadeca-1(10),2(7),3,5,8,11,13,15,17-nonaene-5,9-diamine::Dibenzo[c,f][2,7]naphthyridine, 1 3-phosphoinositide-dependent protein kinase 1 Homo sapiens 60 7.4000 23.00 C Curated from the literature by BindingDB 10.1021/jm070851i 10.7270/Q2639N0S 17941624 aid1797819 Gopalsamy, A; Shi, M; Boschelli, DH; Williamson, R; Olland, A; Hu, Y; Krishnamurthy, G; Han, X; Arndt, K; Guo, B 11/15/2007 11/25/2007 Wyeth Research http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19087 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1744&target=3-phosphoinositide-dependent+protein+kinase+1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19087&enzyme=3-phosphoinositide-dependent+protein+kinase+1&column=ki&startPg=0&Increment=50&submit=Search 253 2R7B 17754396 46519134 DB06932 1 MARTTSQLYDAVPIQSSVVLCSCPSPSMVRTQTESSTPPGIPGGSRQGPAMDGTAAEPRPGAGSLQHAQPPPQPRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILEKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKLYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSALEYLHGKGIIHRDLKPENILLNEDMHIQITDFGTAKVLSPESKQARANSFVGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPFRAGNEYLIFQKIIKLEYDFPEKFFPKARDLVEKLLVLDATKRLGCEEMEGYGPLKAHPFFESVTWENLHQQTPPKLTAYLPAMSEDDEDCYGNYDNLLSQFGCMQVSSSSSSHSLSASDTGLPQRSGSNIEQYIHDLDSNSFELDLQFSEDEKRLLLEKQAGGNPWHQFVENNLILKMGPVDKRKGLFARRRQLLLTEGPHLYYVDPVNKVLKGEIPWSQELRPEAKNFKTFFVHTPNRTYYLMDPSGNAHKWCRKIQEVWRQRYQSHPDAAVQ 3QD4,3QD3,3QD0,3QCY,3QCX,3QCS,3QCQ,3IOP,3ION,2R7B,1UU8,1UU7,1UU3,1OKZ,1OKY,3SC1,3RWQ,3RWP,5HO8,5HO7,5HNG,5HKM,2XCH,3H9O,3NAY,3NAX,3NUN,1UVR,1H1W,1UU9,3NUY,3NUU,3NUS,2PE2,2PE1,2PE0,1Z5M,1W1H,1W1G,1W1D 3-phosphoinositide-dependent protein kinase 1 PDPK1_HUMAN O15530 H0Y4Z0 Q59EH6 Q6FI20 Q8IV52 Q9BRD5 50572246 Cc1c(ccc2c1nc(c3c2c4cc(c(cc4nc3)OC)OC)N)N InChI=1S/C19H18N4O2/c1-9-13(20)5-4-10-17-11-6-15(24-2)16(25-3)7-14(11)22-8-12(17)19(21)23-18(9)10/h4-8H,20H2,1-3H3,(H2,21,23) NVINUNQBDNEMSY-UHFFFAOYSA-N 19087 15,16-dimethoxy-6-methyl-8,12-diazatetracyclo[8.8.0.0^{2,7}.0^{13,18}]octadeca-1(10),2(7),3,5,8,11,13,15,17-nonaene-5,9-diamine::Dibenzo[c,f][2,7]naphthyridine, 1 3-phosphoinositide-dependent protein kinase 1 Homo sapiens 60 ChEMBL 10.1016/j.ejmech.2009.12.036 10.7270/Q2HD7VT5 20074837 Nittoli, T; Dushin, RG; Ingalls, C; Cheung, K; Floyd, MB; Fraser, H; Olland, A; Hu, Y; Grosu, G; Han, X; Arndt, K; Guo, B; Wissner, A 3/8/2010 11/19/2010 Wyeth Research http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19087 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1744&target=3-phosphoinositide-dependent+protein+kinase+1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19087&enzyme=3-phosphoinositide-dependent+protein+kinase+1&column=ki&startPg=0&Increment=50&submit=Search 253 2R7B 17754396 46519134 DB06932 1 MARTTSQLYDAVPIQSSVVLCSCPSPSMVRTQTESSTPPGIPGGSRQGPAMDGTAAEPRPGAGSLQHAQPPPQPRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILEKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKLYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSALEYLHGKGIIHRDLKPENILLNEDMHIQITDFGTAKVLSPESKQARANSFVGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPFRAGNEYLIFQKIIKLEYDFPEKFFPKARDLVEKLLVLDATKRLGCEEMEGYGPLKAHPFFESVTWENLHQQTPPKLTAYLPAMSEDDEDCYGNYDNLLSQFGCMQVSSSSSSHSLSASDTGLPQRSGSNIEQYIHDLDSNSFELDLQFSEDEKRLLLEKQAGGNPWHQFVENNLILKMGPVDKRKGLFARRRQLLLTEGPHLYYVDPVNKVLKGEIPWSQELRPEAKNFKTFFVHTPNRTYYLMDPSGNAHKWCRKIQEVWRQRYQSHPDAAVQ 3QD4,3QD3,3QD0,3QCY,3QCX,3QCS,3QCQ,3IOP,3ION,2R7B,1UU8,1UU7,1UU3,1OKZ,1OKY,3SC1,3RWQ,3RWP,5HO8,5HO7,5HNG,5HKM,2XCH,3H9O,3NAY,3NAX,3NUN,1UVR,1H1W,1UU9,3NUY,3NUU,3NUS,2PE2,2PE1,2PE0,1Z5M,1W1H,1W1G,1W1D 3-phosphoinositide-dependent protein kinase 1 PDPK1_HUMAN O15530 H0Y4Z0 Q59EH6 Q6FI20 Q8IV52 Q9BRD5 51055863 Cc1c(ccc2c1nc(c3c2c4cc(c(cc4nc3)OC)OC)N)N InChI=1S/C19H18N4O2/c1-9-13(20)5-4-10-17-11-6-15(24-2)16(25-3)7-14(11)22-8-12(17)19(21)23-18(9)10/h4-8H,20H2,1-3H3,(H2,21,23) NVINUNQBDNEMSY-UHFFFAOYSA-N 19087 15,16-dimethoxy-6-methyl-8,12-diazatetracyclo[8.8.0.0^{2,7}.0^{13,18}]octadeca-1(10),2(7),3,5,8,11,13,15,17-nonaene-5,9-diamine::Dibenzo[c,f][2,7]naphthyridine, 1 3-phosphoinositide-dependent protein kinase 1 Homo sapiens 60 ChEMBL 10.1021/jm4000227 10.7270/Q24Q7WCF 23448267 Medina, JR 4/11/2013 9/24/2013 Glaxosmithkline http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19087 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1744&target=3-phosphoinositide-dependent+protein+kinase+1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19087&enzyme=3-phosphoinositide-dependent+protein+kinase+1&column=ki&startPg=0&Increment=50&submit=Search 253 2R7B 17754396 46519134 DB06932 1 MARTTSQLYDAVPIQSSVVLCSCPSPSMVRTQTESSTPPGIPGGSRQGPAMDGTAAEPRPGAGSLQHAQPPPQPRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILEKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKLYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSALEYLHGKGIIHRDLKPENILLNEDMHIQITDFGTAKVLSPESKQARANSFVGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPFRAGNEYLIFQKIIKLEYDFPEKFFPKARDLVEKLLVLDATKRLGCEEMEGYGPLKAHPFFESVTWENLHQQTPPKLTAYLPAMSEDDEDCYGNYDNLLSQFGCMQVSSSSSSHSLSASDTGLPQRSGSNIEQYIHDLDSNSFELDLQFSEDEKRLLLEKQAGGNPWHQFVENNLILKMGPVDKRKGLFARRRQLLLTEGPHLYYVDPVNKVLKGEIPWSQELRPEAKNFKTFFVHTPNRTYYLMDPSGNAHKWCRKIQEVWRQRYQSHPDAAVQ 3QD4,3QD3,3QD0,3QCY,3QCX,3QCS,3QCQ,3IOP,3ION,2R7B,1UU8,1UU7,1UU3,1OKZ,1OKY,3SC1,3RWQ,3RWP,5HO8,5HO7,5HNG,5HKM,2XCH,3H9O,3NAY,3NAX,3NUN,1UVR,1H1W,1UU9,3NUY,3NUU,3NUS,2PE2,2PE1,2PE0,1Z5M,1W1H,1W1G,1W1D 3-phosphoinositide-dependent protein kinase 1 PDPK1_HUMAN O15530 H0Y4Z0 Q59EH6 Q6FI20 Q8IV52 Q9BRD5 200313 c1ccc(cc1)[C@H](COc2ccc3c(c2)NC(=O)N3)NC(=O)C4=CC=CN(C4=O)Cc5ccc(c(c5)F)F InChI=1S/C28H22F2N4O4/c29-21-10-8-17(13-22(21)30)15-34-12-4-7-20(27(34)36)26(35)31-25(18-5-2-1-3-6-18)16-38-19-9-11-23-24(14-19)33-28(37)32-23/h1-14,25H,15-16H2,(H,31,35)(H2,32,33,37) GCWCGSPBENFEPE-UHFFFAOYSA-N 92406 PDK1 inhibitor, 7 3-phosphoinositide-dependent protein kinase 1 Homo sapiens 1 Curated from the literature by BindingDB 10.1074/jbc.M110.156463 10.7270/Q21C1VGQ 21118801 aid1799765 Nagashima, K; Shumway, SD; Sathyanarayanan, S; Chen, AH; Dolinski, B; Xu, Y; Keilhack, H; Nguyen, T; Wiznerowicz, M; Li, L; Lutterbach, BA; Chi, A; Paweletz, C; Allison, T; Yan, Y; Munshi, SK; Klippel, A; Kraus, M; Bobkova, EV; Deshmukh, S; Xu, Z; Mueller, U; Szewczak, AA; Pan, BS; Richon, V; Pollock, R; Blume-Jensen, P; Northrup, A; Andersen, JN 2/25/2011 8/27/2012 Merck Research Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=92406 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1744&target=3-phosphoinositide-dependent+protein+kinase+1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=92406&enzyme=3-phosphoinositide-dependent+protein+kinase+1&column=ki&startPg=0&Increment=50&submit=Search MP7 3NAX,3QC4 56965967 160844903 1 MARTTSQLYDAVPIQSSVVLCSCPSPSMVRTQTESSTPPGIPGGSRQGPAMDGTAAEPRPGAGSLQHAQPPPQPRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILEKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKLYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSALEYLHGKGIIHRDLKPENILLNEDMHIQITDFGTAKVLSPESKQARANSFVGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPFRAGNEYLIFQKIIKLEYDFPEKFFPKARDLVEKLLVLDATKRLGCEEMEGYGPLKAHPFFESVTWENLHQQTPPKLTAYLPAMSEDDEDCYGNYDNLLSQFGCMQVSSSSSSHSLSASDTGLPQRSGSNIEQYIHDLDSNSFELDLQFSEDEKRLLLEKQAGGNPWHQFVENNLILKMGPVDKRKGLFARRRQLLLTEGPHLYYVDPVNKVLKGEIPWSQELRPEAKNFKTFFVHTPNRTYYLMDPSGNAHKWCRKIQEVWRQRYQSHPDAAVQ 3QD4,3QD3,3QD0,3QCY,3QCX,3QCS,3QCQ,3IOP,3ION,2R7B,1UU8,1UU7,1UU3,1OKZ,1OKY,3SC1,3RWQ,3RWP,5HO8,5HO7,5HNG,5HKM,2XCH,3H9O,3NAY,3NAX,3NUN,1UVR,1H1W,1UU9,3NUY,3NUU,3NUS,2PE2,2PE1,2PE0,1Z5M,1W1H,1W1G,1W1D 3-phosphoinositide-dependent protein kinase 1 PDPK1_HUMAN O15530 H0Y4Z0 Q59EH6 Q6FI20 Q8IV52 Q9BRD5 868679 CC(C)(C)c1ccc(cc1)N([C@H](c2cccnc2)C(=O)NC(C)(C)C)C(=O)c3ccco3 InChI=1S/C26H31N3O3/c1-25(2,3)19-11-13-20(14-12-19)29(24(31)21-10-8-16-32-21)22(18-9-7-15-27-17-18)23(30)28-26(4,5)6/h7-17,22H,1-6H3,(H,28,30) JXGIYKRRPGCLFV-UHFFFAOYSA-N 429329 jm5b01461, Compound 146-(R)::acs.jmedchem.1c00409_ST.265 Replicase polyprotein 1a Severe acute respiratory syndrome coronavirus 1500 Curated from the literature by BindingDB 10.1021/acs.jmedchem.5b01461 10.7270/Q2PK0JH1 26878082 aid1804126 Pillaiyar, T; Manickam, M; Namasivayam, V; Hayashi, Y; Jung, SH 7/28/2016 11/7/2020 University of Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=429329 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10768&target=Replicase+polyprotein+1a&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=429329&enzyme=Replicase+polyprotein+1a&column=ki&startPg=0&Increment=50&submit=Search 0EN 3V3M,7L0D 46897844 434318838 1 MESLVLGVNEKTHVQLSLPVLQVRDVLVRGFGDSVEEALSEAREHLKNGTCGLVELEKGVLPQLEQPYVFIKRSDALSTNHGHKVVELVAEMDGIQYGRSGITLGVLVPHVGETPIAYRNVLLRKNGNKGAGGHSYGIDLKSYDLGDELGTDPIEDYEQNWNTKHGSGALRELTRELNGGAVTRYVDNNFCGPDGYPLDCIKDFLARAGKSMCTLSEQLDYIESKRGVYCCRDHEHEIAWFTERSDKSYEHQTPFEIKSAKKFDTFKGECPKFVFPLNSKVKVIQPRVEKKKTEGFMGRIRSVYPVASPQECNNMHLSTLMKCNHCDEVSWQTCDFLKATCEHCGTENLVIEGPTTCGYLPTNAVVKMPCPACQDPEIGPEHSVADYHNHSNIETRLRKGGRTRCFGGCVFAYVGCYNKRAYWVPRASADIGSGHTGITGDNVETLNEDLLEILSRERVNINIVGDFHLNEEVAIILASFSASTSAFIDTIKSLDYKSFKTIVESCGNYKVTKGKPVKGAWNIGQQRSVLTPLCGFPSQAAGVIRSIFARTLDAANHSIPDLQRAAVTILDGISEQSLRLVDAMVYTSDLLTNSVIIMAYVTGGLVQQTSQWLSNLLGTTVEKLRPIFEWIEAKLSAGVEFLKDAWEILKFLITGVFDIVKGQIQVASDNIKDCVKCFIDVVNKALEMCIDQVTIAGAKLRSLNLGEVFIAQSKGLYRQCIRGKEQLQLLMPLKAPKEVTFLEGDSHDTVLTSEEVVLKNGELEALETPVDSFTNGAIVGTPVCVNGLMLLEIKDKEQYCALSPGLLATNNVFRLKGGAPIKGVTFGEDTVWEVQGYKNVRITFELDERVDKVLNEKCSVYTVESGTEVTEFACVVAEAVVKTLQPVSDLLTNMGIDLDEWSVATFYLFDDAGEENFSSRMYCSFYPPDEEEEDDAECEEEEIDETCEHEYGTEDDYQGLPLEFGASAETVRVEEEEEEDWLDDTTEQSEIEPEPEPTPEEPVNQFTGYLKLTDNVAIKCVDIVKEAQSANPMVIVNAANIHLKHGGGVAGALNKATNGAMQKESDDYIKLNGPLTVGGSCLLSGHNLAKKCLHVVGPNLNAGEDIQLLKAAYENFNSQDILLAPLLSAGIFGAKPLQSLQVCVQTVRTQVYIAVNDKALYEQVVMDYLDNLKPRVEAPKQEEPPNTEDSKTEEKSVVQKPVDVKPKIKACIDEVTTTLEETKFLTNKLLLFADINGKLYHDSQNMLRGEDMSFLEKDAPYMVGDVITSGDITCVVIPSKKAGGTTEMLSRALKKVPVDEYITTYPGQGCAGYTLEEAKTALKKCKSAFYVLPSEAPNAKEEILGTVSWNLREMLAHAEETRKLMPICMDVRAIMATIQRKYKGIKIQEGIVDYGVRFFFYTSKEPVASIITKLNSLNEPLVTMPIGYVTHGFNLEEAARCMRSLKAPAVVSVSSPDAVTTYNGYLTSSSKTSEEHFVETVSLAGSYRDWSYSGQRTELGVEFLKRGDKIVYHTLESPVEFHLDGEVLSLDKLKSLLSLREVKTIKVFTTVDNTNLHTQLVDMSMTYGQQFGPTYLDGADVTKIKPHVNHEGKTFFVLPSDDTLRSEAFEYYHTLDESFLGRYMSALNHTKKWKFPQVGGLTSIKWADNNCYLSSVLLALQQLEVKFNAPALQEAYYRARAGDAANFCALILAYSNKTVGELGDVRETMTHLLQHANLESAKRVLNVVCKHCGQKTTTLTGVEAVMYMGTLSYDNLKTGVSIPCVCGRDATQYLVQQESSFVMMSAPPAEYKLQQGTFLCANEYTGNYQCGHYTHITAKETLYRIDGAHLTKMSEYKGPVTDVFYKETSYTTTIKPVSYKLDGVTYTEIEPKLDGYYKKDNAYYTEQPIDLVPTQPLPNASFDNFKLTCSNTKFADDLNQMTGFTKPASRELSVTFFPDLNGDVVAIDYRHYSASFKKGAKLLHKPIVWHINQATTKTTFKPNTWCLRCLWSTKPVDTSNSFEVLAVEDTQGMDNLACESQQPTSEEVVENPTIQKEVIECDVKTTEVVGNVILKPSDEGVKVTQELGHEDLMAAYVENTSITIKKPNELSLALGLKTIATHGIAAINSVPWSKILAYVKPFLGQAAITTSNCAKRLAQRVFNNYMPYVFTLLFQLCTFTKSTNSRIRASLPTTIAKNSVKSVAKLCLDAGINYVKSPKFSKLFTIAMWLLLLSICLGSLICVTAAFGVLLSNFGAPSYCNGVRELYLNSSNVTTMDFCEGSFPCSICLSGLDSLDSYPALETIQVTISSYKLDLTILGLAAEWVLAYMLFTKFFYLLGLSAIMQVFFGYFASHFISNSWLMWFIISIVQMAPVSAMVRMYIFFASFYYIWKSYVHIMDGCTSSTCMMCYKRNRATRVECTTIVNGMKRSFYVYANGGRGFCKTHNWNCLNCDTFCTGSTFISDEVARDLSLQFKRPINPTDQSSYIVDSVAVKNGALHLYFDKAGQKTYERHPLSHFVNLDNLRANNTKGSLPINVIVFDGKSKCDESASKSASVYYSQLMCQPILLLDQALVSDVGDSTEVSVKMFDAYVDTFSATFSVPMEKLKALVATAHSELAKGVALDGVLSTFVSAARQGVVDTDVDTKDVIECLKLSHHSDLEVTGDSCNNFMLTYNKVENMTPRDLGACIDCNARHINAQVAKSHNVSLIWNVKDYMSLSEQLRKQIRSAAKKNNIPFRLTCATTRQVVNVITTKISLKGGKIVSTCFKLMLKATLLCVLAALVCYIVMPVHTLSIHDGYTNEIIGYKAIQDGVTRDIISTDDCFANKHAGFDAWFSQRGGSYKNDKSCPVVAAIITREIGFIVPGLPGTVLRAINGDFLHFLPRVFSAVGNICYTPSKLIEYSDFATSACVLAAECTIFKDAMGKPVPYCYDTNLLEGSISYSELRPDTRYVLMDGSIIQFPNTYLEGSVRVVTTFDAEYCRHGTCERSEVGICLSTSGRWVLNNEHYRALSGVFCGVDAMNLIANIFTPLVQPVGALDVSASVVAGGIIAILVTCAAYYFMKFRRVFGEYNHVVAANALLFLMSFTILCLVPAYSFLPGVYSVFYLYLTFYFTNDVSFLAHLQWFAMFSPIVPFWITAIYVFCISLKHCHWFFNNYLRKRVMFNGVTFSTFEEAALCTFLLNKEMYLKLRSETLLPLTQYNRYLALYNKYKYFSGALDTTSYREAACCHLAKALNDFSNSGADVLYQPPQTSITSAVLQSGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDTVYCPRHVICTAEDMLNPNYEDLLIRKSNHSFLVQAGNVQLRVIGHSMQNCLLRLKVDTSNPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNHTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGKFYGPFVDRQTAQAAGTDTTITLNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCAALKELLQNGMNGRTILGSTILEDEFTPFDVVRQCSGVTFQGKFKKIVKGTHHWMLLTFLTSLLILVQSTQWSLFFFVYENAFLPFTLGIMAIAACAMLLVKHKHAFLCLFLLPSLATVAYFNMVYMPASWVMRIMTWLELADTSLSGYRLKDCVMYASALVLLILMTARTVYDDAARRVWTLMNVITLVYKVYYGNALDQAISMWALVISVTSNYSGVVTTIMFLARAIVFVCVEYYPLLFITGNTLQCIMLVYCFLGYCCCCYFGLFCLLNRYFRLTLGVYDYLVSTQEFRYMNSQGLLPPKSSIDAFKLNIKLLGIGGKPCIKVATVQSKMSDVKCTSVVLLSVLQQLRVESSSKLWAQCVQLHNDILLAKDTTEAFEKMVSLLSVLLSMQGAVDINRLCEEMLDNRATLQAIASEFSSLPSYAAYATAQEAYEQAVANGDSEVVLKKLKKSLNVAKSEFDRDAAMQRKLEKMADQAMTQMYKQARSEDKRAKVTSAMQTMLFTMLRKLDNDALNNIINNARDGCVPLNIIPLTTAAKLMVVVPDYGTYKNTCDGNTFTYASALWEIQQVVDADSKIVQLSEINMDNSPNLAWPLIVTALRANSAVKLQNNELSPVALRQMSCAAGTTQTACTDDNALAYYNNSKGGRFVLALLSDHQDLKWARFPKSDGTGTIYTELEPPCRFVTDTPKGPKVKYLYFIKGLNNLNRGMVLGSLAATVRLQAGNATEVPANSTVLSFCAFAVDPAKAYKDYLASGGQPITNCVKMLCTHTGTGQAITVTPEANMDQESFGGASCCLYCRCHIDHPNPKGFCDLKGKYVQIPTTCANDPVGFTLRNTVCTVCGMWKGYGCSCDQLREPLMQSADASTFLNGFAV 7FAC,5TL7,5TL6,3E9S,4OW0,4OVZ,4MM3,3MJ5,2FE8,5Y3Q,5Y3E,9CEH,9XG4,7ZQW,7XAX,7RC1,7LMJ,7LMI,7LMH,7LMG,7LCQ,7LCP,7EO8,7END,7DQZ,6Y7M,6XHO,6XHN,6XHL,6WCO,6W79,6LO0,6LNY,6LNQ,5N5O,5N19,3VB7,3VB6,3VB5,3VB4,3VB3,3V3M,3TNT,3TNS,3TIU,3TIT,3SZN,3SNE,3SND,3SNC,3SNB,3SN8,3IWM,2ZU5,2ZU4,2Z9L,2Z9K,2Z9J,2Z9G,2Z94,2Z3E,2Z3D,2Z3C,2V6N,2HOB,2H2Z,2GZ9,2GZ8,2GZ7,2GX4,2GTB,2GT8,2GT7,2DUC,2C3S,2BX4,2BX3,2A5K,2A5I,2A5A,1Z1I,1UK4,1UK3,1UK2,1UJ1,2D2D,2AMQ,2AMD,1WOF,8ULD,1Q2W,3M3V,3EA8,3EA7,3E91,7K0H,7K0G,6W2A,2ALV,2VJ1,4MDS,2OP9,3SNA,9MBV,9LZQ,8IG5,7WQI,7VLO,3D62,7YGQ,9JGS,8YKK,8Y4E,8HUS Replicase polyprotein 1a R1A_SARS P0C6U8 P59641 51594673 CC(C)(C)c1ccc(cc1)N([C@H](c2cccnc2)C(=O)NC(C)(C)C)C(=O)c3ccco3 InChI=1S/C26H31N3O3/c1-25(2,3)19-11-13-20(14-12-19)29(24(31)21-10-8-16-32-21)22(18-9-7-15-27-17-18)23(30)28-26(4,5)6/h7-17,22H,1-6H3,(H,28,30) JXGIYKRRPGCLFV-UHFFFAOYSA-N 429329 jm5b01461, Compound 146-(R)::acs.jmedchem.1c00409_ST.265 Replicase polyprotein 1a Severe acute respiratory syndrome coronavirus 1500 ChEMBL 10.7270/Q2T72P2D 37659195 Li, X; Song, Y //0 10/12/2025 Baylor College of Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=429329 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10768&target=Replicase+polyprotein+1a&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=429329&enzyme=Replicase+polyprotein+1a&column=ki&startPg=0&Increment=50&submit=Search 0EN 3V3M,7L0D 46897844 434318838 1 MESLVLGVNEKTHVQLSLPVLQVRDVLVRGFGDSVEEALSEAREHLKNGTCGLVELEKGVLPQLEQPYVFIKRSDALSTNHGHKVVELVAEMDGIQYGRSGITLGVLVPHVGETPIAYRNVLLRKNGNKGAGGHSYGIDLKSYDLGDELGTDPIEDYEQNWNTKHGSGALRELTRELNGGAVTRYVDNNFCGPDGYPLDCIKDFLARAGKSMCTLSEQLDYIESKRGVYCCRDHEHEIAWFTERSDKSYEHQTPFEIKSAKKFDTFKGECPKFVFPLNSKVKVIQPRVEKKKTEGFMGRIRSVYPVASPQECNNMHLSTLMKCNHCDEVSWQTCDFLKATCEHCGTENLVIEGPTTCGYLPTNAVVKMPCPACQDPEIGPEHSVADYHNHSNIETRLRKGGRTRCFGGCVFAYVGCYNKRAYWVPRASADIGSGHTGITGDNVETLNEDLLEILSRERVNINIVGDFHLNEEVAIILASFSASTSAFIDTIKSLDYKSFKTIVESCGNYKVTKGKPVKGAWNIGQQRSVLTPLCGFPSQAAGVIRSIFARTLDAANHSIPDLQRAAVTILDGISEQSLRLVDAMVYTSDLLTNSVIIMAYVTGGLVQQTSQWLSNLLGTTVEKLRPIFEWIEAKLSAGVEFLKDAWEILKFLITGVFDIVKGQIQVASDNIKDCVKCFIDVVNKALEMCIDQVTIAGAKLRSLNLGEVFIAQSKGLYRQCIRGKEQLQLLMPLKAPKEVTFLEGDSHDTVLTSEEVVLKNGELEALETPVDSFTNGAIVGTPVCVNGLMLLEIKDKEQYCALSPGLLATNNVFRLKGGAPIKGVTFGEDTVWEVQGYKNVRITFELDERVDKVLNEKCSVYTVESGTEVTEFACVVAEAVVKTLQPVSDLLTNMGIDLDEWSVATFYLFDDAGEENFSSRMYCSFYPPDEEEEDDAECEEEEIDETCEHEYGTEDDYQGLPLEFGASAETVRVEEEEEEDWLDDTTEQSEIEPEPEPTPEEPVNQFTGYLKLTDNVAIKCVDIVKEAQSANPMVIVNAANIHLKHGGGVAGALNKATNGAMQKESDDYIKLNGPLTVGGSCLLSGHNLAKKCLHVVGPNLNAGEDIQLLKAAYENFNSQDILLAPLLSAGIFGAKPLQSLQVCVQTVRTQVYIAVNDKALYEQVVMDYLDNLKPRVEAPKQEEPPNTEDSKTEEKSVVQKPVDVKPKIKACIDEVTTTLEETKFLTNKLLLFADINGKLYHDSQNMLRGEDMSFLEKDAPYMVGDVITSGDITCVVIPSKKAGGTTEMLSRALKKVPVDEYITTYPGQGCAGYTLEEAKTALKKCKSAFYVLPSEAPNAKEEILGTVSWNLREMLAHAEETRKLMPICMDVRAIMATIQRKYKGIKIQEGIVDYGVRFFFYTSKEPVASIITKLNSLNEPLVTMPIGYVTHGFNLEEAARCMRSLKAPAVVSVSSPDAVTTYNGYLTSSSKTSEEHFVETVSLAGSYRDWSYSGQRTELGVEFLKRGDKIVYHTLESPVEFHLDGEVLSLDKLKSLLSLREVKTIKVFTTVDNTNLHTQLVDMSMTYGQQFGPTYLDGADVTKIKPHVNHEGKTFFVLPSDDTLRSEAFEYYHTLDESFLGRYMSALNHTKKWKFPQVGGLTSIKWADNNCYLSSVLLALQQLEVKFNAPALQEAYYRARAGDAANFCALILAYSNKTVGELGDVRETMTHLLQHANLESAKRVLNVVCKHCGQKTTTLTGVEAVMYMGTLSYDNLKTGVSIPCVCGRDATQYLVQQESSFVMMSAPPAEYKLQQGTFLCANEYTGNYQCGHYTHITAKETLYRIDGAHLTKMSEYKGPVTDVFYKETSYTTTIKPVSYKLDGVTYTEIEPKLDGYYKKDNAYYTEQPIDLVPTQPLPNASFDNFKLTCSNTKFADDLNQMTGFTKPASRELSVTFFPDLNGDVVAIDYRHYSASFKKGAKLLHKPIVWHINQATTKTTFKPNTWCLRCLWSTKPVDTSNSFEVLAVEDTQGMDNLACESQQPTSEEVVENPTIQKEVIECDVKTTEVVGNVILKPSDEGVKVTQELGHEDLMAAYVENTSITIKKPNELSLALGLKTIATHGIAAINSVPWSKILAYVKPFLGQAAITTSNCAKRLAQRVFNNYMPYVFTLLFQLCTFTKSTNSRIRASLPTTIAKNSVKSVAKLCLDAGINYVKSPKFSKLFTIAMWLLLLSICLGSLICVTAAFGVLLSNFGAPSYCNGVRELYLNSSNVTTMDFCEGSFPCSICLSGLDSLDSYPALETIQVTISSYKLDLTILGLAAEWVLAYMLFTKFFYLLGLSAIMQVFFGYFASHFISNSWLMWFIISIVQMAPVSAMVRMYIFFASFYYIWKSYVHIMDGCTSSTCMMCYKRNRATRVECTTIVNGMKRSFYVYANGGRGFCKTHNWNCLNCDTFCTGSTFISDEVARDLSLQFKRPINPTDQSSYIVDSVAVKNGALHLYFDKAGQKTYERHPLSHFVNLDNLRANNTKGSLPINVIVFDGKSKCDESASKSASVYYSQLMCQPILLLDQALVSDVGDSTEVSVKMFDAYVDTFSATFSVPMEKLKALVATAHSELAKGVALDGVLSTFVSAARQGVVDTDVDTKDVIECLKLSHHSDLEVTGDSCNNFMLTYNKVENMTPRDLGACIDCNARHINAQVAKSHNVSLIWNVKDYMSLSEQLRKQIRSAAKKNNIPFRLTCATTRQVVNVITTKISLKGGKIVSTCFKLMLKATLLCVLAALVCYIVMPVHTLSIHDGYTNEIIGYKAIQDGVTRDIISTDDCFANKHAGFDAWFSQRGGSYKNDKSCPVVAAIITREIGFIVPGLPGTVLRAINGDFLHFLPRVFSAVGNICYTPSKLIEYSDFATSACVLAAECTIFKDAMGKPVPYCYDTNLLEGSISYSELRPDTRYVLMDGSIIQFPNTYLEGSVRVVTTFDAEYCRHGTCERSEVGICLSTSGRWVLNNEHYRALSGVFCGVDAMNLIANIFTPLVQPVGALDVSASVVAGGIIAILVTCAAYYFMKFRRVFGEYNHVVAANALLFLMSFTILCLVPAYSFLPGVYSVFYLYLTFYFTNDVSFLAHLQWFAMFSPIVPFWITAIYVFCISLKHCHWFFNNYLRKRVMFNGVTFSTFEEAALCTFLLNKEMYLKLRSETLLPLTQYNRYLALYNKYKYFSGALDTTSYREAACCHLAKALNDFSNSGADVLYQPPQTSITSAVLQSGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDTVYCPRHVICTAEDMLNPNYEDLLIRKSNHSFLVQAGNVQLRVIGHSMQNCLLRLKVDTSNPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNHTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGKFYGPFVDRQTAQAAGTDTTITLNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCAALKELLQNGMNGRTILGSTILEDEFTPFDVVRQCSGVTFQGKFKKIVKGTHHWMLLTFLTSLLILVQSTQWSLFFFVYENAFLPFTLGIMAIAACAMLLVKHKHAFLCLFLLPSLATVAYFNMVYMPASWVMRIMTWLELADTSLSGYRLKDCVMYASALVLLILMTARTVYDDAARRVWTLMNVITLVYKVYYGNALDQAISMWALVISVTSNYSGVVTTIMFLARAIVFVCVEYYPLLFITGNTLQCIMLVYCFLGYCCCCYFGLFCLLNRYFRLTLGVYDYLVSTQEFRYMNSQGLLPPKSSIDAFKLNIKLLGIGGKPCIKVATVQSKMSDVKCTSVVLLSVLQQLRVESSSKLWAQCVQLHNDILLAKDTTEAFEKMVSLLSVLLSMQGAVDINRLCEEMLDNRATLQAIASEFSSLPSYAAYATAQEAYEQAVANGDSEVVLKKLKKSLNVAKSEFDRDAAMQRKLEKMADQAMTQMYKQARSEDKRAKVTSAMQTMLFTMLRKLDNDALNNIINNARDGCVPLNIIPLTTAAKLMVVVPDYGTYKNTCDGNTFTYASALWEIQQVVDADSKIVQLSEINMDNSPNLAWPLIVTALRANSAVKLQNNELSPVALRQMSCAAGTTQTACTDDNALAYYNNSKGGRFVLALLSDHQDLKWARFPKSDGTGTIYTELEPPCRFVTDTPKGPKVKYLYFIKGLNNLNRGMVLGSLAATVRLQAGNATEVPANSTVLSFCAFAVDPAKAYKDYLASGGQPITNCVKMLCTHTGTGQAITVTPEANMDQESFGGASCCLYCRCHIDHPNPKGFCDLKGKYVQIPTTCANDPVGFTLRNTVCTVCGMWKGYGCSCDQLREPLMQSADASTFLNGFAV 7FAC,5TL7,5TL6,3E9S,4OW0,4OVZ,4MM3,3MJ5,2FE8,5Y3Q,5Y3E,9CEH,9XG4,7ZQW,7XAX,7RC1,7LMJ,7LMI,7LMH,7LMG,7LCQ,7LCP,7EO8,7END,7DQZ,6Y7M,6XHO,6XHN,6XHL,6WCO,6W79,6LO0,6LNY,6LNQ,5N5O,5N19,3VB7,3VB6,3VB5,3VB4,3VB3,3V3M,3TNT,3TNS,3TIU,3TIT,3SZN,3SNE,3SND,3SNC,3SNB,3SN8,3IWM,2ZU5,2ZU4,2Z9L,2Z9K,2Z9J,2Z9G,2Z94,2Z3E,2Z3D,2Z3C,2V6N,2HOB,2H2Z,2GZ9,2GZ8,2GZ7,2GX4,2GTB,2GT8,2GT7,2DUC,2C3S,2BX4,2BX3,2A5K,2A5I,2A5A,1Z1I,1UK4,1UK3,1UK2,1UJ1,2D2D,2AMQ,2AMD,1WOF,8ULD,1Q2W,3M3V,3EA8,3EA7,3E91,7K0H,7K0G,6W2A,2ALV,2VJ1,4MDS,2OP9,3SNA,9MBV,9LZQ,8IG5,7WQI,7VLO,3D62,7YGQ,9JGS,8YKK,8Y4E,8HUS Replicase polyprotein 1a R1A_SARS P0C6U8 P59641 1539408 Cn1cc2cc(c(cc2n1)Cl)NC3=NC(=O)N(C(=O)N3Cc4cc(c(cc4F)F)F)Cc5ncn(n5)C InChI=1S/C22H17ClF3N9O2/c1-32-7-12-4-18(13(23)5-17(12)30-32)28-20-29-21(36)35(9-19-27-10-33(2)31-19)22(37)34(20)8-11-3-15(25)16(26)6-14(11)24/h3-7,10H,8-9H2,1-2H3,(H,28,29,36) QMPBBNUOBOFBFS-UHFFFAOYSA-N 639154 US20230391736, Example S-217622::US20250025459, Compound I-005::US20250127788, Compound I-005::US20250188102, Compound CVL201 Replicase polyprotein 1ab Human coronavirus NL63 27790 US Patent 10.7270/Q2S46XJR US20250188102 SHEN, X; HUANG, J 6/12/2025 10/7/2025 Jkt Biopharma Co. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=639154 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=781&target=Replicase+polyprotein+1ab&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=639154&enzyme=Replicase+polyprotein+1ab&column=ki&startPg=0&Increment=50&submit=Search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eplicase polyprotein 1ab R1AB_CVHNL P0C6X5 Q6Q1S3 1356903 Cn1cc2cc(c(cc2n1)Cl)NC3=NC(=O)N(C(=O)N3Cc4cc(c(cc4F)F)F)Cc5ncn(n5)C InChI=1S/C22H17ClF3N9O2/c1-32-7-12-4-18(13(23)5-17(12)30-32)28-20-29-21(36)35(9-19-27-10-33(2)31-19)22(37)34(20)8-11-3-15(25)16(26)6-14(11)24/h3-7,10H,8-9H2,1-2H3,(H,28,29,36) QMPBBNUOBOFBFS-UHFFFAOYSA-N 639154 US20230391736, Example S-217622::US20250025459, Compound I-005::US20250127788, Compound I-005::US20250188102, Compound CVL201 Replicase polyprotein 1a Severe acute respiratory syndrome coronavirus 2 33.0 US Patent 10.7270/Q2V410C2 aid1920074 US20230391736 XIE, X; Zhang, D; Ma, Z; Li, B; Zhou, X; Liang, C; Xin, L; Tian, L; Li, J; Wu, K; Zhang, S; Yang, X; Liu, S; Liu, Y 12/7/2023 1/28/2024 Shaanxi Panlong Pharmaceutical Co. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=639154 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1225&target=Replicase+polyprotein+1a&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=639154&enzyme=Replicase+polyprotein+1a&column=ki&startPg=0&Increment=50&submit=Search 7YY 7VU6,8DZ0,8DZ1,8H3G,8H3K,8H3L,8HBK,8HEF,8HOM,8HUR,8HUS,8HUT,8HUU,8HUV,8HUW,8HUX,8INX,8INY,8V8E,8V8G,9CJQ,9CJR,9CMS,9CMU,9N6P,9N6R 170795177 488872080 1 MESLVPGFNEKTHVQLSLPVLQVRDVLVRGFGDSVEEVLSEARQHLKDGTCGLVEVEKGVLPQLEQPYVFIKRSDARTAPHGHVMVELVAELEGIQYGRSGETLGVLVPHVGEIPVAYRKVLLRKNGNKGAGGHSYGADLKSFDLGDELGTDPYEDFQENWNTKHSSGVTRELMRELNGGAYTRYVDNNFCGPDGYPLECIKDLLARAGKASCTLSEQLDFIDTKRGVYCCREHEHEIAWYTERSEKSYELQTPFEIKLAKKFDTFNGECPNFVFPLNSIIKTIQPRVEKKKLDGFMGRIRSVYPVASPNECNQMCLSTLMKCDHCGETSWQTGDFVKATCEFCGTENLTKEGATTCGYLPQNAVVKIYCPACHNSEVGPEHSLAEYHNESGLKTILRKGGRTIAFGGCVFSYVGCHNKCAYWVPRASANIGCNHTGVVGEGSEGLNDNLLEILQKEKVNINIVGDFKLNEEIAIILASFSASTSAFVETVKGLDYKAFKQIVESCGNFKVTKGKAKKGAWNIGEQKSILSPLYAFASEAARVVRSIFSRTLETAQNSVRVLQKAAITILDGISQYSLRLIDAMMFTSDLATNNLVVMAYITGGVVQLTSQWLTNIFGTVYEKLKPVLDWLEEKFKEGVEFLRDGWEIVKFISTCACEIVGGQIVTCAKEIKESVQTFFKLVNKFLALCADSIIIGGAKLKALNLGETFVTHSKGLYRKCVKSREETGLLMPLKAPKEIIFLEGETLPTEVLTEEVVLKTGDLQPLEQPTSEAVEAPLVGTPVCINGLMLLEIKDTEKYCALAPNMMVTNNTFTLKGGAPTKVTFGDDTVIEVQGYKSVNITFELDERIDKVLNEKCSAYTVELGTEVNEFACVVADAVIKTLQPVSELLTPLGIDLDEWSMATYYLFDESGEFKLASHMYCSFYPPDEDEEEGDCEEEEFEPSTQYEYGTEDDYQGKPLEFGATSAALQPEEEQEEDWLDDDSQQTVGQQDGSEDNQTTTIQTIVEVQPQLEMELTPVVQTIEVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYDKLVSSFLEMKSEKQVEQKIAEIPKEEVKPFITESKPSVEQRKQDDKKIKACVEEVTTTLEETKFLTENLLLYIDINGNLHPDSATLVSDIDITFLKKDAPYIVGDVVQEGVLTAVVIPTKKAGGTTEMLAKALRKVPTDNYITTYPGQGLNGYTVEEAKTVLKKCKSAFYILPSIISNEKQEILGTVSWNLREMLAHAEETRKLMPVCVETKAIVSTIQRKYKGIKIQEGVVDYGARFYFYTSKTTVASLINTLNDLNETLVTMPLGYVTHGLNLEEAARYMRSLKVPATVSVSSPDAVTAYNGYLTSSSKTPEEHFIETISLAGSYKDWSYSGQSTQLGIEFLKRGDKSVYYTSNPTTFHLDGEVITFDNLKTLLSLREVRTIKVFTTVDNINLHTQVVDMSMTYGQQFGPTYLDGADVTKIKPHNSHEGKTFYVLPNDDTLRVEAFEYYHTTDPSFLGRYMSALNHTKKWKYPQVNGLTSIKWADNNCYLATALLTLQQIELKFNPPALQDAYYRARAGEAANFCALILAYCNKTVGELGDVRETMSYLFQHANLDSCKRVLNVVCKTCGQQQTTLKGVEAVMYMGTLSYEQFKKGVQIPCTCGKQATKYLVQQESPFVMMSAPPAQYELKHGTFTCASEYTGNYQCGHYKHITSKETLYCIDGALLTKSSEYKGPITDVFYKENSYTTTIKPVTYKLDGVVCTEIDPKLDNYYKKDNSYFTEQPIDLVPNQPYPNASFDNFKFVCDNIKFADDLNQLTGYKKPASRELKVTFFPDLNGDVVAIDYKHYTPSFKKGAKLLHKPIVWHVNNATNKATYKPNTWCIRCLWSTKPVETSNSFDVLKSEDAQGMDNLACEDLKPVSEEVVENPTIQKDVLECNVKTTEVVGDIILKPANNSLKITEEVGHTDLMAAYVDNSSLTIKKPNELSRVLGLKTLATHGLAAVNSVPWDTIANYAKPFLNKVVSTTTNIVTRCLNRVCTNYMPYFFTLLLQLCTFTRSTNSRIKASMPTTIAKNTVKSVGKFCLEASFNYLKSPNFSKLINIIIWFLLLSVCLGSLIYSTAALGVLMSNLGMPSYCTGYREGYLNSTNVTIATYCTGSIPCSVCLSGLDSLDTYPSLETIQITISSFKWDLTAFGLVAEWFLAYILFTRFFYVLGLAAIMQLFFSYFAVHFISNSWLMWLIINLVQMAPISAMVRMYIFFASFYYVWKSYVHVVDGCNSSTCMMCYKRNRATRVECTTIVNGVRRSFYVYANGGKGFCKLHNWNCVNCDTFCAGSTFISDEVARDLSLQFKRPINPTDQSSYIVDSVTVKNGSIHLYFDKAGQKTYERHSLSHFVNLDNLRANNTKGSLPINVIVFDGKSKCEESSAKSASVYYSQLMCQPILLLDQALVSDVGDSAEVAVKMFDAYVNTFSSTFNVPMEKLKTLVATAEAELAKNVSLDNVLSTFISAARQGFVDSDVETKDVVECLKLSHQSDIEVTGDSCNNYMLTYNKVENMTPRDLGACIDCSARHINAQVAKSHNIALIWNVKDFMSLSEQLRKQIRSAAKKNNLPFKLTCATTRQVVNVVTTKIALKGGKIVNNWLKQLIKVTLVFLFVAAIFYLITPVHVMSKHTDFSSEIIGYKAIDGGVTRDIASTDTCFANKHADFDTWFSQRGGSYTNDKACPLIAAVITREVGFVVPGLPGTILRTTNGDFLHFLPRVFSAVGNICYTPSKLIEYTDFATSACVLAAECTIFKDASGKPVPYCYDTNVLEGSVAYESLRPDTRYVLMDGSIIQFPNTYLEGSVRVVTTFDSEYCRHGTCERSEAGVCVSTSGRWVLNNDYYRSLPGVFCGVDAVNLLTNMFTPLIQPIGALDISASIVAGGIVAIVVTCLAYYFMRFRRAFGEYSHVVAFNTLLFLMSFTVLCLTPVYSFLPGVYSVIYLYLTFYLTNDVSFLAHIQWMVMFTPLVPFWITIAYIICISTKHFYWFFSNYLKRRVVFNGVSFSTFEEAALCTFLLNKEMYLKLRSDVLLPLTQYNRYLALYNKYKYFSGAMDTTSYREAACCHLAKALNDFSNSGSDVLYQPPQTSITSAVLQSGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQSAVKRTIKGTHHWLLLTILTSLLVLVQSTQWSLFFFLYENAFLPFAMGIIAMSAFAMMFVKHKHAFLCLFLLPSLATVAYFNMVYMPASWVMRIMTWLDMVDTSLSGFKLKDCVMYASAVVLLILMTARTVYDDGARRVWTLMNVLTLVYKVYYGNALDQAISMWALIISVTSNYSGVVTTVMFLARGIVFMCVEYCPIFFITGNTLQCIMLVYCFLGYFCTCYFGLFCLLNRYFRLTLGVYDYLVSTQEFRYMNSQGLLPPKNSIDAFKLNIKLLGVGGKPCIKVATVQSKMSDVKCTSVVLLSVLQQLRVESSSKLWAQCVQLHNDILLAKDTTEAFEKMVSLLSVLLSMQGAVDINKLCEEMLDNRATLQAIASEFSSLPSYAAFATAQEAYEQAVANGDSEVVLKKLKKSLNVAKSEFDRDAAMQRKLEKMADQAMTQMYKQARSEDKRAKVTSAMQTMLFTMLRKLDNDALNNIINNARDGCVPLNIIPLTTAAKLMVVIPDYNTYKNTCDGTTFTYASALWEIQQVVDADSKIVQLSEISMDNSPNLAWPLIVTALRANSAVKLQNNELSPVALRQMSCAAGTTQTACTDDNALAYYNTTKGGRFVLALLSDLQDLKWARFPKSDGTGTIYTELEPPCRFVTDTPKGPKVKYLYFIKGLNNLNRGMVLGSLAATVRLQAGNATEVPANSTVLSFCAFAVDAAKAYKDYLASGGQPITNCVKMLCTHTGTGQAITVTPEANMDQESFGGASCCLYCRCHIDHPNPKGFCDLKGKYVQIPTTCANDPVGFTLKNTVCTVCGMWKGYGCSCDQLREPMLQSADAQSFLNGFAV 8YB7,8YB5,8YAX,7MSX,7MSW,8EIR,9Z6C,9Z6B,7CMD,6XAA,9HHI,9HHG,6XA9,6W9C,9OR4,9DOI,9DO5,9DO3,9DO1,9DNV,9DNU,9D2K,8UVM,8UUY,8UUW,8UUV,8UUU,8UUH,8UUG,8UUF,8UOB,8G62,8FWO,7SGW,7SDR,7RZC,7NT4,7KOL,7JN2,7JIW,6WZU,9Z0D,9BF8,8Z4W,8IHO,7QCM,7QCK,7QCJ,7QCI,7QCH,7QCG,7OFU,7OFT,7OFS,7NFV,7LOS,7LLZ,7LLF,7LBS,7LBR,7JRN,8CX9,7UV5,9PUJ,9PUH,9LVR,9ZO3,9ZNL,9XZ6,9XYM,9VS1,9UOQ,9SDM,9RJR,9RJF,9RJ8,9RJ7,9RJ5,9RJ3,9RJ0,9RIZ,9RIY,9RIX,9RID,9RI8,9RI5,9RI4,9RI3,9RI1,9RI0,9RHX,9RHT,9RHS,9Q7S,9PJG,9OJT,9OJG,9OIZ,9OIX,9OCK,9NWC,9NWB,9NWA,9NU6,9NSL,9NSK,9N99,9N6R,9MLJ,9LVV,9LVT,9J8U,9J8T,9IZB,9IR9,9IK2,9HJH,9HFY,9HFX,9HDN,9HDJ,9HDC,9HD8,9HC1,9HBQ,9HAK,9HAJ,9H4B,9GV2,9GMQ,9GLV,9GIL,9GIJ,9GF7,9G0I,9G0H,9FX7,9FX6,9FQA,9FQ9,9FHQ,9F2X,9F2V,9EOX,9EOR Replicase polyprotein 1a R1A_SARS2 P0DTC1 1481947 Cn1cc2cc(c(cc2n1)Cl)NC3=NC(=O)N(C(=O)N3Cc4cc(c(cc4F)F)F)Cc5ncn(n5)C InChI=1S/C22H17ClF3N9O2/c1-32-7-12-4-18(13(23)5-17(12)30-32)28-20-29-21(36)35(9-19-27-10-33(2)31-19)22(37)34(20)8-11-3-15(25)16(26)6-14(11)24/h3-7,10H,8-9H2,1-2H3,(H,28,29,36) QMPBBNUOBOFBFS-UHFFFAOYSA-N 639154 US20230391736, Example S-217622::US20250025459, Compound I-005::US20250127788, Compound I-005::US20250188102, Compound CVL201 Replicase polyprotein 1a Severe acute respiratory syndrome coronavirus 2 10.00 US Patent 10.7270/Q2NK3KK5 aid2060933 US20250025459 YANO, R; YAMAMOTO, A; NOBORI, H; KATO, T 1/23/2025 5/29/2025 Shionogi http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=639154 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1225&target=Replicase+polyprotein+1a&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=639154&enzyme=Replicase+polyprotein+1a&column=ki&startPg=0&Increment=50&submit=Search 7YY 7VU6,8DZ0,8DZ1,8H3G,8H3K,8H3L,8HBK,8HEF,8HOM,8HUR,8HUS,8HUT,8HUU,8HUV,8HUW,8HUX,8INX,8INY,8V8E,8V8G,9CJQ,9CJR,9CMS,9CMU,9N6P,9N6R 170795177 488872080 1 MESLVPGFNEKTHVQLSLPVLQVRDVLVRGFGDSVEEVLSEARQHLKDGTCGLVEVEKGVLPQLEQPYVFIKRSDARTAPHGHVMVELVAELEGIQYGRSGETLGVLVPHVGEIPVAYRKVLLRKNGNKGAGGHSYGADLKSFDLGDELGTDPYEDFQENWNTKHSSGVTRELMRELNGGAYTRYVDNNFCGPDGYPLECIKDLLARAGKASCTLSEQLDFIDTKRGVYCCREHEHEIAWYTERSEKSYELQTPFEIKLAKKFDTFNGECPNFVFPLNSIIKTIQPRVEKKKLDGFMGRIRSVYPVASPNECNQMCLSTLMKCDHCGETSWQTGDFVKATCEFCGTENLTKEGATTCGYLPQNAVVKIYCPACHNSEVGPEHSLAEYHNESGLKTILRKGGRTIAFGGCVFSYVGCHNKCAYWVPRASANIGCNHTGVVGEGSEGLNDNLLEILQKEKVNINIVGDFKLNEEIAIILASFSASTSAFVETVKGLDYKAFKQIVESCGNFKVTKGKAKKGAWNIGEQKSILSPLYAFASEAARVVRSIFSRTLETAQNSVRVLQKAAITILDGISQYSLRLIDAMMFTSDLATNNLVVMAYITGGVVQLTSQWLTNIFGTVYEKLKPVLDWLEEKFKEGVEFLRDGWEIVKFISTCACEIVGGQIVTCAKEIKESVQTFFKLVNKFLALCADSIIIGGAKLKALNLGETFVTHSKGLYRKCVKSREETGLLMPLKAPKEIIFLEGETLPTEVLTEEVVLKTGDLQPLEQPTSEAVEAPLVGTPVCINGLMLLEIKDTEKYCALAPNMMVTNNTFTLKGGAPTKVTFGDDTVIEVQGYKSVNITFELDERIDKVLNEKCSAYTVELGTEVNEFACVVADAVIKTLQPVSELLTPLGIDLDEWSMATYYLFDESGEFKLASHMYCSFYPPDEDEEEGDCEEEEFEPSTQYEYGTEDDYQGKPLEFGATSAALQPEEEQEEDWLDDDSQQTVGQQDGSEDNQTTTIQTIVEVQPQLEMELTPVVQTIEVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYDKLVSSFLEMKSEKQVEQKIAEIPKEEVKPFITESKPSVEQRKQDDKKIKACVEEVTTTLEETKFLTENLLLYIDINGNLHPDSATLVSDIDITFLKKDAPYIVGDVVQEGVLTAVVIPTKKAGGTTEMLAKALRKVPTDNYITTYPGQGLNGYTVEEAKTVLKKCKSAFYILPSIISNEKQEILGTVSWNLREMLAHAEETRKLMPVCVETKAIVSTIQRKYKGIKIQEGVVDYGARFYFYTSKTTVASLINTLNDLNETLVTMPLGYVTHGLNLEEAARYMRSLKVPATVSVSSPDAVTAYNGYLTSSSKTPEEHFIETISLAGSYKDWSYSGQSTQLGIEFLKRGDKSVYYTSNPTTFHLDGEVITFDNLKTLLSLREVRTIKVFTTVDNINLHTQVVDMSMTYGQQFGPTYLDGADVTKIKPHNSHEGKTFYVLPNDDTLRVEAFEYYHTTDPSFLGRYMSALNHTKKWKYPQVNGLTSIKWADNNCYLATALLTLQQIELKFNPPALQDAYYRARAGEAANFCALILAYCNKTVGELGDVRETMSYLFQHANLDSCKRVLNVVCKTCGQQQTTLKGVEAVMYMGTLSYEQFKKGVQIPCTCGKQATKYLVQQESPFVMMSAPPAQYELKHGTFTCASEYTGNYQCGHYKHITSKETLYCIDGALLTKSSEYKGPITDVFYKENSYTTTIKPVTYKLDGVVCTEIDPKLDNYYKKDNSYFTEQPIDLVPNQPYPNASFDNFKFVCDNIKFADDLNQLTGYKKPASRELKVTFFPDLNGDVVAIDYKHYTPSFKKGAKLLHKPIVWHVNNATNKATYKPNTWCIRCLWSTKPVETSNSFDVLKSEDAQGMDNLACEDLKPVSEEVVENPTIQKDVLECNVKTTEVVGDIILKPANNSLKITEEVGHTDLMAAYVDNSSLTIKKPNELSRVLGLKTLATHGLAAVNSVPWDTIANYAKPFLNKVVSTTTNIVTRCLNRVCTNYMPYFFTLLLQLCTFTRSTNSRIKASMPTTIAKNTVKSVGKFCLEASFNYLKSPNFSKLINIIIWFLLLSVCLGSLIYSTAALGVLMSNLGMPSYCTGYREGYLNSTNVTIATYCTGSIPCSVCLSGLDSLDTYPSLETIQITISSFKWDLTAFGLVAEWFLAYILFTRFFYVLGLAAIMQLFFSYFAVHFISNSWLMWLIINLVQMAPISAMVRMYIFFASFYYVWKSYVHVVDGCNSSTCMMCYKRNRATRVECTTIVNGVRRSFYVYANGGKGFCKLHNWNCVNCDTFCAGSTFISDEVARDLSLQFKRPINPTDQSSYIVDSVTVKNGSIHLYFDKAGQKTYERHSLSHFVNLDNLRANNTKGSLPINVIVFDGKSKCEESSAKSASVYYSQLMCQPILLLDQALVSDVGDSAEVAVKMFDAYVNTFSSTFNVPMEKLKTLVATAEAELAKNVSLDNVLSTFISAARQGFVDSDVETKDVVECLKLSHQSDIEVTGDSCNNYMLTYNKVENMTPRDLGACIDCSARHINAQVAKSHNIALIWNVKDFMSLSEQLRKQIRSAAKKNNLPFKLTCATTRQVVNVVTTKIALKGGKIVNNWLKQLIKVTLVFLFVAAIFYLITPVHVMSKHTDFSSEIIGYKAIDGGVTRDIASTDTCFANKHADFDTWFSQRGGSYTNDKACPLIAAVITREVGFVVPGLPGTILRTTNGDFLHFLPRVFSAVGNICYTPSKLIEYTDFATSACVLAAECTIFKDASGKPVPYCYDTNVLEGSVAYESLRPDTRYVLMDGSIIQFPNTYLEGSVRVVTTFDSEYCRHGTCERSEAGVCVSTSGRWVLNNDYYRSLPGVFCGVDAVNLLTNMFTPLIQPIGALDISASIVAGGIVAIVVTCLAYYFMRFRRAFGEYSHVVAFNTLLFLMSFTVLCLTPVYSFLPGVYSVIYLYLTFYLTNDVSFLAHIQWMVMFTPLVPFWITIAYIICISTKHFYWFFSNYLKRRVVFNGVSFSTFEEAALCTFLLNKEMYLKLRSDVLLPLTQYNRYLALYNKYKYFSGAMDTTSYREAACCHLAKALNDFSNSGSDVLYQPPQTSITSAVLQSGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQSAVKRTIKGTHHWLLLTILTSLLVLVQSTQWSLFFFLYENAFLPFAMGIIAMSAFAMMFVKHKHAFLCLFLLPSLATVAYFNMVYMPASWVMRIMTWLDMVDTSLSGFKLKDCVMYASAVVLLILMTARTVYDDGARRVWTLMNVLTLVYKVYYGNALDQAISMWALIISVTSNYSGVVTTVMFLARGIVFMCVEYCPIFFITGNTLQCIMLVYCFLGYFCTCYFGLFCLLNRYFRLTLGVYDYLVSTQEFRYMNSQGLLPPKNSIDAFKLNIKLLGVGGKPCIKVATVQSKMSDVKCTSVVLLSVLQQLRVESSSKLWAQCVQLHNDILLAKDTTEAFEKMVSLLSVLLSMQGAVDINKLCEEMLDNRATLQAIASEFSSLPSYAAFATAQEAYEQAVANGDSEVVLKKLKKSLNVAKSEFDRDAAMQRKLEKMADQAMTQMYKQARSEDKRAKVTSAMQTMLFTMLRKLDNDALNNIINNARDGCVPLNIIPLTTAAKLMVVIPDYNTYKNTCDGTTFTYASALWEIQQVVDADSKIVQLSEISMDNSPNLAWPLIVTALRANSAVKLQNNELSPVALRQMSCAAGTTQTACTDDNALAYYNTTKGGRFVLALLSDLQDLKWARFPKSDGTGTIYTELEPPCRFVTDTPKGPKVKYLYFIKGLNNLNRGMVLGSLAATVRLQAGNATEVPANSTVLSFCAFAVDAAKAYKDYLASGGQPITNCVKMLCTHTGTGQAITVTPEANMDQESFGGASCCLYCRCHIDHPNPKGFCDLKGKYVQIPTTCANDPVGFTLKNTVCTVCGMWKGYGCSCDQLREPMLQSADAQSFLNGFAV 8YB7,8YB5,8YAX,7MSX,7MSW,8EIR,9Z6C,9Z6B,7CMD,6XAA,9HHI,9HHG,6XA9,6W9C,9OR4,9DOI,9DO5,9DO3,9DO1,9DNV,9DNU,9D2K,8UVM,8UUY,8UUW,8UUV,8UUU,8UUH,8UUG,8UUF,8UOB,8G62,8FWO,7SGW,7SDR,7RZC,7NT4,7KOL,7JN2,7JIW,6WZU,9Z0D,9BF8,8Z4W,8IHO,7QCM,7QCK,7QCJ,7QCI,7QCH,7QCG,7OFU,7OFT,7OFS,7NFV,7LOS,7LLZ,7LLF,7LBS,7LBR,7JRN,8CX9,7UV5,9PUJ,9PUH,9LVR,9ZO3,9ZNL,9XZ6,9XYM,9VS1,9UOQ,9SDM,9RJR,9RJF,9RJ8,9RJ7,9RJ5,9RJ3,9RJ0,9RIZ,9RIY,9RIX,9RID,9RI8,9RI5,9RI4,9RI3,9RI1,9RI0,9RHX,9RHT,9RHS,9Q7S,9PJG,9OJT,9OJG,9OIZ,9OIX,9OCK,9NWC,9NWB,9NWA,9NU6,9NSL,9NSK,9N99,9N6R,9MLJ,9LVV,9LVT,9J8U,9J8T,9IZB,9IR9,9IK2,9HJH,9HFY,9HFX,9HDN,9HDJ,9HDC,9HD8,9HC1,9HBQ,9HAK,9HAJ,9H4B,9GV2,9GMQ,9GLV,9GIL,9GIJ,9GF7,9G0I,9G0H,9FX7,9FX6,9FQA,9FQ9,9FHQ,9F2X,9F2V,9EOX,9EOR Replicase polyprotein 1a R1A_SARS2 P0DTC1 1539393 Cn1cc2cc(c(cc2n1)Cl)NC3=NC(=O)N(C(=O)N3Cc4cc(c(cc4F)F)F)Cc5ncn(n5)C InChI=1S/C22H17ClF3N9O2/c1-32-7-12-4-18(13(23)5-17(12)30-32)28-20-29-21(36)35(9-19-27-10-33(2)31-19)22(37)34(20)8-11-3-15(25)16(26)6-14(11)24/h3-7,10H,8-9H2,1-2H3,(H,28,29,36) QMPBBNUOBOFBFS-UHFFFAOYSA-N 639154 US20230391736, Example S-217622::US20250025459, Compound I-005::US20250127788, Compound I-005::US20250188102, Compound CVL201 Replicase polyprotein 1a [P3395H] 55.0 US Patent 10.7270/Q2S46XJR US20250188102 SHEN, X; HUANG, J 6/12/2025 10/7/2025 Jkt Biopharma Co. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=639154 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1985&target=Replicase+polyprotein+1a+%5BP3395H%5D&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=639154&enzyme=Replicase+polyprotein+1a+%5BP3395H%5D&column=ki&startPg=0&Increment=50&submit=Search 7YY 7VU6,8DZ0,8DZ1,8H3G,8H3K,8H3L,8HBK,8HEF,8HOM,8HUR,8HUS,8HUT,8HUU,8HUV,8HUW,8HUX,8INX,8INY,8V8E,8V8G,9CJQ,9CJR,9CMS,9CMU,9N6P,9N6R 170795177 488872080 1 SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRHNFTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ 9PFI,9PFH,9MDQ,8Y7U,8Y7T,8WTI,8R26,8R19,8R0V,8HOZ,8HOM,8HOL,8HHU,8DI3,7TVX,7TVS,7TOB,7TLL Replicase polyprotein 1a R1A_SARS2 P0DTC1 1539393 Cn1cc2cc(c(cc2n1)Cl)NC3=NC(=O)N(C(=O)N3Cc4cc(c(cc4F)F)F)Cc5ncn(n5)C InChI=1S/C22H17ClF3N9O2/c1-32-7-12-4-18(13(23)5-17(12)30-32)28-20-29-21(36)35(9-19-27-10-33(2)31-19)22(37)34(20)8-11-3-15(25)16(26)6-14(11)24/h3-7,10H,8-9H2,1-2H3,(H,28,29,36) QMPBBNUOBOFBFS-UHFFFAOYSA-N 639154 US20230391736, Example S-217622::US20250025459, Compound I-005::US20250127788, Compound I-005::US20250188102, Compound CVL201 Replicase polyprotein 1a [P3395H] 55.0 US Patent 10.7270/Q2S46XJR US20250188102 SHEN, X; HUANG, J 6/12/2025 10/7/2025 Jkt Biopharma Co. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=639154 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1985&target=Replicase+polyprotein+1a+%5BP3395H%5D&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=639154&enzyme=Replicase+polyprotein+1a+%5BP3395H%5D&column=ki&startPg=0&Increment=50&submit=Search 7YY 7VU6,8DZ0,8DZ1,8H3G,8H3K,8H3L,8HBK,8HEF,8HOM,8HUR,8HUS,8HUT,8HUU,8HUV,8HUW,8HUX,8INX,8INY,8V8E,8V8G,9CJQ,9CJR,9CMS,9CMU,9N6P,9N6R 170795177 488872080 1 SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRHNFTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ 9PFI,9PFH,9MDQ,8Y7U,8Y7T,8WTI,8R26,8R19,8R0V,8HOZ,8HOM,8HOL,8HHU,8DI3,7TVX,7TVS,7TOB,7TLL Replicase polyprotein 1a R1A_SARS2 P0DTC1 1539393 Cn1cc2cc(c(cc2n1)Cl)NC3=NC(=O)N(C(=O)N3Cc4cc(c(cc4F)F)F)Cc5ncn(n5)C InChI=1S/C22H17ClF3N9O2/c1-32-7-12-4-18(13(23)5-17(12)30-32)28-20-29-21(36)35(9-19-27-10-33(2)31-19)22(37)34(20)8-11-3-15(25)16(26)6-14(11)24/h3-7,10H,8-9H2,1-2H3,(H,28,29,36) QMPBBNUOBOFBFS-UHFFFAOYSA-N 639154 US20230391736, Example S-217622::US20250025459, Compound I-005::US20250127788, Compound I-005::US20250188102, Compound CVL201 Replicase polyprotein 1a [P3395H] 55.0 US Patent 10.7270/Q2S46XJR US20250188102 SHEN, X; HUANG, J 6/12/2025 10/7/2025 Jkt Biopharma Co. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=639154 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1985&target=Replicase+polyprotein+1a+%5BP3395H%5D&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=639154&enzyme=Replicase+polyprotein+1a+%5BP3395H%5D&column=ki&startPg=0&Increment=50&submit=Search 7YY 7VU6,8DZ0,8DZ1,8H3G,8H3K,8H3L,8HBK,8HEF,8HOM,8HUR,8HUS,8HUT,8HUU,8HUV,8HUW,8HUX,8INX,8INY,8V8E,8V8G,9CJQ,9CJR,9CMS,9CMU,9N6P,9N6R 170795177 488872080 1 SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRHNFTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ 9PFI,9PFH,9MDQ,8Y7U,8Y7T,8WTI,8R26,8R19,8R0V,8HOZ,8HOM,8HOL,8HHU,8DI3,7TVX,7TVS,7TOB,7TLL Replicase polyprotein 1a R1A_SARS2 P0DTC1 1539393 Cn1cc2cc(c(cc2n1)Cl)NC3=NC(=O)N(C(=O)N3Cc4cc(c(cc4F)F)F)Cc5ncn(n5)C InChI=1S/C22H17ClF3N9O2/c1-32-7-12-4-18(13(23)5-17(12)30-32)28-20-29-21(36)35(9-19-27-10-33(2)31-19)22(37)34(20)8-11-3-15(25)16(26)6-14(11)24/h3-7,10H,8-9H2,1-2H3,(H,28,29,36) QMPBBNUOBOFBFS-UHFFFAOYSA-N 639154 US20230391736, Example S-217622::US20250025459, Compound I-005::US20250127788, Compound I-005::US20250188102, Compound CVL201 Replicase polyprotein 1a [P3395H] 55.0 US Patent 10.7270/Q2S46XJR US20250188102 SHEN, X; HUANG, J 6/12/2025 10/7/2025 Jkt Biopharma Co. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=639154 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1985&target=Replicase+polyprotein+1a+%5BP3395H%5D&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=639154&enzyme=Replicase+polyprotein+1a+%5BP3395H%5D&column=ki&startPg=0&Increment=50&submit=Search 7YY 7VU6,8DZ0,8DZ1,8H3G,8H3K,8H3L,8HBK,8HEF,8HOM,8HUR,8HUS,8HUT,8HUU,8HUV,8HUW,8HUX,8INX,8INY,8V8E,8V8G,9CJQ,9CJR,9CMS,9CMU,9N6P,9N6R 170795177 488872080 1 SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRHNFTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ 9PFI,9PFH,9MDQ,8Y7U,8Y7T,8WTI,8R26,8R19,8R0V,8HOZ,8HOM,8HOL,8HHU,8DI3,7TVX,7TVS,7TOB,7TLL Replicase polyprotein 1a R1A_SARS2 P0DTC1 50880570 CS(=O)(=O)c1ccc(c(c1COCC(F)(F)F)Cl)C(=O)C2C(=O)CCCC2=O InChI=1S/C17H16ClF3O6S/c1-28(25,26)13-6-5-9(15(18)10(13)7-27-8-17(19,20)21)16(24)14-11(22)3-2-4-12(14)23/h5-6,14H,2-4,7-8H2,1H3 IUQAXCIUEPFPSF-UHFFFAOYSA-N 50264336 TEMBOTRIONE 4-hydroxyphenylpyruvate dioxygenase Arabidopsis thaliana 13 ChEMBL 10.1021/acs.jmedchem.6b01395 10.7270/Q2FN18ND 28128559 Santucci, A; Bernardini, G; Braconi, D; Petricci, E; Manetti, F 5/25/2017 2/4/2020 University of Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50264336 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50007530&target=4-hydroxyphenylpyruvate+dioxygenase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50264336&enzyme=4-hydroxyphenylpyruvate+dioxygenase&column=ki&startPg=0&Increment=50&submit=Search A1I7G 9QMF,9QMY 11556911 404341808 1 MGHQNAAVSENQNHDDGAASSPGFKLVGFSKFVRKNPKSDKFKVKRFHHIEFWCGDATNVARRFSWGLGMRFSAKSDLSTGNMVHASYLLTSGDLRFLFTAPYSPSLSAGEIKPTTTASIPSFDHGSCRSFFSSHGLGVRAVAIEVEDAESAFSISVANGAIPSSPPIVLNEAVTIAEVKLYGDVVLRYVSYKAEDTEKSEFLPGFERVEDASSFPLDYGIRRLDHAVGNVPELGPALTYVAGFTGFHQFAEFTADDVGTAESGLNSAVLASNDEMVLLPINEPVHGTKRKSQIQTYLEHNEGAGLQHLALMSEDIFRTLREMRKRSSIGGFDFMPSPPPTYYQNLKKRVGDVLSDDQIKECEELGILVDRDDQGTLLQIFTKPLGDRPTIFIEIIQRVGCMMKDEEGKAYQSGGCGGFGKGNFSELFKSIEEYEKTLEAKQLVG 7CJK,6M6D,6LGT,6JX9,6J63,6ISD,5YY7,5YWK,5YWH,5YWG,5XGK,1SP9,9KOZ,1TG5,1TFZ,1SQD,5YY6,5YWI,8XUG,8XUE,8XUC,8XU9,8XR0,8XQZ,8XQY,8XLY,8XLX,8XLW,8XIN,8XII,8XIB,8XHJ,8X6C,8X6A,8X69,8X68,8X5C,8X42,8WQM,8WPD,8WPC,8WL0,8WI6,8WHQ,8WHP,8WHO,8J8X,8J8W,8J3C,8IOK,8I2P,8I15,8I0Y,8I0G,8HZU,8HZ9,8HZ7,8HZ6,8HYS,8HYP,8HYM,8HXH,8HXG,8HXF,8HX4,8HX2,8HWR,8HOW,8H6B,8H6A,8GWD,7XVH,7X8I,7X8H,7X8D,7X6N,7X6M,7X69,7X67,7X64,7X62,7X5Z,7X5Y,7X5X,7X5W,7X5U,7X5S,7X5R,7WJK,7WJJ,7WJ8,7VC8,7V6X,9QMZ,9QMY,9QMX,9QMW,9QMV,9QMU,9QMT,7VO8,7E0X,8XQV,9JS2,9JHU,7CQR,7CQS 4-hydroxyphenylpyruvate dioxygenase HPPD_ARATH P93836 F4IDP1 O04330 Q9SHK1 50880574 CS(=O)(=O)c1ccc(c(c1)Cl)C(=O)C2C(=O)CCCC2=O InChI=1S/C14H13ClO5S/c1-21(19,20)8-5-6-9(10(15)7-8)14(18)13-11(16)3-2-4-12(13)17/h5-7,13H,2-4H2,1H3 PQTBTIFWAXVEPB-UHFFFAOYSA-N 50075318 2-(2-Chloro-4-methanesulfonyl-benzoyl)-3-hydroxy-cyclohex-2-enone::CHEMBL73467 4-hydroxyphenylpyruvate dioxygenase Arabidopsis thaliana 250 ChEMBL 10.1021/acs.jmedchem.6b01395 10.7270/Q2FN18ND 28128559 Santucci, A; Bernardini, G; Braconi, D; Petricci, E; Manetti, F 5/25/2017 2/4/2020 University of Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50075318 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50007530&target=4-hydroxyphenylpyruvate+dioxygenase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50075318&enzyme=4-hydroxyphenylpyruvate+dioxygenase&column=ki&startPg=0&Increment=50&submit=Search 5BQ 6ISD 91760 103968461 CHEMBL73467 1 MGHQNAAVSENQNHDDGAASSPGFKLVGFSKFVRKNPKSDKFKVKRFHHIEFWCGDATNVARRFSWGLGMRFSAKSDLSTGNMVHASYLLTSGDLRFLFTAPYSPSLSAGEIKPTTTASIPSFDHGSCRSFFSSHGLGVRAVAIEVEDAESAFSISVANGAIPSSPPIVLNEAVTIAEVKLYGDVVLRYVSYKAEDTEKSEFLPGFERVEDASSFPLDYGIRRLDHAVGNVPELGPALTYVAGFTGFHQFAEFTADDVGTAESGLNSAVLASNDEMVLLPINEPVHGTKRKSQIQTYLEHNEGAGLQHLALMSEDIFRTLREMRKRSSIGGFDFMPSPPPTYYQNLKKRVGDVLSDDQIKECEELGILVDRDDQGTLLQIFTKPLGDRPTIFIEIIQRVGCMMKDEEGKAYQSGGCGGFGKGNFSELFKSIEEYEKTLEAKQLVG 7CJK,6M6D,6LGT,6JX9,6J63,6ISD,5YY7,5YWK,5YWH,5YWG,5XGK,1SP9,9KOZ,1TG5,1TFZ,1SQD,5YY6,5YWI,8XUG,8XUE,8XUC,8XU9,8XR0,8XQZ,8XQY,8XLY,8XLX,8XLW,8XIN,8XII,8XIB,8XHJ,8X6C,8X6A,8X69,8X68,8X5C,8X42,8WQM,8WPD,8WPC,8WL0,8WI6,8WHQ,8WHP,8WHO,8J8X,8J8W,8J3C,8IOK,8I2P,8I15,8I0Y,8I0G,8HZU,8HZ9,8HZ7,8HZ6,8HYS,8HYP,8HYM,8HXH,8HXG,8HXF,8HX4,8HX2,8HWR,8HOW,8H6B,8H6A,8GWD,7XVH,7X8I,7X8H,7X8D,7X6N,7X6M,7X69,7X67,7X64,7X62,7X5Z,7X5Y,7X5X,7X5W,7X5U,7X5S,7X5R,7WJK,7WJJ,7WJ8,7VC8,7V6X,7VO8,7E0X,8XQV,9JS2,9JHU,7CQR,7CQS 4-hydroxyphenylpyruvate dioxygenase HPPD_ARATH P93836 F4IDP1 O04330 Q9SHK1 50880574 CS(=O)(=O)c1ccc(c(c1)Cl)C(=O)C2C(=O)CCCC2=O InChI=1S/C14H13ClO5S/c1-21(19,20)8-5-6-9(10(15)7-8)14(18)13-11(16)3-2-4-12(13)17/h5-7,13H,2-4H2,1H3 PQTBTIFWAXVEPB-UHFFFAOYSA-N 50075318 2-(2-Chloro-4-methanesulfonyl-benzoyl)-3-hydroxy-cyclohex-2-enone::CHEMBL73467 4-hydroxyphenylpyruvate dioxygenase Arabidopsis thaliana 250 ChEMBL 10.1021/acs.jmedchem.6b01395 10.7270/Q2FN18ND 28128559 Santucci, A; Bernardini, G; Braconi, D; Petricci, E; Manetti, F 5/25/2017 2/4/2020 University of Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50075318 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50007530&target=4-hydroxyphenylpyruvate+dioxygenase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50075318&enzyme=4-hydroxyphenylpyruvate+dioxygenase&column=ki&startPg=0&Increment=50&submit=Search 5BQ 6ISD 91760 103968461 CHEMBL73467 1 MGHQNAAVSENQNHDDGAASSPGFKLVGFSKFVRKNPKSDKFKVKRFHHIEFWCGDATNVARRFSWGLGMRFSAKSDLSTGNMVHASYLLTSGDLRFLFTAPYSPSLSAGEIKPTTTASIPSFDHGSCRSFFSSHGLGVRAVAIEVEDAESAFSISVANGAIPSSPPIVLNEAVTIAEVKLYGDVVLRYVSYKAEDTEKSEFLPGFERVEDASSFPLDYGIRRLDHAVGNVPELGPALTYVAGFTGFHQFAEFTADDVGTAESGLNSAVLASNDEMVLLPINEPVHGTKRKSQIQTYLEHNEGAGLQHLALMSEDIFRTLREMRKRSSIGGFDFMPSPPPTYYQNLKKRVGDVLSDDQIKECEELGILVDRDDQGTLLQIFTKPLGDRPTIFIEIIQRVGCMMKDEEGKAYQSGGCGGFGKGNFSELFKSIEEYEKTLEAKQLVG 7CJK,6M6D,6LGT,6JX9,6J63,6ISD,5YY7,5YWK,5YWH,5YWG,5XGK,1SP9,9KOZ,1TG5,1TFZ,1SQD,5YY6,5YWI,8XUG,8XUE,8XUC,8XU9,8XR0,8XQZ,8XQY,8XLY,8XLX,8XLW,8XIN,8XII,8XIB,8XHJ,8X6C,8X6A,8X69,8X68,8X5C,8X42,8WQM,8WPD,8WPC,8WL0,8WI6,8WHQ,8WHP,8WHO,8J8X,8J8W,8J3C,8IOK,8I2P,8I15,8I0Y,8I0G,8HZU,8HZ9,8HZ7,8HZ6,8HYS,8HYP,8HYM,8HXH,8HXG,8HXF,8HX4,8HX2,8HWR,8HOW,8H6B,8H6A,8GWD,7XVH,7X8I,7X8H,7X8D,7X6N,7X6M,7X69,7X67,7X64,7X62,7X5Z,7X5Y,7X5X,7X5W,7X5U,7X5S,7X5R,7WJK,7WJJ,7WJ8,7VC8,7V6X,7VO8,7E0X,8XQV,9JS2,9JHU,7CQR,7CQS 4-hydroxyphenylpyruvate dioxygenase HPPD_ARATH P93836 F4IDP1 O04330 Q9SHK1 122677 C[C@H]1C[C@@H](C(=O)[C@@H](C1)[C@@H](CC2CC(=O)NC(=O)C2)O)C InChI=1S/C15H23NO4/c1-8-3-9(2)15(20)11(4-8)12(17)5-10-6-13(18)16-14(19)7-10/h8-12,17H,3-7H2,1-2H3,(H,16,18,19) YPHMISFOHDHNIV-UHFFFAOYSA-N 50080528 Cycloheximid::3-((R)-2-((1S,3S,5S)-3,5-dimethyl-2-oxocyclohexyl)-2-hydroxyethyl)glutarimide::CHEMBL123292::cycloheximide::Zykloheximid::cid_6197::4-{(2R)-2-[(1S,3S,5S)-3,5-dimethyl-2-oxocyclohexyl]-2-hydroxyethyl}piperidine-2,6-dione::med.21724, Compound Cycloheximide 60S ribosomal protein L19-A Saccharomyces cerevisiae (strain ATCC 204508 / S288c) 644 PubChem 10.7270/Q2JQ0ZGP aid2740 PubChem, PC 4/1/2010 7/11/2011 Nmmlsc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50080528 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4787&target=60S+ribosomal+protein+L19-A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50080528&enzyme=60S+ribosomal+protein+L19-A&column=ki&startPg=0&Increment=50&submit=Search 3HE 4U3U,5GAK,5LKS,6HD7,6TNU,6Y0G,6Y2L,7N8B,7Q08,7R81,8BN3,8G6J,8IPA,8IPB,8T2X,8T2Y,8T2Z,8T30,8UT0,8UTI,9BH5,9CAI,9FQZ,9P7F,9P7G,9P7H,9P7I,9P7J,9P8I 6197 103980685 CHEMBL123292 C06685 1 MANLRTQKRLAASVVGVGKRKVWLDPNETSEIAQANSRNAIRKLVKNGTIVKKAVTVHSKSRTRAHAQSKREGRHSGYGKRKGTREARLPSQVVWIRRLRVLRRLLAKYRDAGKIDKHLYHVLYKESKGNAFKHKRALVEHIIQAKADAQREKALNEEAEARRLKNRAARDRRAQRVAEKRDALLKEDA 9R9P,9R9O,9PN5,9F9S,9DP7,9DOV,8Y0U,8V87,8T3F,8T3E,8T3D,8T3C,8T3B,8T3A,8T30,8T2Z,8T2Y,8T2X,8PNN,8PFR,8P9A,8P8U,8P8N,8P8M,8P85,8P4V,8K82,8K2D,8HFR,8EWC,8EWB,8EVT,8EVS,8EVR,8EVQ,8EVP,8EUB,8CMJ,8CKU,8CIV,8CGN,8CG8,8CF5,8CEH,8CDR,8CDL,8CCS,8AGZ,8AGX,8AGW,8AGV,8AGU,8AGT,8AAF,7ZW0,7Z34,7V08,7UQZ,7UQB,7UOO,7UG6,7U0H,7TOP,7TOO,7RR5,7R7A,7R72,7OHV,7OHR,7OHQ,7OH3,7OF1,7NAD,7NAC,7BTB,7BT6,7AZY,6Z6K,6Z6J,6YLY,6YLX,6YLH,6YLG,6XIR,6XIQ,6T83,6T7I,6SV4,6S05,6RZZ,6RI5,6QTZ,6QT0,6QIK,6N8L,6N8K,6N8J,6M62,6HHQ,6HD7,6FT6,6EM5,6ELZ,5MC6,5JUU,5JUT,5JUS,5JUP,5JUO,5JCS,5H4P,5GAK,5APO,5APN,4V91,4V8T,4V88,4V7R,4V7F,4V6I,3JCT,2WWB,2WWA,2WW9,8ZHC,8ZHB,8ZH3,8ZGY,8ZGR,8Z71,8Z70,8YLR,8YLD,8XU8,8UTI,8UT0,8BQX,8BQD,8BN3,8BJQ,8BIP,7ZUX,7ZUW,7ZRS,7ZPQ,7NRD,7NRC,7N8B,7MPJ,7MPI,7B7D,6WOO,6TNU,6TB3,6T7T,6T4Q,6S47,6Q8Y,6OIG,6I7O,6GQV,6GQB,6GQ1,5TGM,5TGA,5TBW,5ON6,5OBM,5NDW,5NDV,5NDG,5MEI,5M1J,5LYB,5I4L,5FCJ,5FCI,5DGV,5DGF,5DGE,5DC3,5DAT,4V8Z,4V8Y,4U6F,4U56,4U55,4U53,4U52,4U51,4U50,4U4Z,4U4Y,4U4U,4U4R,4U4Q,4U4O,4U4N,4U3U,4U3N,4U3M,7ZS5,6R87,6R86,6R84,4V4B,4V7H Large ribosomal subunit protein eL19A RL19A_YEAST P0CX82 D6VPX3 P05735 122677 C[C@H]1C[C@@H](C(=O)[C@@H](C1)[C@@H](CC2CC(=O)NC(=O)C2)O)C InChI=1S/C15H23NO4/c1-8-3-9(2)15(20)11(4-8)12(17)5-10-6-13(18)16-14(19)7-10/h8-12,17H,3-7H2,1-2H3,(H,16,18,19) YPHMISFOHDHNIV-UHFFFAOYSA-N 50080528 Cycloheximid::3-((R)-2-((1S,3S,5S)-3,5-dimethyl-2-oxocyclohexyl)-2-hydroxyethyl)glutarimide::CHEMBL123292::cycloheximide::Zykloheximid::cid_6197::4-{(2R)-2-[(1S,3S,5S)-3,5-dimethyl-2-oxocyclohexyl]-2-hydroxyethyl}piperidine-2,6-dione::med.21724, Compound Cycloheximide 60S ribosomal protein L19-A Saccharomyces cerevisiae (strain ATCC 204508 / S288c) 644 PubChem 10.7270/Q2JQ0ZGP aid2740 PubChem, PC 4/1/2010 7/11/2011 Nmmlsc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50080528 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4787&target=60S+ribosomal+protein+L19-A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50080528&enzyme=60S+ribosomal+protein+L19-A&column=ki&startPg=0&Increment=50&submit=Search 3HE 4U3U,5GAK,5LKS,6HD7,6TNU,6Y0G,6Y2L,7N8B,7Q08,7R81,8BN3,8G6J,8IPA,8IPB,8T2X,8T2Y,8T2Z,8T30,8UT0,8UTI,9BH5,9CAI,9FQZ,9P7F,9P7G,9P7H,9P7I,9P7J,9P8I 6197 103980685 CHEMBL123292 C06685 1 MANLRTQKRLAASVVGVGKRKVWLDPNETSEIAQANSRNAIRKLVKNGTIVKKAVTVHSKSRTRAHAQSKREGRHSGYGKRKGTREARLPSQVVWIRRLRVLRRLLAKYRDAGKIDKHLYHVLYKESKGNAFKHKRALVEHIIQAKADAQREKALNEEAEARRLKNRAARDRRAQRVAEKRDALLKEDA 9R9P,9R9O,9PN5,9F9S,9DP7,9DOV,8Y0U,8V87,8T3F,8T3E,8T3D,8T3C,8T3B,8T3A,8T30,8T2Z,8T2Y,8T2X,8PNN,8PFR,8P9A,8P8U,8P8N,8P8M,8P85,8P4V,8K82,8K2D,8HFR,8EWC,8EWB,8EVT,8EVS,8EVR,8EVQ,8EVP,8EUB,8CMJ,8CKU,8CIV,8CGN,8CG8,8CF5,8CEH,8CDR,8CDL,8CCS,8AGZ,8AGX,8AGW,8AGV,8AGU,8AGT,8AAF,7ZW0,7Z34,7V08,7UQZ,7UQB,7UOO,7UG6,7U0H,7TOP,7TOO,7RR5,7R7A,7R72,7OHV,7OHR,7OHQ,7OH3,7OF1,7NAD,7NAC,7BTB,7BT6,7AZY,6Z6K,6Z6J,6YLY,6YLX,6YLH,6YLG,6XIR,6XIQ,6T83,6T7I,6SV4,6S05,6RZZ,6RI5,6QTZ,6QT0,6QIK,6N8L,6N8K,6N8J,6M62,6HHQ,6HD7,6FT6,6EM5,6ELZ,5MC6,5JUU,5JUT,5JUS,5JUP,5JUO,5JCS,5H4P,5GAK,5APO,5APN,4V91,4V8T,4V88,4V7R,4V7F,4V6I,3JCT,2WWB,2WWA,2WW9,8ZHC,8ZHB,8ZH3,8ZGY,8ZGR,8Z71,8Z70,8YLR,8YLD,8XU8,8UTI,8UT0,8BQX,8BQD,8BN3,8BJQ,8BIP,7ZUX,7ZUW,7ZRS,7ZPQ,7NRD,7NRC,7N8B,7MPJ,7MPI,7B7D,6WOO,6TNU,6TB3,6T7T,6T4Q,6S47,6Q8Y,6OIG,6I7O,6GQV,6GQB,6GQ1,5TGM,5TGA,5TBW,5ON6,5OBM,5NDW,5NDV,5NDG,5MEI,5M1J,5LYB,5I4L,5FCJ,5FCI,5DGV,5DGF,5DGE,5DC3,5DAT,4V8Z,4V8Y,4U6F,4U56,4U55,4U53,4U52,4U51,4U50,4U4Z,4U4Y,4U4U,4U4R,4U4Q,4U4O,4U4N,4U3U,4U3N,4U3M,7ZS5,6R87,6R86,6R84,4V4B,4V7H Large ribosomal subunit protein eL19A RL19A_YEAST P0CX82 D6VPX3 P05735 122677 C[C@H]1C[C@@H](C(=O)[C@@H](C1)[C@@H](CC2CC(=O)NC(=O)C2)O)C InChI=1S/C15H23NO4/c1-8-3-9(2)15(20)11(4-8)12(17)5-10-6-13(18)16-14(19)7-10/h8-12,17H,3-7H2,1-2H3,(H,16,18,19) YPHMISFOHDHNIV-UHFFFAOYSA-N 50080528 Cycloheximid::3-((R)-2-((1S,3S,5S)-3,5-dimethyl-2-oxocyclohexyl)-2-hydroxyethyl)glutarimide::CHEMBL123292::cycloheximide::Zykloheximid::cid_6197::4-{(2R)-2-[(1S,3S,5S)-3,5-dimethyl-2-oxocyclohexyl]-2-hydroxyethyl}piperidine-2,6-dione::med.21724, Compound Cycloheximide 60S ribosomal protein L19-A Saccharomyces cerevisiae (strain ATCC 204508 / S288c) 644 PubChem 10.7270/Q2JQ0ZGP aid2740 PubChem, PC 4/1/2010 7/11/2011 Nmmlsc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50080528 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4787&target=60S+ribosomal+protein+L19-A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50080528&enzyme=60S+ribosomal+protein+L19-A&column=ki&startPg=0&Increment=50&submit=Search 3HE 4U3U,5GAK,5LKS,6HD7,6TNU,6Y0G,6Y2L,7N8B,7Q08,7R81,8BN3,8G6J,8IPA,8IPB,8T2X,8T2Y,8T2Z,8T30,8UT0,8UTI,9BH5,9CAI,9FQZ,9P7F,9P7G,9P7H,9P7I,9P7J,9P8I 6197 103980685 CHEMBL123292 C06685 1 MANLRTQKRLAASVVGVGKRKVWLDPNETSEIAQANSRNAIRKLVKNGTIVKKAVTVHSKSRTRAHAQSKREGRHSGYGKRKGTREARLPSQVVWIRRLRVLRRLLAKYRDAGKIDKHLYHVLYKESKGNAFKHKRALVEHIIQAKADAQREKALNEEAEARRLKNRAARDRRAQRVAEKRDALLKEDA 9R9P,9R9O,9PN5,9F9S,9DP7,9DOV,8Y0U,8V87,8T3F,8T3E,8T3D,8T3C,8T3B,8T3A,8T30,8T2Z,8T2Y,8T2X,8PNN,8PFR,8P9A,8P8U,8P8N,8P8M,8P85,8P4V,8K82,8K2D,8HFR,8EWC,8EWB,8EVT,8EVS,8EVR,8EVQ,8EVP,8EUB,8CMJ,8CKU,8CIV,8CGN,8CG8,8CF5,8CEH,8CDR,8CDL,8CCS,8AGZ,8AGX,8AGW,8AGV,8AGU,8AGT,8AAF,7ZW0,7Z34,7V08,7UQZ,7UQB,7UOO,7UG6,7U0H,7TOP,7TOO,7RR5,7R7A,7R72,7OHV,7OHR,7OHQ,7OH3,7OF1,7NAD,7NAC,7BTB,7BT6,7AZY,6Z6K,6Z6J,6YLY,6YLX,6YLH,6YLG,6XIR,6XIQ,6T83,6T7I,6SV4,6S05,6RZZ,6RI5,6QTZ,6QT0,6QIK,6N8L,6N8K,6N8J,6M62,6HHQ,6HD7,6FT6,6EM5,6ELZ,5MC6,5JUU,5JUT,5JUS,5JUP,5JUO,5JCS,5H4P,5GAK,5APO,5APN,4V91,4V8T,4V88,4V7R,4V7F,4V6I,3JCT,2WWB,2WWA,2WW9,8ZHC,8ZHB,8ZH3,8ZGY,8ZGR,8Z71,8Z70,8YLR,8YLD,8XU8,8UTI,8UT0,8BQX,8BQD,8BN3,8BJQ,8BIP,7ZUX,7ZUW,7ZRS,7ZPQ,7NRD,7NRC,7N8B,7MPJ,7MPI,7B7D,6WOO,6TNU,6TB3,6T7T,6T4Q,6S47,6Q8Y,6OIG,6I7O,6GQV,6GQB,6GQ1,5TGM,5TGA,5TBW,5ON6,5OBM,5NDW,5NDV,5NDG,5MEI,5M1J,5LYB,5I4L,5FCJ,5FCI,5DGV,5DGF,5DGE,5DC3,5DAT,4V8Z,4V8Y,4U6F,4U56,4U55,4U53,4U52,4U51,4U50,4U4Z,4U4Y,4U4U,4U4R,4U4Q,4U4O,4U4N,4U3U,4U3N,4U3M,7ZS5,6R87,6R86,6R84,4V4B,4V7H Large ribosomal subunit protein eL19A RL19A_YEAST P0CX82 D6VPX3 P05735 122677 C[C@H]1C[C@@H](C(=O)[C@@H](C1)[C@@H](CC2CC(=O)NC(=O)C2)O)C InChI=1S/C15H23NO4/c1-8-3-9(2)15(20)11(4-8)12(17)5-10-6-13(18)16-14(19)7-10/h8-12,17H,3-7H2,1-2H3,(H,16,18,19) YPHMISFOHDHNIV-UHFFFAOYSA-N 50080528 Cycloheximid::3-((R)-2-((1S,3S,5S)-3,5-dimethyl-2-oxocyclohexyl)-2-hydroxyethyl)glutarimide::CHEMBL123292::cycloheximide::Zykloheximid::cid_6197::4-{(2R)-2-[(1S,3S,5S)-3,5-dimethyl-2-oxocyclohexyl]-2-hydroxyethyl}piperidine-2,6-dione::med.21724, Compound Cycloheximide 60S ribosomal protein L19-A Saccharomyces cerevisiae (strain ATCC 204508 / S288c) 644 PubChem 10.7270/Q2JQ0ZGP aid2740 PubChem, PC 4/1/2010 7/11/2011 Nmmlsc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50080528 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4787&target=60S+ribosomal+protein+L19-A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50080528&enzyme=60S+ribosomal+protein+L19-A&column=ki&startPg=0&Increment=50&submit=Search 3HE 4U3U,5GAK,5LKS,6HD7,6TNU,6Y0G,6Y2L,7N8B,7Q08,7R81,8BN3,8G6J,8IPA,8IPB,8T2X,8T2Y,8T2Z,8T30,8UT0,8UTI,9BH5,9CAI,9FQZ,9P7F,9P7G,9P7H,9P7I,9P7J,9P8I 6197 103980685 CHEMBL123292 C06685 1 MANLRTQKRLAASVVGVGKRKVWLDPNETSEIAQANSRNAIRKLVKNGTIVKKAVTVHSKSRTRAHAQSKREGRHSGYGKRKGTREARLPSQVVWIRRLRVLRRLLAKYRDAGKIDKHLYHVLYKESKGNAFKHKRALVEHIIQAKADAQREKALNEEAEARRLKNRAARDRRAQRVAEKRDALLKEDA 9R9P,9R9O,9PN5,9F9S,9DP7,9DOV,8Y0U,8V87,8T3F,8T3E,8T3D,8T3C,8T3B,8T3A,8T30,8T2Z,8T2Y,8T2X,8PNN,8PFR,8P9A,8P8U,8P8N,8P8M,8P85,8P4V,8K82,8K2D,8HFR,8EWC,8EWB,8EVT,8EVS,8EVR,8EVQ,8EVP,8EUB,8CMJ,8CKU,8CIV,8CGN,8CG8,8CF5,8CEH,8CDR,8CDL,8CCS,8AGZ,8AGX,8AGW,8AGV,8AGU,8AGT,8AAF,7ZW0,7Z34,7V08,7UQZ,7UQB,7UOO,7UG6,7U0H,7TOP,7TOO,7RR5,7R7A,7R72,7OHV,7OHR,7OHQ,7OH3,7OF1,7NAD,7NAC,7BTB,7BT6,7AZY,6Z6K,6Z6J,6YLY,6YLX,6YLH,6YLG,6XIR,6XIQ,6T83,6T7I,6SV4,6S05,6RZZ,6RI5,6QTZ,6QT0,6QIK,6N8L,6N8K,6N8J,6M62,6HHQ,6HD7,6FT6,6EM5,6ELZ,5MC6,5JUU,5JUT,5JUS,5JUP,5JUO,5JCS,5H4P,5GAK,5APO,5APN,4V91,4V8T,4V88,4V7R,4V7F,4V6I,3JCT,2WWB,2WWA,2WW9,8ZHC,8ZHB,8ZH3,8ZGY,8ZGR,8Z71,8Z70,8YLR,8YLD,8XU8,8UTI,8UT0,8BQX,8BQD,8BN3,8BJQ,8BIP,7ZUX,7ZUW,7ZRS,7ZPQ,7NRD,7NRC,7N8B,7MPJ,7MPI,7B7D,6WOO,6TNU,6TB3,6T7T,6T4Q,6S47,6Q8Y,6OIG,6I7O,6GQV,6GQB,6GQ1,5TGM,5TGA,5TBW,5ON6,5OBM,5NDW,5NDV,5NDG,5MEI,5M1J,5LYB,5I4L,5FCJ,5FCI,5DGV,5DGF,5DGE,5DC3,5DAT,4V8Z,4V8Y,4U6F,4U56,4U55,4U53,4U52,4U51,4U50,4U4Z,4U4Y,4U4U,4U4R,4U4Q,4U4O,4U4N,4U3U,4U3N,4U3M,7ZS5,6R87,6R86,6R84,4V4B,4V7H Large ribosomal subunit protein eL19A RL19A_YEAST P0CX82 D6VPX3 P05735 122677 C[C@H]1C[C@@H](C(=O)[C@@H](C1)[C@@H](CC2CC(=O)NC(=O)C2)O)C InChI=1S/C15H23NO4/c1-8-3-9(2)15(20)11(4-8)12(17)5-10-6-13(18)16-14(19)7-10/h8-12,17H,3-7H2,1-2H3,(H,16,18,19) YPHMISFOHDHNIV-UHFFFAOYSA-N 50080528 Cycloheximid::3-((R)-2-((1S,3S,5S)-3,5-dimethyl-2-oxocyclohexyl)-2-hydroxyethyl)glutarimide::CHEMBL123292::cycloheximide::Zykloheximid::cid_6197::4-{(2R)-2-[(1S,3S,5S)-3,5-dimethyl-2-oxocyclohexyl]-2-hydroxyethyl}piperidine-2,6-dione::med.21724, Compound Cycloheximide 60S ribosomal protein L19-A Saccharomyces cerevisiae (strain ATCC 204508 / S288c) 644 PubChem 10.7270/Q2JQ0ZGP aid2740 PubChem, PC 4/1/2010 7/11/2011 Nmmlsc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50080528 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4787&target=60S+ribosomal+protein+L19-A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50080528&enzyme=60S+ribosomal+protein+L19-A&column=ki&startPg=0&Increment=50&submit=Search 3HE 4U3U,5GAK,5LKS,6HD7,6TNU,6Y0G,6Y2L,7N8B,7Q08,7R81,8BN3,8G6J,8IPA,8IPB,8T2X,8T2Y,8T2Z,8T30,8UT0,8UTI,9BH5,9CAI,9FQZ,9P7F,9P7G,9P7H,9P7I,9P7J,9P8I 6197 103980685 CHEMBL123292 C06685 1 MANLRTQKRLAASVVGVGKRKVWLDPNETSEIAQANSRNAIRKLVKNGTIVKKAVTVHSKSRTRAHAQSKREGRHSGYGKRKGTREARLPSQVVWIRRLRVLRRLLAKYRDAGKIDKHLYHVLYKESKGNAFKHKRALVEHIIQAKADAQREKALNEEAEARRLKNRAARDRRAQRVAEKRDALLKEDA 9R9P,9R9O,9PN5,9F9S,9DP7,9DOV,8Y0U,8V87,8T3F,8T3E,8T3D,8T3C,8T3B,8T3A,8T30,8T2Z,8T2Y,8T2X,8PNN,8PFR,8P9A,8P8U,8P8N,8P8M,8P85,8P4V,8K82,8K2D,8HFR,8EWC,8EWB,8EVT,8EVS,8EVR,8EVQ,8EVP,8EUB,8CMJ,8CKU,8CIV,8CGN,8CG8,8CF5,8CEH,8CDR,8CDL,8CCS,8AGZ,8AGX,8AGW,8AGV,8AGU,8AGT,8AAF,7ZW0,7Z34,7V08,7UQZ,7UQB,7UOO,7UG6,7U0H,7TOP,7TOO,7RR5,7R7A,7R72,7OHV,7OHR,7OHQ,7OH3,7OF1,7NAD,7NAC,7BTB,7BT6,7AZY,6Z6K,6Z6J,6YLY,6YLX,6YLH,6YLG,6XIR,6XIQ,6T83,6T7I,6SV4,6S05,6RZZ,6RI5,6QTZ,6QT0,6QIK,6N8L,6N8K,6N8J,6M62,6HHQ,6HD7,6FT6,6EM5,6ELZ,5MC6,5JUU,5JUT,5JUS,5JUP,5JUO,5JCS,5H4P,5GAK,5APO,5APN,4V91,4V8T,4V88,4V7R,4V7F,4V6I,3JCT,2WWB,2WWA,2WW9,8ZHC,8ZHB,8ZH3,8ZGY,8ZGR,8Z71,8Z70,8YLR,8YLD,8XU8,8UTI,8UT0,8BQX,8BQD,8BN3,8BJQ,8BIP,7ZUX,7ZUW,7ZRS,7ZPQ,7NRD,7NRC,7N8B,7MPJ,7MPI,7B7D,6WOO,6TNU,6TB3,6T7T,6T4Q,6S47,6Q8Y,6OIG,6I7O,6GQV,6GQB,6GQ1,5TGM,5TGA,5TBW,5ON6,5OBM,5NDW,5NDV,5NDG,5MEI,5M1J,5LYB,5I4L,5FCJ,5FCI,5DGV,5DGF,5DGE,5DC3,5DAT,4V8Z,4V8Y,4U6F,4U56,4U55,4U53,4U52,4U51,4U50,4U4Z,4U4Y,4U4U,4U4R,4U4Q,4U4O,4U4N,4U3U,4U3N,4U3M,7ZS5,6R87,6R86,6R84,4V4B,4V7H Large ribosomal subunit protein eL19A RL19A_YEAST P0CX82 D6VPX3 P05735 122677 C[C@H]1C[C@@H](C(=O)[C@@H](C1)[C@@H](CC2CC(=O)NC(=O)C2)O)C InChI=1S/C15H23NO4/c1-8-3-9(2)15(20)11(4-8)12(17)5-10-6-13(18)16-14(19)7-10/h8-12,17H,3-7H2,1-2H3,(H,16,18,19) YPHMISFOHDHNIV-UHFFFAOYSA-N 50080528 Cycloheximid::3-((R)-2-((1S,3S,5S)-3,5-dimethyl-2-oxocyclohexyl)-2-hydroxyethyl)glutarimide::CHEMBL123292::cycloheximide::Zykloheximid::cid_6197::4-{(2R)-2-[(1S,3S,5S)-3,5-dimethyl-2-oxocyclohexyl]-2-hydroxyethyl}piperidine-2,6-dione::med.21724, Compound Cycloheximide 60S ribosomal protein L19-A Saccharomyces cerevisiae (strain ATCC 204508 / S288c) 644 PubChem 10.7270/Q2JQ0ZGP aid2740 PubChem, PC 4/1/2010 7/11/2011 Nmmlsc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50080528 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4787&target=60S+ribosomal+protein+L19-A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50080528&enzyme=60S+ribosomal+protein+L19-A&column=ki&startPg=0&Increment=50&submit=Search 3HE 4U3U,5GAK,5LKS,6HD7,6TNU,6Y0G,6Y2L,7N8B,7Q08,7R81,8BN3,8G6J,8IPA,8IPB,8T2X,8T2Y,8T2Z,8T30,8UT0,8UTI,9BH5,9CAI,9FQZ,9P7F,9P7G,9P7H,9P7I,9P7J,9P8I 6197 103980685 CHEMBL123292 C06685 1 MANLRTQKRLAASVVGVGKRKVWLDPNETSEIAQANSRNAIRKLVKNGTIVKKAVTVHSKSRTRAHAQSKREGRHSGYGKRKGTREARLPSQVVWIRRLRVLRRLLAKYRDAGKIDKHLYHVLYKESKGNAFKHKRALVEHIIQAKADAQREKALNEEAEARRLKNRAARDRRAQRVAEKRDALLKEDA 9R9P,9R9O,9PN5,9F9S,9DP7,9DOV,8Y0U,8V87,8T3F,8T3E,8T3D,8T3C,8T3B,8T3A,8T30,8T2Z,8T2Y,8T2X,8PNN,8PFR,8P9A,8P8U,8P8N,8P8M,8P85,8P4V,8K82,8K2D,8HFR,8EWC,8EWB,8EVT,8EVS,8EVR,8EVQ,8EVP,8EUB,8CMJ,8CKU,8CIV,8CGN,8CG8,8CF5,8CEH,8CDR,8CDL,8CCS,8AGZ,8AGX,8AGW,8AGV,8AGU,8AGT,8AAF,7ZW0,7Z34,7V08,7UQZ,7UQB,7UOO,7UG6,7U0H,7TOP,7TOO,7RR5,7R7A,7R72,7OHV,7OHR,7OHQ,7OH3,7OF1,7NAD,7NAC,7BTB,7BT6,7AZY,6Z6K,6Z6J,6YLY,6YLX,6YLH,6YLG,6XIR,6XIQ,6T83,6T7I,6SV4,6S05,6RZZ,6RI5,6QTZ,6QT0,6QIK,6N8L,6N8K,6N8J,6M62,6HHQ,6HD7,6FT6,6EM5,6ELZ,5MC6,5JUU,5JUT,5JUS,5JUP,5JUO,5JCS,5H4P,5GAK,5APO,5APN,4V91,4V8T,4V88,4V7R,4V7F,4V6I,3JCT,2WWB,2WWA,2WW9,8ZHC,8ZHB,8ZH3,8ZGY,8ZGR,8Z71,8Z70,8YLR,8YLD,8XU8,8UTI,8UT0,8BQX,8BQD,8BN3,8BJQ,8BIP,7ZUX,7ZUW,7ZRS,7ZPQ,7NRD,7NRC,7N8B,7MPJ,7MPI,7B7D,6WOO,6TNU,6TB3,6T7T,6T4Q,6S47,6Q8Y,6OIG,6I7O,6GQV,6GQB,6GQ1,5TGM,5TGA,5TBW,5ON6,5OBM,5NDW,5NDV,5NDG,5MEI,5M1J,5LYB,5I4L,5FCJ,5FCI,5DGV,5DGF,5DGE,5DC3,5DAT,4V8Z,4V8Y,4U6F,4U56,4U55,4U53,4U52,4U51,4U50,4U4Z,4U4Y,4U4U,4U4R,4U4Q,4U4O,4U4N,4U3U,4U3N,4U3M,7ZS5,6R87,6R86,6R84,4V4B,4V7H Large ribosomal subunit protein eL19A RL19A_YEAST P0CX82 D6VPX3 P05735 122677 C[C@H]1C[C@@H](C(=O)[C@@H](C1)[C@@H](CC2CC(=O)NC(=O)C2)O)C InChI=1S/C15H23NO4/c1-8-3-9(2)15(20)11(4-8)12(17)5-10-6-13(18)16-14(19)7-10/h8-12,17H,3-7H2,1-2H3,(H,16,18,19) YPHMISFOHDHNIV-UHFFFAOYSA-N 50080528 Cycloheximid::3-((R)-2-((1S,3S,5S)-3,5-dimethyl-2-oxocyclohexyl)-2-hydroxyethyl)glutarimide::CHEMBL123292::cycloheximide::Zykloheximid::cid_6197::4-{(2R)-2-[(1S,3S,5S)-3,5-dimethyl-2-oxocyclohexyl]-2-hydroxyethyl}piperidine-2,6-dione::med.21724, Compound Cycloheximide 60S ribosomal protein L19-A Saccharomyces cerevisiae (strain ATCC 204508 / S288c) 644 PubChem 10.7270/Q2JQ0ZGP aid2740 PubChem, PC 4/1/2010 7/11/2011 Nmmlsc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50080528 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4787&target=60S+ribosomal+protein+L19-A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50080528&enzyme=60S+ribosomal+protein+L19-A&column=ki&startPg=0&Increment=50&submit=Search 3HE 4U3U,5GAK,5LKS,6HD7,6TNU,6Y0G,6Y2L,7N8B,7Q08,7R81,8BN3,8G6J,8IPA,8IPB,8T2X,8T2Y,8T2Z,8T30,8UT0,8UTI,9BH5,9CAI,9FQZ,9P7F,9P7G,9P7H,9P7I,9P7J,9P8I 6197 103980685 CHEMBL123292 C06685 1 MANLRTQKRLAASVVGVGKRKVWLDPNETSEIAQANSRNAIRKLVKNGTIVKKAVTVHSKSRTRAHAQSKREGRHSGYGKRKGTREARLPSQVVWIRRLRVLRRLLAKYRDAGKIDKHLYHVLYKESKGNAFKHKRALVEHIIQAKADAQREKALNEEAEARRLKNRAARDRRAQRVAEKRDALLKEDA 9R9P,9R9O,9PN5,9F9S,9DP7,9DOV,8Y0U,8V87,8T3F,8T3E,8T3D,8T3C,8T3B,8T3A,8T30,8T2Z,8T2Y,8T2X,8PNN,8PFR,8P9A,8P8U,8P8N,8P8M,8P85,8P4V,8K82,8K2D,8HFR,8EWC,8EWB,8EVT,8EVS,8EVR,8EVQ,8EVP,8EUB,8CMJ,8CKU,8CIV,8CGN,8CG8,8CF5,8CEH,8CDR,8CDL,8CCS,8AGZ,8AGX,8AGW,8AGV,8AGU,8AGT,8AAF,7ZW0,7Z34,7V08,7UQZ,7UQB,7UOO,7UG6,7U0H,7TOP,7TOO,7RR5,7R7A,7R72,7OHV,7OHR,7OHQ,7OH3,7OF1,7NAD,7NAC,7BTB,7BT6,7AZY,6Z6K,6Z6J,6YLY,6YLX,6YLH,6YLG,6XIR,6XIQ,6T83,6T7I,6SV4,6S05,6RZZ,6RI5,6QTZ,6QT0,6QIK,6N8L,6N8K,6N8J,6M62,6HHQ,6HD7,6FT6,6EM5,6ELZ,5MC6,5JUU,5JUT,5JUS,5JUP,5JUO,5JCS,5H4P,5GAK,5APO,5APN,4V91,4V8T,4V88,4V7R,4V7F,4V6I,3JCT,2WWB,2WWA,2WW9,8ZHC,8ZHB,8ZH3,8ZGY,8ZGR,8Z71,8Z70,8YLR,8YLD,8XU8,8UTI,8UT0,8BQX,8BQD,8BN3,8BJQ,8BIP,7ZUX,7ZUW,7ZRS,7ZPQ,7NRD,7NRC,7N8B,7MPJ,7MPI,7B7D,6WOO,6TNU,6TB3,6T7T,6T4Q,6S47,6Q8Y,6OIG,6I7O,6GQV,6GQB,6GQ1,5TGM,5TGA,5TBW,5ON6,5OBM,5NDW,5NDV,5NDG,5MEI,5M1J,5LYB,5I4L,5FCJ,5FCI,5DGV,5DGF,5DGE,5DC3,5DAT,4V8Z,4V8Y,4U6F,4U56,4U55,4U53,4U52,4U51,4U50,4U4Z,4U4Y,4U4U,4U4R,4U4Q,4U4O,4U4N,4U3U,4U3N,4U3M,7ZS5,6R87,6R86,6R84,4V4B,4V7H Large ribosomal subunit protein eL19A RL19A_YEAST P0CX82 D6VPX3 P05735 85300 Nc1ncnc2n(cnc12)C1OC(COP(O)(=O)OP(O)(O)=O)C(O)C1O InChI=1S/C10H15N5O10P2/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(24-10)1-23-27(21,22)25-26(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H2,11,12,13)(H2,18,19,20) XTWYTFMLZFPYCI-UHFFFAOYSA-N 50013703 (ADP)[5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl trihydrogen diphosphate::5'-Adenosinediphosphate (5'-ADP)::Adenosine diphosphate::Aenosine 5'-Diphosphate::CHEMBL14830::Diphosphoric acid -[5-(6-amino-purin-9-yl)-3,4-dihydroxy-tetrahydro-furan-2-ylmethyl] ester::cid_16654696::diPhosphoric acid [5-(6-amino-purin-9-yl)-3,4-dihydroxy-tetrahydro-furan-2-ylmethyl] ester Heat shock cognate 71 kDa protein Homo sapiens 280 PubChem 10.7270/Q20G3HKD aid1193 PubChem, PC 3/5/2008 5/28/2011 Sanford-Burnham Center for Chemical Genomics http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50013703 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4692&target=Heat+shock+cognate+71+kDa+protein&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50013703&enzyme=Heat+shock+cognate+71+kDa+protein&column=ki&startPg=0&Increment=50&submit=Search ADP 7X5B,7UT9,7X54,1Y63,8A2T,8A2S,8A2R,7LNX,7LNW,7LNU,7LNT,7LN3,7LN2,7LN1,7LN0,7LN6,7LN5,7LN4,1NG9,1NGD,1NGA,1NGB,1NGC,8EGL,3LTD,3LTB,3LT9,3LT8,1W9J,2ZDG,1W9L,2ZDH,2ZDY,4M15,1IHU,3QVH,3QVF,1G3Q,7SGZ,6JKM,2BU8,2BUP,6K91,2BUF,1NN3,1NN0,4Q4C,6DJN,4BG4,4BGB,4BGA,4BGD,4C12,4NST,1TZD,8AG6,3WXL,1H8H,1H8E,6Z9S,6Z9R,6Z9Q,6Z9P,7LW1,7WBU,1O6B,6I59,3O8N,6I5F,3O8L,7ZTD,3O8R,7RIG,7PMF,8BNS,4XHG,7ABR,3EHH,5KK8,1GKI,7R32,7R30,1W0J,1W0K,3PEY,3PEW,4ARK,5LIH,7A4V,1XMV,7VYS,1YYF,4JKY,4JKI,7JIJ,3H4M,7CRC,4B2Q,1DAM,1G8X,2W58,2W5A,3HBL,3HB9,3K60,3NWN,8DVS,3MBL,3MBI,1UJ2,8DVU,8DAR,4IX4,4IX6,7QV8,7QV9,1Q9S,5T5T,4F7W,4GYI,6FUA,6FUX,1E4E,8G1F,1MO3,7V2F,7V2K,7UKA,7V2R,6D3K,5HE9,5KPZ,7P2Y,7TTN,2PMK,5EC0,1VOM,4XWO,4XW6,2VHU,2VHJ,1QQN,3I33,2DWC,2DWO,2I5B,6NHK,1S4E,2V26,2V2Z,6MT9,3UNG,4V81,4V8R,1RRC,3U06,3DIN,5VZ0,7NPE,4PJM,3NBX,1OL5,1OL7,7D4I,7D4O,5WDE,5WDH,1JDB,1ZAR,3A5C,6ZQM,3RV4,7TTS,3TPT,3FMP,3FMO,7C1Y,1MP8,4Q47,6B5D,5Z3U,5Z3V,5Z3O,6ZO4,7ADD,7ADE,5ELZ,5O7D,4BZQ,4BQS,6NE3,1UC9,1L0O,6L5O,7PX9,1THN,4CJ7,7U9K,1REA,2C2A,5D4N,5D4W,6M5U,6M5V,4NL0,4NL4,7TNE,6VVO,6GFG,3G8C,3G8D,6GQ6,8E3H,7NGP,7NGF,7NGC,7NGA,7NGL,7QIN,7QIM,7KY9,7KYB,5AFU,7KSM,1ZTH,6HD3,6HD0,5GM6,5GME,7DUT,6RKE,7YZO,6FO1,6FOC,1X6V,3IIL,3IIJ,6Z9T,7V2D,5BVC,3L4I,4AM7,2OLC,2OLJ,3ZUH,1NMX,1NMY,3LJ0,1M34,1DFL,8BV0,2HYD,1GSA,2YZL,6KY4,3N83,4GP6,1RDQ,6K7K,6ZYW,6ZYY,6ZYI,4NYE,1SVL,1SVT,5I0I,2QC8,6IUG,6G2W,6G2V,6G2Z,6G2Y,6G2X,6G2J,3JA8,7VLR,6HQU,3JAH,3JAI,3JAG,3FI8,7RSI,7DHW,7ZTC,1Z59,1Z5C,1HPM,6QDJ,6EP2,6EP5,3C4N,7L1R,7L1Q,1N2C,4WW4,4WW0,4WW9,6N30,6OAX,6OAY,6OAB,6OAA,6OA9,4AX8,4AXE,7S61,7S67,1XW4,8CCN,6BIH,7VZ8,3BZ9,3BZ8,7U4T,3IO3,2X7C,2X7E,2X7D,5FL3,5FL7,3QUI,3GBJ,1KSF,6YA7,6YA8,4QOS,5TDF,1QVI,7M74,2IF8,6JJ8,6JJ9,2BTD,6LYM,6LYL,6LYO,6LYK,6LY8,3RER,3RES,6ZNX,1CE8,7TTT,3EH9,6F5D,6OPC,7UDT,7UDU,4GCZ,6IHK,1FNN,3EGI,7AI6,4TLA,2JI6,1O51,7DCP,1VRP,6RU8,6RU7,7ZBH,6N2Y,6CZD,7ZBG,3BF1,2D7D,2IUU,1S3S,1W7K,1W7J,1W78,3PFF,3PFI,4ASU,4AS7,5EVZ,1XJK,1XJQ,3ZOZ,7ZI4,6NR6,2CGL,2CGJ,7JGA,2X86,4JJZ,6T1Y,1XTJ,6C8Z,2W6E,6W17,6W1Z,7U8R,1CZ7,1CZA,1T36,1T3T,8AK3,2F43,4IY0,4IYN,7QUX,2QUR,1Q8Y,4GVY,4GVZ,4GVA,4GVJ,1E79,6FTX,2ZTS,2VAS,8G6P,1TF2,1MND,6CMZ,7UJ0,7UJX,7UJS,7UJP,7TTR,5UFU,7P3N,5KWA,2PL3,5Y5X,5Y5Z,1IQP,5E7P,6NON,6NO5,6NO1,6NO0,6NO3,6NO2,6KLL,6KLN,2V1U,2V1X,3UMM,6V6S,7WZ3,2X6T,6ITC,1U0J,1A9X,6KS6,8E9B,2GM1,7MDM,7MDO,3NCR,3UQD,2WW4,7D5T,2WWI,2WWF,7KW7,5WC2,3R5H,3H4S,1PKG,7DWR,6FAA,3TQC,2FSN,2FSI,7BT7,7BTE,7BTI,7ED9,7ED6,6EOF,6EOE,5TSG,5MOE,8DAV,6B4I,3EQI,3EQH,3EQG,5EOY,5EOX,7FID,7T6F,5LBA,4XCJ,4XCG,6PAM,7PT7,7PT6,1RPZ,6NDY,4CK6,4CK7,4CK5,1LKX,1RFU,2Y83,8DMY,5JRJ,5JR7,6GR2,6GR5,6GRG,4PFK,4PFO,4PFP,1OXU,3SJD,4YSJ,4YS0,4Z9M,3CF0,3CF1,3CF2,3CF3,8SBV,3RTD,6RJ4,3TLX,3KZB,7VW7,5ZI2,3FYH,3IHL,7W1T,7W1V,7W1Y,4ANJ,7W1O,7UTJ,7W0Y,1NNE,7O3W,7O3Z,7O3Y,7O3X,1BR4,1BR2,1BR1,6BS4,6BS3,4NU1,4XHP,4XH0,1DGK,7TUB,7NK7,1R7R,1IAH,7MHS,5YA2,4CVN,7T4H,3DKP,6JDB,6K0R,1LVG,1COW,5ERR,4NXW,4NXU,4IFW,7MU0,8DAS,8DAT,5DRK,7QO6,3J4K,3EC2,6IRO,1ZXN,6G30,6G3R,6G3S,6HPU,8AS8,1EA6,6XLH,1Z6T,7VZW,7VZV,6QEL,6QEM,2IOR,2IOP,2IOA,2IO8,2IO9,6N2I,4WTJ,6N2Z,4WTD,3CJO,5GSZ,4L78,4AY2,6OBY,3B1N,3B1P,1Y8O,2DCN,1NY6,1NY5,1NY3,3LV8,3LVV,7U35,6WQH,5FM7,4ETP,8B6F,4XIV,5YZG,1G18,2Y8Q,2Y8I,2Y8L,6JIM,6JIL,6ZME,6ZM2,3W0O,1F9V,1F9W,1F9T,1F9U,7QO5,7QO4,4IOL,4IOK,4YIX,3W0P,7DRP,3JUX,7K21,5A5F,7S9W,7S9V,8A2Z,8A2Y,8A2U,7F4Z,7F4X,5HLE,6D8C,8G1E,3OAA,3VPC,3VPB,5TTH,3ZL8,2NCD,7RDZ,7RDY,7RDX,4LV7,4LV5,4LV8,2CH6,6ACX,4V1T,3GVI,8H77,1QQM,1QQO,1X3M,6YUF,3U9Z,6W23,6W22,6W21,6W20,6W24,4FFP,6S85,7AI7,3NUA,1EHI,7UK7,3WO1,3WO0,8ATF,4IZ5,6UPW,6UPV,6UP4,6N9L,4F9A,5T3O,4F93,4F99,4GW2,4GW0,6X2F,7AOI,3FD6,1HW8,1HW9,5U3C,1HWL,1HWJ,1HWK,1HWI,3JXU,6OK2,2ECK,5OVO,7YLX,7YLY,7UIX,7UIW,7UIV,2UYT,2UYI,5UIE,5UIV,7SX8,2PO0,1UCN,2VF7,2VF8,3MFP,5EXT,2HMF,2HMV,4U0U,4U0S,7SQ0,3I12,3KIN,4A50,4A51,4A5Y,1VFX,8ET3,4D26,8ETR,1RL9,4EBU,1U3G,1U3F,6VOM,6VOL,6VOO,6VON,6VOI,6VOH,6VOK,6VOJ,6VOG,6VOF,3U60,2XZO,1JBP,3HWS,7LJF,7LJO,2WPD,7D63,6SZB,6SZA,4H7Q,5B7I,1PHP,7VAL,7VAW,6DZG,4XE8,3DSR,7PZC,4KIT,7FJP,4KI8,3LA6,5LU4,2ZWH,2O1V,2HV7,2HVD,7PUX,7U19,1YP4,1WB9,1WBD,1WBB,1WBP,3KB1,5X9U,4UQO,7P3W,1S5G,3A7J,7THV,7THJ,2XOC,4BUB,8E5L 197 103925778 CHEMBL14830 C03517 ZINC08586022 1 MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANGILNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAFNMKATVEDEKLQGKINDEDKQKILDKCNEIINWLDKNQTAEKEEFEHQQKELEKVCNPIITKLYQSAGGMPGGMPGGFPGGGAPPSGGASSGPTIEEVD 1CKR,1HPM,1NGI,1NGJ,2QW9,2QWL,2QWM,2QWN,2QWO,2QWP,2QWQ,2QWR,3C7N,3CQX,3D2E,3D2F,3HSC,3JXU,4H5N,4H5R,4H5T,4H5V,4H5W,4HWI,5AQF,5AQG,5AQH,5AQI,5AQJ,5AQK,5AQN,5AQO,5AQP,5AQQ,5AQR,5AQS,5AQT,5AQU,5AQV,5BN9,5BPL,5XI9,6B1I,6ZYJ,7FGM,7HSC Heat shock cognate 71 kDa protein HSP7C_HUMAN P11142 Q9H3R6 51129389 c1cc(ccc1C[C@@H](C(=O)O)N)O InChI=1S/C9H11NO3/c10-8(9(12)13)5-6-1-3-7(11)4-2-6/h1-4,8,11H,5,10H2,(H,12,13) OUYCCCASQSFEME-UHFFFAOYSA-N 18129 (2S)-2-amino-3-(4-hydroxyphenyl)propanoic acid::L-[U-14C]Tyr::Tyrosine::US11021454, Compound L-tyr::US20240415800, Compound 2-2 (Tyr) Large neutral amino acids transporter small subunit 1 Homo sapiens 68000 ChEMBL 10.1021/acs.jmedchem.8b01007 10.7270/Q2XK8J66 30048132 Chien, HC; Colas, C; Finke, K; Springer, S; Stoner, L; Zur, AA; Venteicher, B; Campbell, J; Hall, C; Flint, A; Augustyn, E; Hernandez, C; Heeren, N; Hansen, L; Anthony, A; Bauer, J; Fotiadis, D; Schlessinger, A; Giacomini, KM; Thomas, AA 8/23/2018 8/17/2020 University of California http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=18129 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50007107&target=Large+neutral+amino+acids+transporter+small+subunit+1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=18129&enzyme=Large+neutral+amino+acids+transporter+small+subunit+1&column=ki&startPg=0&Increment=50&submit=Search TYR 1AHG,1FE1,1J1U,1S2K,1TYA,1TYB,1TYD,1WQ4,1X8X,1Y42,1YXW,2AMC,2BN2,2CSM,2CYB,2CYC,2HNU,2HNV,2PV7,2QAA,2VBY,2WHZ,2XII,2YPP,2YPQ,3B37,3CPA,3GGG,3JW7,3JZU,3K1G,3KDZ,3KUM,3MO4,3O7B,3PG9,3VGJ,3WOL,3WOM,3WON,4CSM,4D56,4GRS,4HSO,4I4T,4OEL,4OJM,4OUD,4P6R,4PPU,4QBT,4R0T,4TS1,4WJI,5CKV,5CKX,5DCD,5IHX,5IJX,5JVO,5M8P,5T95,5T9F,5THH,5UXN,5UYY,6A8Z,6AGM,6BQZ,6EEM,6EYV,6HJW,6HNI,6IFF,6JU7,6JU9,6L1O,6OTJ,6PZ0,6U60,6WJO,6YJY,6YU7,7C3L,7DKB,7DKC,7DKD,7DKE,7KNX,7KQR,7PD1,7QI1,7REU,7RS3,7UX8,7VYS,8DAY,8GRT,8IDA,8X0O,8ZVG,9B10,9DH4,9SDF 6057 172097273 DB00135 C01536 1 MAGAGPKRRALAAPAAEEKEEAREKMLAAKSADGSAPAGEGEGVTLQRNITLLNGVAIIVGTIIGSGIFVTPTGVLKEAGSPGLALVVWAACGVFSIVGALCYAELGTTISKSGGDYAYMLEVYGSLPAFLKLWIELLIIRPSSQYIVALVFATYLLKPLFPTCPVPEEAAKLVACLCVLLLTAVNCYSVKAATRVQDAFAAAKLLALALIILLGFVQIGKGDVSNLDPNFSFEGTKLDVGNIVLALYSGLFAYGGWNYLNFVTEEMINPYRNLPLAIIISLPIVTLVYVLTNLAYFTTLSTEQMLSSEAVAVDFGNYHLGVMSWIIPVFVGLSCFGSVNGSLFTSSRLFFVGSREGHLPSILSMIHPQLLTPVPSLVFTCVMTLLYAFSKDIFSVINFFSFFNWLCVALAIIGMIWLRHRKPELERPIKVNLALPVFFILACLFLIAVSFWKTPVECGIGFTIILSGLPVYFFGVWWKNKPKWLLQGIFSTTVLCQKLMQVVPQET 8KDP,8KDO,8KDN,8KDJ,8KDI,8KDH,8KDG,8KDF,8KDD,6JMQ,8XPU,8J8M,8J8L,8IDA,7DSQ,7DSN,7DSL,7DSK,6IRT,6IRS,8X0W Large neutral amino acids transporter small subunit 1 LAT1_HUMAN Q01650 Q8IV97 Q9UBN8 Q9UP15 Q9UQC0 51129687 c1cc(c(cc1C[C@@H](C(=O)O)N)O)O InChI=1S/C9H11NO4/c10-6(9(13)14)3-5-1-2-7(11)8(12)4-5/h1-2,4,6,11-12H,3,10H2,(H,13,14) WTDRDQBEARUVNC-UHFFFAOYSA-N 60928 L-DOPA::dihydroxyphenylalanine::BDBM50130192::L-3,4-dihydroxyphenylalanine::US11021454, Compound L-dopa::US20240415800, Compound 2-1 (L-DOPA) Large neutral amino acids transporter small subunit 1 Homo sapiens 100000 ChEMBL 10.1016/j.bmcl.2018.07.030 10.7270/Q2WM1H2C 30055889 Thiele, NA; Kärkkäinen, J; Sloan, KB; Rautio, J; Huttunen, KM 9/15/2018 8/17/2020 University of Florida http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=60928 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50007107&target=Large+neutral+amino+acids+transporter+small+subunit+1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=60928&enzyme=Large+neutral+amino+acids+transporter+small+subunit+1&column=ki&startPg=0&Increment=50&submit=Search DAH 1IVV,1RNR,2VH3,2ZWE,2ZWF,2ZWG,3TEG,3TEH,4EIS,4P6S,5XDH,5Z0F,5Z0G,5Z0H,5Z0I,5Z0J,5Z0K,5Z0L,5Z0M,6EBP,6EBZ,6GP2,6JU4,6JU5,6JU9,6ON3,6PAH,8BT3,8BT4,8J8L,8RAH 6047 321900691 DB01235 C00355 1 MAGAGPKRRALAAPAAEEKEEAREKMLAAKSADGSAPAGEGEGVTLQRNITLLNGVAIIVGTIIGSGIFVTPTGVLKEAGSPGLALVVWAACGVFSIVGALCYAELGTTISKSGGDYAYMLEVYGSLPAFLKLWIELLIIRPSSQYIVALVFATYLLKPLFPTCPVPEEAAKLVACLCVLLLTAVNCYSVKAATRVQDAFAAAKLLALALIILLGFVQIGKGDVSNLDPNFSFEGTKLDVGNIVLALYSGLFAYGGWNYLNFVTEEMINPYRNLPLAIIISLPIVTLVYVLTNLAYFTTLSTEQMLSSEAVAVDFGNYHLGVMSWIIPVFVGLSCFGSVNGSLFTSSRLFFVGSREGHLPSILSMIHPQLLTPVPSLVFTCVMTLLYAFSKDIFSVINFFSFFNWLCVALAIIGMIWLRHRKPELERPIKVNLALPVFFILACLFLIAVSFWKTPVECGIGFTIILSGLPVYFFGVWWKNKPKWLLQGIFSTTVLCQKLMQVVPQET 8KDP,8KDO,8KDN,8KDJ,8KDI,8KDH,8KDG,8KDF,8KDD,6JMQ,8XPU,8J8M,8J8L,8IDA,7DSQ,7DSN,7DSL,7DSK,6IRT,6IRS,8X0W Large neutral amino acids transporter small subunit 1 LAT1_HUMAN Q01650 Q8IV97 Q9UBN8 Q9UP15 Q9UQC0 50580123 c1cc(ccc1C[C@@H](C(=O)O)N)N(CCCl)CCCl InChI=1S/C13H18Cl2N2O2/c14-5-7-17(8-6-15)11-3-1-10(2-4-11)9-12(16)13(18)19/h1-4,12H,5-9,16H2,(H,18,19) SGDBTWWWUNNDEQ-UHFFFAOYSA-N 50025837 CHEMBL852::2-amino-3-[4-bis(2-chloroethyl)amino]phenylpropanoic acid::L-Sarcolysin::3-(p-(bis(2-chloroethyl)amino)phenyl)-L-alanine::Melfalan::Alanine Nitrogen Mustard::2-amino-3-(4-(bis(2-chloroethyl)amino)phenyl)propanoic acid::Phenylalanine Mustard::2-Amino-3-{4-[bis-(2-chloro-ethyl)-amino]-phenyl}-propionic acid(L-PAM)::2-Amino-3-{4-[bis-(2-chloro-ethyl)-amino]-phenyl}-propionic acid::2-Amino-3-{4-[bis-(2-chloro-ethyl)-amino]-phenyl}-propionic acid(Melphalan)::CB-3025::(S)-2-Amino-3-{4-[bis-(2-chloro-ethyl)-amino]-phenyl}-propionic acid::(S)-2-amino-3-(4-(bis(2-chloroethyl)amino)phenyl)propanoic acid::2-Amino-3-{4-[bis-(2-chloro-ethyl)-amino]-phenyl}-propionic acid (melphalan)::Alkeran::MELPHALAN Large neutral amino acids transporter small subunit 1 Rattus norvegicus 55000 ChEMBL 10.1016/j.bmcl.2010.04.086 10.7270/Q2HM58MR 20466543 Matharu, J; Oki, J; Worthen, DR; Smith, QR; Crooks, PA 6/4/2010 11/20/2010 University of Kentucky http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50025837 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50003204&target=Large+neutral+amino+acids+transporter+small+subunit+1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50025837&enzyme=Large+neutral+amino+acids+transporter+small+subunit+1&column=ki&startPg=0&Increment=50&submit=Search VUC 8KDO 460612 103935587 CHEMBL852 DB01042 C07122 1 MAVAGAKRRAVAAPATTAAEEERQAREKMLEARRGDGADPEGEGVTLQRNITLINGVAIIVGTIIGSGIFVTPTGVLKEAGSPGLSLVVWAVCGVFSIVGALCYAELGTTISKSGGDYAYMLEVYGSLPAFLKLWIELLIIRPSSQYIVALVFATYLLKPVFPTCPVPEEAAKLVACLCVLLLTAVNCYSVKAATRVQDAFAAAKLLALALIILLGFIQMGKDIGQGDASNLHQKLSFEGTNLDVGNIVLALYSGLFAYGGWNYLNFVTEEMINPYRNLPLAIIISLPIVTLVYVLTNLAYFTTLSTNQMLTSEAVAVDFGNYHLGVMSWIIPVFVGLSCFGSVNGSLFTSSRLFFVGSREGHLPSILSMIHPQLLTPVPSLVFTCVMTLMYAFSRDIFSIINFFSFFNWLCVALAIIGMMWLRFKKPELERPIKVNLALPVFFILACLFLIAVSFWKTPLECGIGFAIILSGLPVYFFGVWWKNKPKWILQVIFSVTVLCQKLMQVVPQET Large neutral amino acids transporter small subunit 1 LAT1_RAT Q63016 Q9QWL4 51521991 c1cc(ccc1c2cnc3c(cnn3c2)c4ccncc4)OCCN5CCCCC5 InChI=1S/C24H25N5O/c1-2-12-28(13-3-1)14-15-30-22-6-4-19(5-7-22)21-16-26-24-23(17-27-29(24)18-21)20-8-10-25-11-9-20/h4-11,16-18H,1-3,12-15H2 XHBVYDAKJHETMP-UHFFFAOYSA-N 50262685 CHEMBL478629::6-(4-(2-(piperidin-1-yl)ethoxy)phenyl)-3-(pyridin-4-yl)pyrazolo[1,5-a]pyrimidine::Dorsomorphin::6-[4-(2-piperidin-1-ylethoxy)phenyl]-3-pyridin-4-ylpyrazolo[1,5-a]pyrimidine::US9040694, Dorsomorphin 5'-AMP-activated protein kinase subunit beta-2 Rattus norvegicus 1280 ChEMBL 10.7270/Q2CF9VC6 36283182 Ye, W; Fan, C; Fu, K; Wang, X; Lin, J; Nian, S; Liu, C; Zhou, W 12/15/2022 4/21/2024 Guangzhou University of Chinese Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50262685 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000464&target=5%27-AMP-activated+protein+kinase+subunit+beta-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50262685&enzyme=5%27-AMP-activated+protein+kinase+subunit+beta-2&column=ki&startPg=0&Increment=50&submit=Search TAK 3AQV,3H9R,3Q4T,4C02,6GVX,7JHG,7M74 11524144 104111291 CHEMBL478629 DB08597 1 MGNTTSERVSGERHGAKAARAEGGGHGPGKEHKIMVGSTDDPSVFSLPDSKLPGDKEFVPWQQDLDDSVKPTQQARPTVIRWSEGGKEVFISGSFNNWSTKIPLIKSHNDFVAILDLPEGEHQYKFFVDGQWVHDPSEPVVTSQLGTINNLIHVKKSDFEVFDALKLDSMESSETSCRDLSSSPPGPYGQEMYVFRSEERFKSPPILPPHLLQVILNKDTNISCDPALLPEPNHVMLNHLYALSTKDSVMVLSATHRYKKKYVTTLLYKPI 2LU4,2LU3,2F15,4EAL,4EAK 5'-AMP-activated protein kinase subunit beta-2 AAKB2_RAT Q9QZH4 63995 c1cc(ccc1c2cnc3c(cnn3c2)c4ccncc4)OCCN5CCCCC5 InChI=1S/C24H25N5O/c1-2-12-28(13-3-1)14-15-30-22-6-4-19(5-7-22)21-16-26-24-23(17-27-29(24)18-21)20-8-10-25-11-9-20/h4-11,16-18H,1-3,12-15H2 XHBVYDAKJHETMP-UHFFFAOYSA-N 50262685 CHEMBL478629::6-(4-(2-(piperidin-1-yl)ethoxy)phenyl)-3-(pyridin-4-yl)pyrazolo[1,5-a]pyrimidine::Dorsomorphin::6-[4-(2-piperidin-1-ylethoxy)phenyl]-3-pyridin-4-ylpyrazolo[1,5-a]pyrimidine::US9040694, Dorsomorphin 5'-AMP-activated protein kinase subunit beta-1/5'-AMP-activated protein kinase subunit gamma-1/Dual specificity protein kinase CLK2 Homo sapiens 234.6 Curated from the literature by BindingDB 10.1021/cb9002865 10.7270/Q2JW8C78 20020776 aid1799383 Hao, J; Ho, JN; Lewis, JA; Karim, KA; Daniels, RN; Gentry, PR; Hopkins, CR; Lindsley, CW; Hong, CC 2/19/2010 2/11/2011 Vanderbilt University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50262685 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000296&target=5%27-AMP-activated+protein+kinase+subunit+beta-1%2F5%27-AMP-activated+protein+kinase+subunit+gamma-1%2FDual+specificity+protein+kinase+CLK2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50262685&enzyme=5%27-AMP-activated+protein+kinase+subunit+beta-1%2F5%27-AMP-activated+protein+kinase+subunit+gamma-1%2FDual+specificity+protein+kinase+CLK2&column=ki&startPg=0&Increment=50&submit=Search TAK 3AQV,3H9R,3Q4T,4C02,6GVX,7JHG,7M74 11524144 104111291 CHEMBL478629 DB08597 3 MPHPRRYHSSERGSRGSYREHYRSRKHKRRRSRSWSSSSDRTRRRRREDSYHVRSRSSYDDRSSDRRVYDRRYCGSYRRNDYSRDRGDAYYDTDYRHSYEYQRENSSYRSQRSSRRKHRRRRRRSRTFSRSSSQHSSRRAKSVEDDAEGHLIYHVGDWLQERYEIVSTLGEGTFGRVVQCVDHRRGGARVALKIIKNVEKYKEAARLEINVLEKINEKDPDNKNLCVQMFDWFDYHGHMCISFELLGLSTFDFLKDNNYLPYPIHQVRHMAFQLCQAVKFLHDNKLTHTDLKPENILFVNSDYELTYNLEKKRDERSVKSTAVRVVDFGSATFDHEHHSTIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNREHLAMMERILGPIPSRMIRKTRKQKYFYRGRLDWDENTSAGRYVRENCKPLRRYLTSEAEEHHQLFDLIESMLEYEPAKRLTLGEALQHPFFARLRAEPPNKLWDSSRDISR 6KHE,5UNP,6FYL,6FYK Dual specificity protein kinase CLK2 CLK2_HUMAN P49760 B1AVS9 B5MBX6 Q96CQ0 MGNTSSERAALERHGGHKTPRRDSSGGTKDGDRPKILMDSPEDADLFHSEEIKAPEKEEFLAWQHDLEVNDKAPAQARPTVFRWTGGGKEVYLSGSFNNWSKLPLTRSHNNFVAILDLPEGEHQYKFFVDGQWTHDPSEPIVTSQLGTVNNIIQVKKTDFEVFDALMVDSQKCSDVSELSSSPPGPYHQEPYVCKPEERFRAPPILPPHLLQVILNKDTGISCDPALLPEPNHVMLNHLYALSIKDGVMVLSATHRYKKKYVTTLLYKPI 8BIK,7MYJ,6B1U,5EZV,4ZHX,5ISO,4CFF,4CFE,6C9J,6C9H,6C9G,6C9F 5'-AMP-activated protein kinase subunit beta-1 AAKB1_HUMAN Q9Y478 Q9UBV0 Q9UE20 Q9UEX2 Q9Y6V8 METVISSDSSPAVENEHPQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDENDVVKGIVSLSDILQALVLTGGEKKP 8BIK,6C9H,6C9G,6C9F,5ISO,4CFF,4CFE,7MYJ,6B2E,6B1U,5EZV,4ZHX,6C9J,7M74,7JHH,7JHG,4REW,4RER,7JIJ,2UV5,2UV4 5'-AMP-activated protein kinase subunit gamma-1 AAKG1_HUMAN P54619 B4DDT7 Q8N7V9 51521991 c1cc(ccc1c2cnc3c(cnn3c2)c4ccncc4)OCCN5CCCCC5 InChI=1S/C24H25N5O/c1-2-12-28(13-3-1)14-15-30-22-6-4-19(5-7-22)21-16-26-24-23(17-27-29(24)18-21)20-8-10-25-11-9-20/h4-11,16-18H,1-3,12-15H2 XHBVYDAKJHETMP-UHFFFAOYSA-N 50262685 CHEMBL478629::6-(4-(2-(piperidin-1-yl)ethoxy)phenyl)-3-(pyridin-4-yl)pyrazolo[1,5-a]pyrimidine::Dorsomorphin::6-[4-(2-piperidin-1-ylethoxy)phenyl]-3-pyridin-4-ylpyrazolo[1,5-a]pyrimidine::US9040694, Dorsomorphin 5'-AMP-activated protein kinase subunit beta-2 Rattus norvegicus 1280 ChEMBL 10.7270/Q2CF9VC6 36283182 Ye, W; Fan, C; Fu, K; Wang, X; Lin, J; Nian, S; Liu, C; Zhou, W 12/15/2022 4/21/2024 Guangzhou University of Chinese Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50262685 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50000464&target=5%27-AMP-activated+protein+kinase+subunit+beta-2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50262685&enzyme=5%27-AMP-activated+protein+kinase+subunit+beta-2&column=ki&startPg=0&Increment=50&submit=Search TAK 3AQV,3H9R,3Q4T,4C02,6GVX,7JHG,7M74 11524144 104111291 CHEMBL478629 DB08597 1 MGNTTSERVSGERHGAKAARAEGGGHGPGKEHKIMVGSTDDPSVFSLPDSKLPGDKEFVPWQQDLDDSVKPTQQARPTVIRWSEGGKEVFISGSFNNWSTKIPLIKSHNDFVAILDLPEGEHQYKFFVDGQWVHDPSEPVVTSQLGTINNLIHVKKSDFEVFDALKLDSMESSETSCRDLSSSPPGPYGQEMYVFRSEERFKSPPILPPHLLQVILNKDTNISCDPALLPEPNHVMLNHLYALSTKDSVMVLSATHRYKKKYVTTLLYKPI 2LU4,2LU3,2F15,4EAL,4EAK 5'-AMP-activated protein kinase subunit beta-2 AAKB2_RAT Q9QZH4 63995 c1cc(ccc1c2cnc3c(cnn3c2)c4ccncc4)OCCN5CCCCC5 InChI=1S/C24H25N5O/c1-2-12-28(13-3-1)14-15-30-22-6-4-19(5-7-22)21-16-26-24-23(17-27-29(24)18-21)20-8-10-25-11-9-20/h4-11,16-18H,1-3,12-15H2 XHBVYDAKJHETMP-UHFFFAOYSA-N 50262685 CHEMBL478629::6-(4-(2-(piperidin-1-yl)ethoxy)phenyl)-3-(pyridin-4-yl)pyrazolo[1,5-a]pyrimidine::Dorsomorphin::6-[4-(2-piperidin-1-ylethoxy)phenyl]-3-pyridin-4-ylpyrazolo[1,5-a]pyrimidine::US9040694, Dorsomorphin 5'-AMP-activated protein kinase subunit beta-1/5'-AMP-activated protein kinase subunit gamma-1/Dual specificity protein kinase CLK2 Homo sapiens 234.6 Curated from the literature by BindingDB 10.1021/cb9002865 10.7270/Q2JW8C78 20020776 aid1799383 Hao, J; Ho, JN; Lewis, JA; Karim, KA; Daniels, RN; Gentry, PR; Hopkins, CR; Lindsley, CW; Hong, CC 2/19/2010 2/11/2011 Vanderbilt University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50262685 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000296&target=5%27-AMP-activated+protein+kinase+subunit+beta-1%2F5%27-AMP-activated+protein+kinase+subunit+gamma-1%2FDual+specificity+protein+kinase+CLK2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50262685&enzyme=5%27-AMP-activated+protein+kinase+subunit+beta-1%2F5%27-AMP-activated+protein+kinase+subunit+gamma-1%2FDual+specificity+protein+kinase+CLK2&column=ki&startPg=0&Increment=50&submit=Search TAK 3AQV,3H9R,3Q4T,4C02,6GVX,7JHG,7M74 11524144 104111291 CHEMBL478629 DB08597 3 MPHPRRYHSSERGSRGSYREHYRSRKHKRRRSRSWSSSSDRTRRRRREDSYHVRSRSSYDDRSSDRRVYDRRYCGSYRRNDYSRDRGDAYYDTDYRHSYEYQRENSSYRSQRSSRRKHRRRRRRSRTFSRSSSQHSSRRAKSVEDDAEGHLIYHVGDWLQERYEIVSTLGEGTFGRVVQCVDHRRGGARVALKIIKNVEKYKEAARLEINVLEKINEKDPDNKNLCVQMFDWFDYHGHMCISFELLGLSTFDFLKDNNYLPYPIHQVRHMAFQLCQAVKFLHDNKLTHTDLKPENILFVNSDYELTYNLEKKRDERSVKSTAVRVVDFGSATFDHEHHSTIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNREHLAMMERILGPIPSRMIRKTRKQKYFYRGRLDWDENTSAGRYVRENCKPLRRYLTSEAEEHHQLFDLIESMLEYEPAKRLTLGEALQHPFFARLRAEPPNKLWDSSRDISR 6KHE,5UNP,6FYL,6FYK Dual specificity protein kinase CLK2 CLK2_HUMAN P49760 B1AVS9 B5MBX6 Q96CQ0 MGNTSSERAALERHGGHKTPRRDSSGGTKDGDRPKILMDSPEDADLFHSEEIKAPEKEEFLAWQHDLEVNDKAPAQARPTVFRWTGGGKEVYLSGSFNNWSKLPLTRSHNNFVAILDLPEGEHQYKFFVDGQWTHDPSEPIVTSQLGTVNNIIQVKKTDFEVFDALMVDSQKCSDVSELSSSPPGPYHQEPYVCKPEERFRAPPILPPHLLQVILNKDTGISCDPALLPEPNHVMLNHLYALSIKDGVMVLSATHRYKKKYVTTLLYKPI 8BIK,7MYJ,6B1U,5EZV,4ZHX,5ISO,4CFF,4CFE,6C9J,6C9H,6C9G,6C9F 5'-AMP-activated protein kinase subunit beta-1 AAKB1_HUMAN Q9Y478 Q9UBV0 Q9UE20 Q9UEX2 Q9Y6V8 METVISSDSSPAVENEHPQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDENDVVKGIVSLSDILQALVLTGGEKKP 8BIK,6C9H,6C9G,6C9F,5ISO,4CFF,4CFE,7MYJ,6B2E,6B1U,5EZV,4ZHX,6C9J,7M74,7JHH,7JHG,4REW,4RER,7JIJ,2UV5,2UV4 5'-AMP-activated protein kinase subunit gamma-1 AAKG1_HUMAN P54619 B4DDT7 Q8N7V9 50521692 c1ccc(c(c1)c2ccc(cc2)c3csc4c3C(=C(C(=O)N4)C#N)O)O InChI=1S/C20H12N2O3S/c21-9-14-18(24)17-15(10-26-20(17)22-19(14)25)12-7-5-11(6-8-12)13-3-1-2-4-16(13)23/h1-8,10,23H,(H2,22,24,25) CTESJDQKVOEUOY-UHFFFAOYSA-N 50242401 A-769662::4-hydroxy-3-(2'-hydroxybiphenyl-4-yl)-6-oxo-6,7-dihydrothieno[2,3-b]pyridine-5-carbonitrile::CHEMBL512504 5'-AMP-activated protein kinase catalytic subunit alpha-1/subunit beta-1/subunit gamma-1 Homo sapiens 487 ChEMBL 10.1016/j.bmcl.2016.09.065 10.7270/Q25M67PH 27727125 Cameron, KO; Kurumbail, RG 11/1/2016 7/9/2018 Pfizer http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50242401 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=14&target=5%27-AMP-activated+protein+kinase+catalytic+subunit+alpha-1%2Fsubunit+beta-1%2Fsubunit+gamma-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50242401&enzyme=5%27-AMP-activated+protein+kinase+catalytic+subunit+alpha-1%2Fsubunit+beta-1%2Fsubunit+gamma-1&column=ki&startPg=0&Increment=50&submit=Search C1V 4CFF,4ZHX,5EZV 54708532 104099049 CHEMBL512504 3 MGNTSSERAALERHGGHKTPRRDSSGGTKDGDRPKILMDSPEDADLFHSEEIKAPEKEEFLAWQHDLEVNDKAPAQARPTVFRWTGGGKEVYLSGSFNNWSKLPLTRSHNNFVAILDLPEGEHQYKFFVDGQWTHDPSEPIVTSQLGTVNNIIQVKKTDFEVFDALMVDSQKCSDVSELSSSPPGPYHQEPYVCKPEERFRAPPILPPHLLQVILNKDTGISCDPALLPEPNHVMLNHLYALSIKDGVMVLSATHRYKKKYVTTLLYKPI 8BIK,7MYJ,6B1U,5EZV,4ZHX,5ISO,4CFF,4CFE,6C9J,6C9H,6C9G,6C9F 5'-AMP-activated protein kinase subunit beta-1 AAKB1_HUMAN Q9Y478 Q9UBV0 Q9UE20 Q9UEX2 Q9Y6V8 METVISSDSSPAVENEHPQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDENDVVKGIVSLSDILQALVLTGGEKKP 8BIK,6C9H,6C9G,6C9F,5ISO,4CFF,4CFE,7MYJ,6B2E,6B1U,5EZV,4ZHX,6C9J,7M74,7JHH,7JHG,4REW,4RER,7JIJ,2UV5,2UV4 5'-AMP-activated protein kinase subunit gamma-1 AAKG1_HUMAN P54619 B4DDT7 Q8N7V9 MRRLSSWRKMATAEKQKHDGRVKIGHYILGDTLGVGTFGKVKVGKHELTGHKVAVKILNRQKIRSLDVVGKIRREIQNLKLFRHPHIIKLYQVISTPSDIFMVMEYVSGGELFDYICKNGRLDEKESRRLFQQILSGVDYCHRHMVVHRDLKPENVLLDAHMNAKIADFGLSNMMSDGEFLRTSCGSPNYAAPEVISGRLYAGPEVDIWSSGVILYALLCGTLPFDDDHVPTLFKKICDGIFYTPQYLNPSVISLLKHMLQVDPMKRATIKDIREHEWFKQDLPKYLFPEDPSYSSTMIDDEALKEVCEKFECSEEEVLSCLYNRNHQDPLAVAYHLIIDNRRIMNEAKDFYLATSPPDSFLDDHHLTRPHPERVPFLVAETPRARHTLDELNPQKSKHQGVRKAKWHLGIRSQSRPNDIMAEVCRAIKQLDYEWKVVNPYYLRVRRKNPVTSTYSKMSLQLYQVDSRTYLLDFRSIDDEITEAKSGTATPQRSGSVSNYRSCQRSDSDAEAQGKSSEVSLTSSVTSLDSSPVDLTPRPGSHTIEFFEMCANLIKILAQ 4REW,4RER,7M74,7JIJ,7JHH,7JHG 5'-AMP-activated protein kinase catalytic subunit alpha-1 AAPK1_HUMAN Q13131 A8MTQ6 B2R7E1 O00286 Q5D0E1 Q86VS1 Q9UNQ4 51118972 c1ccc(c(c1)c2ccc(cc2)c3csc4c3C(=C(C(=O)N4)C#N)O)O InChI=1S/C20H12N2O3S/c21-9-14-18(24)17-15(10-26-20(17)22-19(14)25)12-7-5-11(6-8-12)13-3-1-2-4-16(13)23/h1-8,10,23H,(H2,22,24,25) CTESJDQKVOEUOY-UHFFFAOYSA-N 50242401 A-769662::4-hydroxy-3-(2'-hydroxybiphenyl-4-yl)-6-oxo-6,7-dihydrothieno[2,3-b]pyridine-5-carbonitrile::CHEMBL512504 5'-AMP-activated protein kinase catalytic subunit alpha-2/subunit beta-1/subunit gamma-1 Homo sapiens 390 ChEMBL 10.1021/acs.jmedchem.8b00180 10.7270/Q2DJ5J62 29620890 Young, RJ; Leeson, PD 8/9/2018 8/16/2020 Glaxosmithkline http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50242401 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000057&target=5%27-AMP-activated+protein+kinase+catalytic+subunit+alpha-2%2Fsubunit+beta-1%2Fsubunit+gamma-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50242401&enzyme=5%27-AMP-activated+protein+kinase+catalytic+subunit+alpha-2%2Fsubunit+beta-1%2Fsubunit+gamma-1&column=ki&startPg=0&Increment=50&submit=Search C1V 4CFF,4ZHX,5EZV 54708532 104099049 CHEMBL512504 3 MGNTSSERAALERHGGHKTPRRDSSGGTKDGDRPKILMDSPEDADLFHSEEIKAPEKEEFLAWQHDLEVNDKAPAQARPTVFRWTGGGKEVYLSGSFNNWSKLPLTRSHNNFVAILDLPEGEHQYKFFVDGQWTHDPSEPIVTSQLGTVNNIIQVKKTDFEVFDALMVDSQKCSDVSELSSSPPGPYHQEPYVCKPEERFRAPPILPPHLLQVILNKDTGISCDPALLPEPNHVMLNHLYALSIKDGVMVLSATHRYKKKYVTTLLYKPI 8BIK,7MYJ,6B1U,5EZV,4ZHX,5ISO,4CFF,4CFE,6C9J,6C9H,6C9G,6C9F 5'-AMP-activated protein kinase subunit beta-1 AAKB1_HUMAN Q9Y478 Q9UBV0 Q9UE20 Q9UEX2 Q9Y6V8 METVISSDSSPAVENEHPQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDENDVVKGIVSLSDILQALVLTGGEKKP 8BIK,6C9H,6C9G,6C9F,5ISO,4CFF,4CFE,7MYJ,6B2E,6B1U,5EZV,4ZHX,6C9J,7M74,7JHH,7JHG,4REW,4RER,7JIJ,2UV5,2UV4 5'-AMP-activated protein kinase subunit gamma-1 AAKG1_HUMAN P54619 B4DDT7 Q8N7V9 MAEKQKHDGRVKIGHYVLGDTLGVGTFGKVKIGEHQLTGHKVAVKILNRQKIRSLDVVGKIKREIQNLKLFRHPHIIKLYQVISTPTDFFMVMEYVSGGELFDYICKHGRVEEMEARRLFQQILSAVDYCHRHMVVHRDLKPENVLLDAHMNAKIADFGLSNMMSDGEFLRTSCGSPNYAAPEVISGRLYAGPEVDIWSCGVILYALLCGTLPFDDEHVPTLFKKIRGGVFYIPEYLNRSVATLLMHMLQVDPLKRATIKDIREHEWFKQDLPSYLFPEDPSYDANVIDDEAVKEVCEKFECTESEVMNSLYSGDPQDQLAVAYHLIIDNRRIMNQASEFYLASSPPSGSFMDDSAMHIPPGLKPHPERMPPLIADSPKARCPLDALNTTKPKSLAVKKAKWHLGIRSQSKPYDIMAEVYRAMKQLDFEWKVVNAYHLRVRRKNPVTGNYVKMSLQLYLVDNRSYLLDFKSIDDEVVEQRSGSSTPQRSCSAAGLHRPRSSFDSTTAESHSLSGSLTGSLTGSTLSSVSPRLGSHTMDFFEMCASLITTLAR 5ISO,8BIK,4CFF,4CFE,9IC2,2H6D 5'-AMP-activated protein kinase catalytic subunit alpha-2 AAPK2_HUMAN P54646 Q9H1E8 Q9UD43 51219552 c1ccc(c(c1)c2ccc(cc2)c3csc4c3C(=C(C(=O)N4)C#N)O)O InChI=1S/C20H12N2O3S/c21-9-14-18(24)17-15(10-26-20(17)22-19(14)25)12-7-5-11(6-8-12)13-3-1-2-4-16(13)23/h1-8,10,23H,(H2,22,24,25) CTESJDQKVOEUOY-UHFFFAOYSA-N 50242401 A-769662::4-hydroxy-3-(2'-hydroxybiphenyl-4-yl)-6-oxo-6,7-dihydrothieno[2,3-b]pyridine-5-carbonitrile::CHEMBL512504 5'-AMP-activated protein kinase catalytic subunit alpha-1/subunit beta-1/subunit gamma-1 Homo sapiens 510 ChEMBL 10.1021/acs.jmedchem.5b01201 10.7270/Q26976KB 26510622 Miglianico, M; Nicolaes, GA; Neumann, D 4/14/2016 9/4/2020 Maastricht University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50242401 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=14&target=5%27-AMP-activated+protein+kinase+catalytic+subunit+alpha-1%2Fsubunit+beta-1%2Fsubunit+gamma-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50242401&enzyme=5%27-AMP-activated+protein+kinase+catalytic+subunit+alpha-1%2Fsubunit+beta-1%2Fsubunit+gamma-1&column=ki&startPg=0&Increment=50&submit=Search C1V 4CFF,4ZHX,5EZV 54708532 104099049 CHEMBL512504 3 MGNTSSERAALERHGGHKTPRRDSSGGTKDGDRPKILMDSPEDADLFHSEEIKAPEKEEFLAWQHDLEVNDKAPAQARPTVFRWTGGGKEVYLSGSFNNWSKLPLTRSHNNFVAILDLPEGEHQYKFFVDGQWTHDPSEPIVTSQLGTVNNIIQVKKTDFEVFDALMVDSQKCSDVSELSSSPPGPYHQEPYVCKPEERFRAPPILPPHLLQVILNKDTGISCDPALLPEPNHVMLNHLYALSIKDGVMVLSATHRYKKKYVTTLLYKPI 8BIK,7MYJ,6B1U,5EZV,4ZHX,5ISO,4CFF,4CFE,6C9J,6C9H,6C9G,6C9F 5'-AMP-activated protein kinase subunit beta-1 AAKB1_HUMAN Q9Y478 Q9UBV0 Q9UE20 Q9UEX2 Q9Y6V8 METVISSDSSPAVENEHPQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDENDVVKGIVSLSDILQALVLTGGEKKP 8BIK,6C9H,6C9G,6C9F,5ISO,4CFF,4CFE,7MYJ,6B2E,6B1U,5EZV,4ZHX,6C9J,7M74,7JHH,7JHG,4REW,4RER,7JIJ,2UV5,2UV4 5'-AMP-activated protein kinase subunit gamma-1 AAKG1_HUMAN P54619 B4DDT7 Q8N7V9 MRRLSSWRKMATAEKQKHDGRVKIGHYILGDTLGVGTFGKVKVGKHELTGHKVAVKILNRQKIRSLDVVGKIRREIQNLKLFRHPHIIKLYQVISTPSDIFMVMEYVSGGELFDYICKNGRLDEKESRRLFQQILSGVDYCHRHMVVHRDLKPENVLLDAHMNAKIADFGLSNMMSDGEFLRTSCGSPNYAAPEVISGRLYAGPEVDIWSSGVILYALLCGTLPFDDDHVPTLFKKICDGIFYTPQYLNPSVISLLKHMLQVDPMKRATIKDIREHEWFKQDLPKYLFPEDPSYSSTMIDDEALKEVCEKFECSEEEVLSCLYNRNHQDPLAVAYHLIIDNRRIMNEAKDFYLATSPPDSFLDDHHLTRPHPERVPFLVAETPRARHTLDELNPQKSKHQGVRKAKWHLGIRSQSRPNDIMAEVCRAIKQLDYEWKVVNPYYLRVRRKNPVTSTYSKMSLQLYQVDSRTYLLDFRSIDDEITEAKSGTATPQRSGSVSNYRSCQRSDSDAEAQGKSSEVSLTSSVTSLDSSPVDLTPRPGSHTIEFFEMCANLIKILAQ 4REW,4RER,7M74,7JIJ,7JHH,7JHG 5'-AMP-activated protein kinase catalytic subunit alpha-1 AAPK1_HUMAN Q13131 A8MTQ6 B2R7E1 O00286 Q5D0E1 Q86VS1 Q9UNQ4 51219553 c1ccc(c(c1)c2ccc(cc2)c3csc4c3C(=C(C(=O)N4)C#N)O)O InChI=1S/C20H12N2O3S/c21-9-14-18(24)17-15(10-26-20(17)22-19(14)25)12-7-5-11(6-8-12)13-3-1-2-4-16(13)23/h1-8,10,23H,(H2,22,24,25) CTESJDQKVOEUOY-UHFFFAOYSA-N 50242401 A-769662::4-hydroxy-3-(2'-hydroxybiphenyl-4-yl)-6-oxo-6,7-dihydrothieno[2,3-b]pyridine-5-carbonitrile::CHEMBL512504 5'-AMP-activated protein kinase catalytic subunit alpha-1/subunit beta-2/subunit gamma-1 Homo sapiens 14500 ChEMBL 10.1021/acs.jmedchem.5b01201 10.7270/Q26976KB 26510622 Miglianico, M; Nicolaes, GA; Neumann, D 4/14/2016 9/4/2020 Maastricht University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50242401 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50004248&target=5%27-AMP-activated+protein+kinase+catalytic+subunit+alpha-1%2Fsubunit+beta-2%2Fsubunit+gamma-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50242401&enzyme=5%27-AMP-activated+protein+kinase+catalytic+subunit+alpha-1%2Fsubunit+beta-2%2Fsubunit+gamma-1&column=ki&startPg=0&Increment=50&submit=Search C1V 4CFF,4ZHX,5EZV 54708532 104099049 CHEMBL512504 3 METVISSDSSPAVENEHPQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDENDVVKGIVSLSDILQALVLTGGEKKP 8BIK,6C9H,6C9G,6C9F,5ISO,4CFF,4CFE,7MYJ,6B2E,6B1U,5EZV,4ZHX,6C9J,7M74,7JHH,7JHG,4REW,4RER,7JIJ,2UV5,2UV4 5'-AMP-activated protein kinase subunit gamma-1 AAKG1_HUMAN P54619 B4DDT7 Q8N7V9 MRRLSSWRKMATAEKQKHDGRVKIGHYILGDTLGVGTFGKVKVGKHELTGHKVAVKILNRQKIRSLDVVGKIRREIQNLKLFRHPHIIKLYQVISTPSDIFMVMEYVSGGELFDYICKNGRLDEKESRRLFQQILSGVDYCHRHMVVHRDLKPENVLLDAHMNAKIADFGLSNMMSDGEFLRTSCGSPNYAAPEVISGRLYAGPEVDIWSSGVILYALLCGTLPFDDDHVPTLFKKICDGIFYTPQYLNPSVISLLKHMLQVDPMKRATIKDIREHEWFKQDLPKYLFPEDPSYSSTMIDDEALKEVCEKFECSEEEVLSCLYNRNHQDPLAVAYHLIIDNRRIMNEAKDFYLATSPPDSFLDDHHLTRPHPERVPFLVAETPRARHTLDELNPQKSKHQGVRKAKWHLGIRSQSRPNDIMAEVCRAIKQLDYEWKVVNPYYLRVRRKNPVTSTYSKMSLQLYQVDSRTYLLDFRSIDDEITEAKSGTATPQRSGSVSNYRSCQRSDSDAEAQGKSSEVSLTSSVTSLDSSPVDLTPRPGSHTIEFFEMCANLIKILAQ 4REW,4RER,7M74,7JIJ,7JHH,7JHG 5'-AMP-activated protein kinase catalytic subunit alpha-1 AAPK1_HUMAN Q13131 A8MTQ6 B2R7E1 O00286 Q5D0E1 Q86VS1 Q9UNQ4 MGNTTSDRVSGERHGAKAARSEGAGGHAPGKEHKIMVGSTDDPSVFSLPDSKLPGDKEFVSWQQDLEDSVKPTQQARPTVIRWSEGGKEVFISGSFNNWSTKIPLIKSHNDFVAILDLPEGEHQYKFFVDGQWVHDPSEPVVTSQLGTINNLIHVKKSDFEVFDALKLDSMESSETSCRDLSSSPPGPYGQEMYAFRSEERFKSPPILPPHLLQVILNKDTNISCDPALLPEPNHVMLNHLYALSIKDSVMVLSATHRYKKKYVTTLLYKPI 6B2E,4REW,4RER,2LU4,2LU3,2F15,4CFH,2YA3,2Y8Q,2Y8L,2V9J,2V92,2V8Q,4EAJ,4EAI 5'-AMP-activated protein kinase subunit beta-2 AAKB2_HUMAN O43741 A8K9V5 B4DH06 Q5VXY0 51253823 c1ccc(c(c1)c2ccc(cc2)c3csc4c3C(=C(C(=O)N4)C#N)O)O InChI=1S/C20H12N2O3S/c21-9-14-18(24)17-15(10-26-20(17)22-19(14)25)12-7-5-11(6-8-12)13-3-1-2-4-16(13)23/h1-8,10,23H,(H2,22,24,25) CTESJDQKVOEUOY-UHFFFAOYSA-N 50242401 A-769662::4-hydroxy-3-(2'-hydroxybiphenyl-4-yl)-6-oxo-6,7-dihydrothieno[2,3-b]pyridine-5-carbonitrile::CHEMBL512504 5'-AMP-activated protein kinase catalytic subunit alpha-1/subunit beta-1/subunit gamma-1 Homo sapiens 800 ChEMBL 10.1016/j.bmcl.2019.07.035 10.7270/Q2QF8X6H 31358465 Babkov, DA; Zhukowskaya, ON; Borisov, AV; Babkova, VA; Sokolova, EV; Brigadirova, AA; Litvinov, RA; Kolodina, AA; Morkovnik, AS; Sochnev, VS; Borodkin, GS; Spasov, AA 9/1/2019 2/20/2021 Volgograd State Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50242401 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=14&target=5%27-AMP-activated+protein+kinase+catalytic+subunit+alpha-1%2Fsubunit+beta-1%2Fsubunit+gamma-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50242401&enzyme=5%27-AMP-activated+protein+kinase+catalytic+subunit+alpha-1%2Fsubunit+beta-1%2Fsubunit+gamma-1&column=ki&startPg=0&Increment=50&submit=Search C1V 4CFF,4ZHX,5EZV 54708532 104099049 CHEMBL512504 3 MGNTSSERAALERHGGHKTPRRDSSGGTKDGDRPKILMDSPEDADLFHSEEIKAPEKEEFLAWQHDLEVNDKAPAQARPTVFRWTGGGKEVYLSGSFNNWSKLPLTRSHNNFVAILDLPEGEHQYKFFVDGQWTHDPSEPIVTSQLGTVNNIIQVKKTDFEVFDALMVDSQKCSDVSELSSSPPGPYHQEPYVCKPEERFRAPPILPPHLLQVILNKDTGISCDPALLPEPNHVMLNHLYALSIKDGVMVLSATHRYKKKYVTTLLYKPI 8BIK,7MYJ,6B1U,5EZV,4ZHX,5ISO,4CFF,4CFE,6C9J,6C9H,6C9G,6C9F 5'-AMP-activated protein kinase subunit beta-1 AAKB1_HUMAN Q9Y478 Q9UBV0 Q9UE20 Q9UEX2 Q9Y6V8 METVISSDSSPAVENEHPQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDENDVVKGIVSLSDILQALVLTGGEKKP 8BIK,6C9H,6C9G,6C9F,5ISO,4CFF,4CFE,7MYJ,6B2E,6B1U,5EZV,4ZHX,6C9J,7M74,7JHH,7JHG,4REW,4RER,7JIJ,2UV5,2UV4 5'-AMP-activated protein kinase subunit gamma-1 AAKG1_HUMAN P54619 B4DDT7 Q8N7V9 MRRLSSWRKMATAEKQKHDGRVKIGHYILGDTLGVGTFGKVKVGKHELTGHKVAVKILNRQKIRSLDVVGKIRREIQNLKLFRHPHIIKLYQVISTPSDIFMVMEYVSGGELFDYICKNGRLDEKESRRLFQQILSGVDYCHRHMVVHRDLKPENVLLDAHMNAKIADFGLSNMMSDGEFLRTSCGSPNYAAPEVISGRLYAGPEVDIWSSGVILYALLCGTLPFDDDHVPTLFKKICDGIFYTPQYLNPSVISLLKHMLQVDPMKRATIKDIREHEWFKQDLPKYLFPEDPSYSSTMIDDEALKEVCEKFECSEEEVLSCLYNRNHQDPLAVAYHLIIDNRRIMNEAKDFYLATSPPDSFLDDHHLTRPHPERVPFLVAETPRARHTLDELNPQKSKHQGVRKAKWHLGIRSQSRPNDIMAEVCRAIKQLDYEWKVVNPYYLRVRRKNPVTSTYSKMSLQLYQVDSRTYLLDFRSIDDEITEAKSGTATPQRSGSVSNYRSCQRSDSDAEAQGKSSEVSLTSSVTSLDSSPVDLTPRPGSHTIEFFEMCANLIKILAQ 4REW,4RER,7M74,7JIJ,7JHH,7JHG 5'-AMP-activated protein kinase catalytic subunit alpha-1 AAPK1_HUMAN Q13131 A8MTQ6 B2R7E1 O00286 Q5D0E1 Q86VS1 Q9UNQ4 50521692 c1ccc(c(c1)c2ccc(cc2)c3csc4c3C(=C(C(=O)N4)C#N)O)O InChI=1S/C20H12N2O3S/c21-9-14-18(24)17-15(10-26-20(17)22-19(14)25)12-7-5-11(6-8-12)13-3-1-2-4-16(13)23/h1-8,10,23H,(H2,22,24,25) CTESJDQKVOEUOY-UHFFFAOYSA-N 50242401 A-769662::4-hydroxy-3-(2'-hydroxybiphenyl-4-yl)-6-oxo-6,7-dihydrothieno[2,3-b]pyridine-5-carbonitrile::CHEMBL512504 5'-AMP-activated protein kinase catalytic subunit alpha-1/subunit beta-1/subunit gamma-1 Homo sapiens 487 ChEMBL 10.1016/j.bmcl.2016.09.065 10.7270/Q25M67PH 27727125 Cameron, KO; Kurumbail, RG 11/1/2016 7/9/2018 Pfizer http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50242401 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=14&target=5%27-AMP-activated+protein+kinase+catalytic+subunit+alpha-1%2Fsubunit+beta-1%2Fsubunit+gamma-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50242401&enzyme=5%27-AMP-activated+protein+kinase+catalytic+subunit+alpha-1%2Fsubunit+beta-1%2Fsubunit+gamma-1&column=ki&startPg=0&Increment=50&submit=Search C1V 4CFF,4ZHX,5EZV 54708532 104099049 CHEMBL512504 3 MGNTSSERAALERHGGHKTPRRDSSGGTKDGDRPKILMDSPEDADLFHSEEIKAPEKEEFLAWQHDLEVNDKAPAQARPTVFRWTGGGKEVYLSGSFNNWSKLPLTRSHNNFVAILDLPEGEHQYKFFVDGQWTHDPSEPIVTSQLGTVNNIIQVKKTDFEVFDALMVDSQKCSDVSELSSSPPGPYHQEPYVCKPEERFRAPPILPPHLLQVILNKDTGISCDPALLPEPNHVMLNHLYALSIKDGVMVLSATHRYKKKYVTTLLYKPI 8BIK,7MYJ,6B1U,5EZV,4ZHX,5ISO,4CFF,4CFE,6C9J,6C9H,6C9G,6C9F 5'-AMP-activated protein kinase subunit beta-1 AAKB1_HUMAN Q9Y478 Q9UBV0 Q9UE20 Q9UEX2 Q9Y6V8 METVISSDSSPAVENEHPQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDENDVVKGIVSLSDILQALVLTGGEKKP 8BIK,6C9H,6C9G,6C9F,5ISO,4CFF,4CFE,7MYJ,6B2E,6B1U,5EZV,4ZHX,6C9J,7M74,7JHH,7JHG,4REW,4RER,7JIJ,2UV5,2UV4 5'-AMP-activated protein kinase subunit gamma-1 AAKG1_HUMAN P54619 B4DDT7 Q8N7V9 MRRLSSWRKMATAEKQKHDGRVKIGHYILGDTLGVGTFGKVKVGKHELTGHKVAVKILNRQKIRSLDVVGKIRREIQNLKLFRHPHIIKLYQVISTPSDIFMVMEYVSGGELFDYICKNGRLDEKESRRLFQQILSGVDYCHRHMVVHRDLKPENVLLDAHMNAKIADFGLSNMMSDGEFLRTSCGSPNYAAPEVISGRLYAGPEVDIWSSGVILYALLCGTLPFDDDHVPTLFKKICDGIFYTPQYLNPSVISLLKHMLQVDPMKRATIKDIREHEWFKQDLPKYLFPEDPSYSSTMIDDEALKEVCEKFECSEEEVLSCLYNRNHQDPLAVAYHLIIDNRRIMNEAKDFYLATSPPDSFLDDHHLTRPHPERVPFLVAETPRARHTLDELNPQKSKHQGVRKAKWHLGIRSQSRPNDIMAEVCRAIKQLDYEWKVVNPYYLRVRRKNPVTSTYSKMSLQLYQVDSRTYLLDFRSIDDEITEAKSGTATPQRSGSVSNYRSCQRSDSDAEAQGKSSEVSLTSSVTSLDSSPVDLTPRPGSHTIEFFEMCANLIKILAQ 4REW,4RER,7M74,7JIJ,7JHH,7JHG 5'-AMP-activated protein kinase catalytic subunit alpha-1 AAPK1_HUMAN Q13131 A8MTQ6 B2R7E1 O00286 Q5D0E1 Q86VS1 Q9UNQ4 51118972 c1ccc(c(c1)c2ccc(cc2)c3csc4c3C(=C(C(=O)N4)C#N)O)O InChI=1S/C20H12N2O3S/c21-9-14-18(24)17-15(10-26-20(17)22-19(14)25)12-7-5-11(6-8-12)13-3-1-2-4-16(13)23/h1-8,10,23H,(H2,22,24,25) CTESJDQKVOEUOY-UHFFFAOYSA-N 50242401 A-769662::4-hydroxy-3-(2'-hydroxybiphenyl-4-yl)-6-oxo-6,7-dihydrothieno[2,3-b]pyridine-5-carbonitrile::CHEMBL512504 5'-AMP-activated protein kinase catalytic subunit alpha-2/subunit beta-1/subunit gamma-1 Homo sapiens 390 ChEMBL 10.1021/acs.jmedchem.8b00180 10.7270/Q2DJ5J62 29620890 Young, RJ; Leeson, PD 8/9/2018 8/16/2020 Glaxosmithkline http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50242401 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000057&target=5%27-AMP-activated+protein+kinase+catalytic+subunit+alpha-2%2Fsubunit+beta-1%2Fsubunit+gamma-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50242401&enzyme=5%27-AMP-activated+protein+kinase+catalytic+subunit+alpha-2%2Fsubunit+beta-1%2Fsubunit+gamma-1&column=ki&startPg=0&Increment=50&submit=Search C1V 4CFF,4ZHX,5EZV 54708532 104099049 CHEMBL512504 3 MGNTSSERAALERHGGHKTPRRDSSGGTKDGDRPKILMDSPEDADLFHSEEIKAPEKEEFLAWQHDLEVNDKAPAQARPTVFRWTGGGKEVYLSGSFNNWSKLPLTRSHNNFVAILDLPEGEHQYKFFVDGQWTHDPSEPIVTSQLGTVNNIIQVKKTDFEVFDALMVDSQKCSDVSELSSSPPGPYHQEPYVCKPEERFRAPPILPPHLLQVILNKDTGISCDPALLPEPNHVMLNHLYALSIKDGVMVLSATHRYKKKYVTTLLYKPI 8BIK,7MYJ,6B1U,5EZV,4ZHX,5ISO,4CFF,4CFE,6C9J,6C9H,6C9G,6C9F 5'-AMP-activated protein kinase subunit beta-1 AAKB1_HUMAN Q9Y478 Q9UBV0 Q9UE20 Q9UEX2 Q9Y6V8 METVISSDSSPAVENEHPQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDENDVVKGIVSLSDILQALVLTGGEKKP 8BIK,6C9H,6C9G,6C9F,5ISO,4CFF,4CFE,7MYJ,6B2E,6B1U,5EZV,4ZHX,6C9J,7M74,7JHH,7JHG,4REW,4RER,7JIJ,2UV5,2UV4 5'-AMP-activated protein kinase subunit gamma-1 AAKG1_HUMAN P54619 B4DDT7 Q8N7V9 MAEKQKHDGRVKIGHYVLGDTLGVGTFGKVKIGEHQLTGHKVAVKILNRQKIRSLDVVGKIKREIQNLKLFRHPHIIKLYQVISTPTDFFMVMEYVSGGELFDYICKHGRVEEMEARRLFQQILSAVDYCHRHMVVHRDLKPENVLLDAHMNAKIADFGLSNMMSDGEFLRTSCGSPNYAAPEVISGRLYAGPEVDIWSCGVILYALLCGTLPFDDEHVPTLFKKIRGGVFYIPEYLNRSVATLLMHMLQVDPLKRATIKDIREHEWFKQDLPSYLFPEDPSYDANVIDDEAVKEVCEKFECTESEVMNSLYSGDPQDQLAVAYHLIIDNRRIMNQASEFYLASSPPSGSFMDDSAMHIPPGLKPHPERMPPLIADSPKARCPLDALNTTKPKSLAVKKAKWHLGIRSQSKPYDIMAEVYRAMKQLDFEWKVVNAYHLRVRRKNPVTGNYVKMSLQLYLVDNRSYLLDFKSIDDEVVEQRSGSSTPQRSCSAAGLHRPRSSFDSTTAESHSLSGSLTGSLTGSTLSSVSPRLGSHTMDFFEMCASLITTLAR 5ISO,8BIK,4CFF,4CFE,9IC2,2H6D 5'-AMP-activated protein kinase catalytic subunit alpha-2 AAPK2_HUMAN P54646 Q9H1E8 Q9UD43 51219552 c1ccc(c(c1)c2ccc(cc2)c3csc4c3C(=C(C(=O)N4)C#N)O)O InChI=1S/C20H12N2O3S/c21-9-14-18(24)17-15(10-26-20(17)22-19(14)25)12-7-5-11(6-8-12)13-3-1-2-4-16(13)23/h1-8,10,23H,(H2,22,24,25) CTESJDQKVOEUOY-UHFFFAOYSA-N 50242401 A-769662::4-hydroxy-3-(2'-hydroxybiphenyl-4-yl)-6-oxo-6,7-dihydrothieno[2,3-b]pyridine-5-carbonitrile::CHEMBL512504 5'-AMP-activated protein kinase catalytic subunit alpha-1/subunit beta-1/subunit gamma-1 Homo sapiens 510 ChEMBL 10.1021/acs.jmedchem.5b01201 10.7270/Q26976KB 26510622 Miglianico, M; Nicolaes, GA; Neumann, D 4/14/2016 9/4/2020 Maastricht University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50242401 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=14&target=5%27-AMP-activated+protein+kinase+catalytic+subunit+alpha-1%2Fsubunit+beta-1%2Fsubunit+gamma-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50242401&enzyme=5%27-AMP-activated+protein+kinase+catalytic+subunit+alpha-1%2Fsubunit+beta-1%2Fsubunit+gamma-1&column=ki&startPg=0&Increment=50&submit=Search C1V 4CFF,4ZHX,5EZV 54708532 104099049 CHEMBL512504 3 MGNTSSERAALERHGGHKTPRRDSSGGTKDGDRPKILMDSPEDADLFHSEEIKAPEKEEFLAWQHDLEVNDKAPAQARPTVFRWTGGGKEVYLSGSFNNWSKLPLTRSHNNFVAILDLPEGEHQYKFFVDGQWTHDPSEPIVTSQLGTVNNIIQVKKTDFEVFDALMVDSQKCSDVSELSSSPPGPYHQEPYVCKPEERFRAPPILPPHLLQVILNKDTGISCDPALLPEPNHVMLNHLYALSIKDGVMVLSATHRYKKKYVTTLLYKPI 8BIK,7MYJ,6B1U,5EZV,4ZHX,5ISO,4CFF,4CFE,6C9J,6C9H,6C9G,6C9F 5'-AMP-activated protein kinase subunit beta-1 AAKB1_HUMAN Q9Y478 Q9UBV0 Q9UE20 Q9UEX2 Q9Y6V8 METVISSDSSPAVENEHPQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDENDVVKGIVSLSDILQALVLTGGEKKP 8BIK,6C9H,6C9G,6C9F,5ISO,4CFF,4CFE,7MYJ,6B2E,6B1U,5EZV,4ZHX,6C9J,7M74,7JHH,7JHG,4REW,4RER,7JIJ,2UV5,2UV4 5'-AMP-activated protein kinase subunit gamma-1 AAKG1_HUMAN P54619 B4DDT7 Q8N7V9 MRRLSSWRKMATAEKQKHDGRVKIGHYILGDTLGVGTFGKVKVGKHELTGHKVAVKILNRQKIRSLDVVGKIRREIQNLKLFRHPHIIKLYQVISTPSDIFMVMEYVSGGELFDYICKNGRLDEKESRRLFQQILSGVDYCHRHMVVHRDLKPENVLLDAHMNAKIADFGLSNMMSDGEFLRTSCGSPNYAAPEVISGRLYAGPEVDIWSSGVILYALLCGTLPFDDDHVPTLFKKICDGIFYTPQYLNPSVISLLKHMLQVDPMKRATIKDIREHEWFKQDLPKYLFPEDPSYSSTMIDDEALKEVCEKFECSEEEVLSCLYNRNHQDPLAVAYHLIIDNRRIMNEAKDFYLATSPPDSFLDDHHLTRPHPERVPFLVAETPRARHTLDELNPQKSKHQGVRKAKWHLGIRSQSRPNDIMAEVCRAIKQLDYEWKVVNPYYLRVRRKNPVTSTYSKMSLQLYQVDSRTYLLDFRSIDDEITEAKSGTATPQRSGSVSNYRSCQRSDSDAEAQGKSSEVSLTSSVTSLDSSPVDLTPRPGSHTIEFFEMCANLIKILAQ 4REW,4RER,7M74,7JIJ,7JHH,7JHG 5'-AMP-activated protein kinase catalytic subunit alpha-1 AAPK1_HUMAN Q13131 A8MTQ6 B2R7E1 O00286 Q5D0E1 Q86VS1 Q9UNQ4 51219553 c1ccc(c(c1)c2ccc(cc2)c3csc4c3C(=C(C(=O)N4)C#N)O)O InChI=1S/C20H12N2O3S/c21-9-14-18(24)17-15(10-26-20(17)22-19(14)25)12-7-5-11(6-8-12)13-3-1-2-4-16(13)23/h1-8,10,23H,(H2,22,24,25) CTESJDQKVOEUOY-UHFFFAOYSA-N 50242401 A-769662::4-hydroxy-3-(2'-hydroxybiphenyl-4-yl)-6-oxo-6,7-dihydrothieno[2,3-b]pyridine-5-carbonitrile::CHEMBL512504 5'-AMP-activated protein kinase catalytic subunit alpha-1/subunit beta-2/subunit gamma-1 Homo sapiens 14500 ChEMBL 10.1021/acs.jmedchem.5b01201 10.7270/Q26976KB 26510622 Miglianico, M; Nicolaes, GA; Neumann, D 4/14/2016 9/4/2020 Maastricht University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50242401 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50004248&target=5%27-AMP-activated+protein+kinase+catalytic+subunit+alpha-1%2Fsubunit+beta-2%2Fsubunit+gamma-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50242401&enzyme=5%27-AMP-activated+protein+kinase+catalytic+subunit+alpha-1%2Fsubunit+beta-2%2Fsubunit+gamma-1&column=ki&startPg=0&Increment=50&submit=Search C1V 4CFF,4ZHX,5EZV 54708532 104099049 CHEMBL512504 3 METVISSDSSPAVENEHPQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDENDVVKGIVSLSDILQALVLTGGEKKP 8BIK,6C9H,6C9G,6C9F,5ISO,4CFF,4CFE,7MYJ,6B2E,6B1U,5EZV,4ZHX,6C9J,7M74,7JHH,7JHG,4REW,4RER,7JIJ,2UV5,2UV4 5'-AMP-activated protein kinase subunit gamma-1 AAKG1_HUMAN P54619 B4DDT7 Q8N7V9 MRRLSSWRKMATAEKQKHDGRVKIGHYILGDTLGVGTFGKVKVGKHELTGHKVAVKILNRQKIRSLDVVGKIRREIQNLKLFRHPHIIKLYQVISTPSDIFMVMEYVSGGELFDYICKNGRLDEKESRRLFQQILSGVDYCHRHMVVHRDLKPENVLLDAHMNAKIADFGLSNMMSDGEFLRTSCGSPNYAAPEVISGRLYAGPEVDIWSSGVILYALLCGTLPFDDDHVPTLFKKICDGIFYTPQYLNPSVISLLKHMLQVDPMKRATIKDIREHEWFKQDLPKYLFPEDPSYSSTMIDDEALKEVCEKFECSEEEVLSCLYNRNHQDPLAVAYHLIIDNRRIMNEAKDFYLATSPPDSFLDDHHLTRPHPERVPFLVAETPRARHTLDELNPQKSKHQGVRKAKWHLGIRSQSRPNDIMAEVCRAIKQLDYEWKVVNPYYLRVRRKNPVTSTYSKMSLQLYQVDSRTYLLDFRSIDDEITEAKSGTATPQRSGSVSNYRSCQRSDSDAEAQGKSSEVSLTSSVTSLDSSPVDLTPRPGSHTIEFFEMCANLIKILAQ 4REW,4RER,7M74,7JIJ,7JHH,7JHG 5'-AMP-activated protein kinase catalytic subunit alpha-1 AAPK1_HUMAN Q13131 A8MTQ6 B2R7E1 O00286 Q5D0E1 Q86VS1 Q9UNQ4 MGNTTSDRVSGERHGAKAARSEGAGGHAPGKEHKIMVGSTDDPSVFSLPDSKLPGDKEFVSWQQDLEDSVKPTQQARPTVIRWSEGGKEVFISGSFNNWSTKIPLIKSHNDFVAILDLPEGEHQYKFFVDGQWVHDPSEPVVTSQLGTINNLIHVKKSDFEVFDALKLDSMESSETSCRDLSSSPPGPYGQEMYAFRSEERFKSPPILPPHLLQVILNKDTNISCDPALLPEPNHVMLNHLYALSIKDSVMVLSATHRYKKKYVTTLLYKPI 6B2E,4REW,4RER,2LU4,2LU3,2F15,4CFH,2YA3,2Y8Q,2Y8L,2V9J,2V92,2V8Q,4EAJ,4EAI 5'-AMP-activated protein kinase subunit beta-2 AAKB2_HUMAN O43741 A8K9V5 B4DH06 Q5VXY0 51253823 c1ccc(c(c1)c2ccc(cc2)c3csc4c3C(=C(C(=O)N4)C#N)O)O InChI=1S/C20H12N2O3S/c21-9-14-18(24)17-15(10-26-20(17)22-19(14)25)12-7-5-11(6-8-12)13-3-1-2-4-16(13)23/h1-8,10,23H,(H2,22,24,25) CTESJDQKVOEUOY-UHFFFAOYSA-N 50242401 A-769662::4-hydroxy-3-(2'-hydroxybiphenyl-4-yl)-6-oxo-6,7-dihydrothieno[2,3-b]pyridine-5-carbonitrile::CHEMBL512504 5'-AMP-activated protein kinase catalytic subunit alpha-1/subunit beta-1/subunit gamma-1 Homo sapiens 800 ChEMBL 10.1016/j.bmcl.2019.07.035 10.7270/Q2QF8X6H 31358465 Babkov, DA; Zhukowskaya, ON; Borisov, AV; Babkova, VA; Sokolova, EV; Brigadirova, AA; Litvinov, RA; Kolodina, AA; Morkovnik, AS; Sochnev, VS; Borodkin, GS; Spasov, AA 9/1/2019 2/20/2021 Volgograd State Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50242401 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=14&target=5%27-AMP-activated+protein+kinase+catalytic+subunit+alpha-1%2Fsubunit+beta-1%2Fsubunit+gamma-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50242401&enzyme=5%27-AMP-activated+protein+kinase+catalytic+subunit+alpha-1%2Fsubunit+beta-1%2Fsubunit+gamma-1&column=ki&startPg=0&Increment=50&submit=Search C1V 4CFF,4ZHX,5EZV 54708532 104099049 CHEMBL512504 3 MGNTSSERAALERHGGHKTPRRDSSGGTKDGDRPKILMDSPEDADLFHSEEIKAPEKEEFLAWQHDLEVNDKAPAQARPTVFRWTGGGKEVYLSGSFNNWSKLPLTRSHNNFVAILDLPEGEHQYKFFVDGQWTHDPSEPIVTSQLGTVNNIIQVKKTDFEVFDALMVDSQKCSDVSELSSSPPGPYHQEPYVCKPEERFRAPPILPPHLLQVILNKDTGISCDPALLPEPNHVMLNHLYALSIKDGVMVLSATHRYKKKYVTTLLYKPI 8BIK,7MYJ,6B1U,5EZV,4ZHX,5ISO,4CFF,4CFE,6C9J,6C9H,6C9G,6C9F 5'-AMP-activated protein kinase subunit beta-1 AAKB1_HUMAN Q9Y478 Q9UBV0 Q9UE20 Q9UEX2 Q9Y6V8 METVISSDSSPAVENEHPQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDENDVVKGIVSLSDILQALVLTGGEKKP 8BIK,6C9H,6C9G,6C9F,5ISO,4CFF,4CFE,7MYJ,6B2E,6B1U,5EZV,4ZHX,6C9J,7M74,7JHH,7JHG,4REW,4RER,7JIJ,2UV5,2UV4 5'-AMP-activated protein kinase subunit gamma-1 AAKG1_HUMAN P54619 B4DDT7 Q8N7V9 MRRLSSWRKMATAEKQKHDGRVKIGHYILGDTLGVGTFGKVKVGKHELTGHKVAVKILNRQKIRSLDVVGKIRREIQNLKLFRHPHIIKLYQVISTPSDIFMVMEYVSGGELFDYICKNGRLDEKESRRLFQQILSGVDYCHRHMVVHRDLKPENVLLDAHMNAKIADFGLSNMMSDGEFLRTSCGSPNYAAPEVISGRLYAGPEVDIWSSGVILYALLCGTLPFDDDHVPTLFKKICDGIFYTPQYLNPSVISLLKHMLQVDPMKRATIKDIREHEWFKQDLPKYLFPEDPSYSSTMIDDEALKEVCEKFECSEEEVLSCLYNRNHQDPLAVAYHLIIDNRRIMNEAKDFYLATSPPDSFLDDHHLTRPHPERVPFLVAETPRARHTLDELNPQKSKHQGVRKAKWHLGIRSQSRPNDIMAEVCRAIKQLDYEWKVVNPYYLRVRRKNPVTSTYSKMSLQLYQVDSRTYLLDFRSIDDEITEAKSGTATPQRSGSVSNYRSCQRSDSDAEAQGKSSEVSLTSSVTSLDSSPVDLTPRPGSHTIEFFEMCANLIKILAQ 4REW,4RER,7M74,7JIJ,7JHH,7JHG 5'-AMP-activated protein kinase catalytic subunit alpha-1 AAPK1_HUMAN Q13131 A8MTQ6 B2R7E1 O00286 Q5D0E1 Q86VS1 Q9UNQ4 50521692 c1ccc(c(c1)c2ccc(cc2)c3csc4c3C(=C(C(=O)N4)C#N)O)O InChI=1S/C20H12N2O3S/c21-9-14-18(24)17-15(10-26-20(17)22-19(14)25)12-7-5-11(6-8-12)13-3-1-2-4-16(13)23/h1-8,10,23H,(H2,22,24,25) CTESJDQKVOEUOY-UHFFFAOYSA-N 50242401 A-769662::4-hydroxy-3-(2'-hydroxybiphenyl-4-yl)-6-oxo-6,7-dihydrothieno[2,3-b]pyridine-5-carbonitrile::CHEMBL512504 5'-AMP-activated protein kinase catalytic subunit alpha-1/subunit beta-1/subunit gamma-1 Homo sapiens 487 ChEMBL 10.1016/j.bmcl.2016.09.065 10.7270/Q25M67PH 27727125 Cameron, KO; Kurumbail, RG 11/1/2016 7/9/2018 Pfizer http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50242401 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=14&target=5%27-AMP-activated+protein+kinase+catalytic+subunit+alpha-1%2Fsubunit+beta-1%2Fsubunit+gamma-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50242401&enzyme=5%27-AMP-activated+protein+kinase+catalytic+subunit+alpha-1%2Fsubunit+beta-1%2Fsubunit+gamma-1&column=ki&startPg=0&Increment=50&submit=Search C1V 4CFF,4ZHX,5EZV 54708532 104099049 CHEMBL512504 3 MGNTSSERAALERHGGHKTPRRDSSGGTKDGDRPKILMDSPEDADLFHSEEIKAPEKEEFLAWQHDLEVNDKAPAQARPTVFRWTGGGKEVYLSGSFNNWSKLPLTRSHNNFVAILDLPEGEHQYKFFVDGQWTHDPSEPIVTSQLGTVNNIIQVKKTDFEVFDALMVDSQKCSDVSELSSSPPGPYHQEPYVCKPEERFRAPPILPPHLLQVILNKDTGISCDPALLPEPNHVMLNHLYALSIKDGVMVLSATHRYKKKYVTTLLYKPI 8BIK,7MYJ,6B1U,5EZV,4ZHX,5ISO,4CFF,4CFE,6C9J,6C9H,6C9G,6C9F 5'-AMP-activated protein kinase subunit beta-1 AAKB1_HUMAN Q9Y478 Q9UBV0 Q9UE20 Q9UEX2 Q9Y6V8 METVISSDSSPAVENEHPQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDENDVVKGIVSLSDILQALVLTGGEKKP 8BIK,6C9H,6C9G,6C9F,5ISO,4CFF,4CFE,7MYJ,6B2E,6B1U,5EZV,4ZHX,6C9J,7M74,7JHH,7JHG,4REW,4RER,7JIJ,2UV5,2UV4 5'-AMP-activated protein kinase subunit gamma-1 AAKG1_HUMAN P54619 B4DDT7 Q8N7V9 MRRLSSWRKMATAEKQKHDGRVKIGHYILGDTLGVGTFGKVKVGKHELTGHKVAVKILNRQKIRSLDVVGKIRREIQNLKLFRHPHIIKLYQVISTPSDIFMVMEYVSGGELFDYICKNGRLDEKESRRLFQQILSGVDYCHRHMVVHRDLKPENVLLDAHMNAKIADFGLSNMMSDGEFLRTSCGSPNYAAPEVISGRLYAGPEVDIWSSGVILYALLCGTLPFDDDHVPTLFKKICDGIFYTPQYLNPSVISLLKHMLQVDPMKRATIKDIREHEWFKQDLPKYLFPEDPSYSSTMIDDEALKEVCEKFECSEEEVLSCLYNRNHQDPLAVAYHLIIDNRRIMNEAKDFYLATSPPDSFLDDHHLTRPHPERVPFLVAETPRARHTLDELNPQKSKHQGVRKAKWHLGIRSQSRPNDIMAEVCRAIKQLDYEWKVVNPYYLRVRRKNPVTSTYSKMSLQLYQVDSRTYLLDFRSIDDEITEAKSGTATPQRSGSVSNYRSCQRSDSDAEAQGKSSEVSLTSSVTSLDSSPVDLTPRPGSHTIEFFEMCANLIKILAQ 4REW,4RER,7M74,7JIJ,7JHH,7JHG 5'-AMP-activated protein kinase catalytic subunit alpha-1 AAPK1_HUMAN Q13131 A8MTQ6 B2R7E1 O00286 Q5D0E1 Q86VS1 Q9UNQ4 51118972 c1ccc(c(c1)c2ccc(cc2)c3csc4c3C(=C(C(=O)N4)C#N)O)O InChI=1S/C20H12N2O3S/c21-9-14-18(24)17-15(10-26-20(17)22-19(14)25)12-7-5-11(6-8-12)13-3-1-2-4-16(13)23/h1-8,10,23H,(H2,22,24,25) CTESJDQKVOEUOY-UHFFFAOYSA-N 50242401 A-769662::4-hydroxy-3-(2'-hydroxybiphenyl-4-yl)-6-oxo-6,7-dihydrothieno[2,3-b]pyridine-5-carbonitrile::CHEMBL512504 5'-AMP-activated protein kinase catalytic subunit alpha-2/subunit beta-1/subunit gamma-1 Homo sapiens 390 ChEMBL 10.1021/acs.jmedchem.8b00180 10.7270/Q2DJ5J62 29620890 Young, RJ; Leeson, PD 8/9/2018 8/16/2020 Glaxosmithkline http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50242401 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000057&target=5%27-AMP-activated+protein+kinase+catalytic+subunit+alpha-2%2Fsubunit+beta-1%2Fsubunit+gamma-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50242401&enzyme=5%27-AMP-activated+protein+kinase+catalytic+subunit+alpha-2%2Fsubunit+beta-1%2Fsubunit+gamma-1&column=ki&startPg=0&Increment=50&submit=Search C1V 4CFF,4ZHX,5EZV 54708532 104099049 CHEMBL512504 3 MGNTSSERAALERHGGHKTPRRDSSGGTKDGDRPKILMDSPEDADLFHSEEIKAPEKEEFLAWQHDLEVNDKAPAQARPTVFRWTGGGKEVYLSGSFNNWSKLPLTRSHNNFVAILDLPEGEHQYKFFVDGQWTHDPSEPIVTSQLGTVNNIIQVKKTDFEVFDALMVDSQKCSDVSELSSSPPGPYHQEPYVCKPEERFRAPPILPPHLLQVILNKDTGISCDPALLPEPNHVMLNHLYALSIKDGVMVLSATHRYKKKYVTTLLYKPI 8BIK,7MYJ,6B1U,5EZV,4ZHX,5ISO,4CFF,4CFE,6C9J,6C9H,6C9G,6C9F 5'-AMP-activated protein kinase subunit beta-1 AAKB1_HUMAN Q9Y478 Q9UBV0 Q9UE20 Q9UEX2 Q9Y6V8 METVISSDSSPAVENEHPQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDENDVVKGIVSLSDILQALVLTGGEKKP 8BIK,6C9H,6C9G,6C9F,5ISO,4CFF,4CFE,7MYJ,6B2E,6B1U,5EZV,4ZHX,6C9J,7M74,7JHH,7JHG,4REW,4RER,7JIJ,2UV5,2UV4 5'-AMP-activated protein kinase subunit gamma-1 AAKG1_HUMAN P54619 B4DDT7 Q8N7V9 MAEKQKHDGRVKIGHYVLGDTLGVGTFGKVKIGEHQLTGHKVAVKILNRQKIRSLDVVGKIKREIQNLKLFRHPHIIKLYQVISTPTDFFMVMEYVSGGELFDYICKHGRVEEMEARRLFQQILSAVDYCHRHMVVHRDLKPENVLLDAHMNAKIADFGLSNMMSDGEFLRTSCGSPNYAAPEVISGRLYAGPEVDIWSCGVILYALLCGTLPFDDEHVPTLFKKIRGGVFYIPEYLNRSVATLLMHMLQVDPLKRATIKDIREHEWFKQDLPSYLFPEDPSYDANVIDDEAVKEVCEKFECTESEVMNSLYSGDPQDQLAVAYHLIIDNRRIMNQASEFYLASSPPSGSFMDDSAMHIPPGLKPHPERMPPLIADSPKARCPLDALNTTKPKSLAVKKAKWHLGIRSQSKPYDIMAEVYRAMKQLDFEWKVVNAYHLRVRRKNPVTGNYVKMSLQLYLVDNRSYLLDFKSIDDEVVEQRSGSSTPQRSCSAAGLHRPRSSFDSTTAESHSLSGSLTGSLTGSTLSSVSPRLGSHTMDFFEMCASLITTLAR 5ISO,8BIK,4CFF,4CFE,9IC2,2H6D 5'-AMP-activated protein kinase catalytic subunit alpha-2 AAPK2_HUMAN P54646 Q9H1E8 Q9UD43 51219552 c1ccc(c(c1)c2ccc(cc2)c3csc4c3C(=C(C(=O)N4)C#N)O)O InChI=1S/C20H12N2O3S/c21-9-14-18(24)17-15(10-26-20(17)22-19(14)25)12-7-5-11(6-8-12)13-3-1-2-4-16(13)23/h1-8,10,23H,(H2,22,24,25) CTESJDQKVOEUOY-UHFFFAOYSA-N 50242401 A-769662::4-hydroxy-3-(2'-hydroxybiphenyl-4-yl)-6-oxo-6,7-dihydrothieno[2,3-b]pyridine-5-carbonitrile::CHEMBL512504 5'-AMP-activated protein kinase catalytic subunit alpha-1/subunit beta-1/subunit gamma-1 Homo sapiens 510 ChEMBL 10.1021/acs.jmedchem.5b01201 10.7270/Q26976KB 26510622 Miglianico, M; Nicolaes, GA; Neumann, D 4/14/2016 9/4/2020 Maastricht University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50242401 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=14&target=5%27-AMP-activated+protein+kinase+catalytic+subunit+alpha-1%2Fsubunit+beta-1%2Fsubunit+gamma-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50242401&enzyme=5%27-AMP-activated+protein+kinase+catalytic+subunit+alpha-1%2Fsubunit+beta-1%2Fsubunit+gamma-1&column=ki&startPg=0&Increment=50&submit=Search C1V 4CFF,4ZHX,5EZV 54708532 104099049 CHEMBL512504 3 MGNTSSERAALERHGGHKTPRRDSSGGTKDGDRPKILMDSPEDADLFHSEEIKAPEKEEFLAWQHDLEVNDKAPAQARPTVFRWTGGGKEVYLSGSFNNWSKLPLTRSHNNFVAILDLPEGEHQYKFFVDGQWTHDPSEPIVTSQLGTVNNIIQVKKTDFEVFDALMVDSQKCSDVSELSSSPPGPYHQEPYVCKPEERFRAPPILPPHLLQVILNKDTGISCDPALLPEPNHVMLNHLYALSIKDGVMVLSATHRYKKKYVTTLLYKPI 8BIK,7MYJ,6B1U,5EZV,4ZHX,5ISO,4CFF,4CFE,6C9J,6C9H,6C9G,6C9F 5'-AMP-activated protein kinase subunit beta-1 AAKB1_HUMAN Q9Y478 Q9UBV0 Q9UE20 Q9UEX2 Q9Y6V8 METVISSDSSPAVENEHPQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDENDVVKGIVSLSDILQALVLTGGEKKP 8BIK,6C9H,6C9G,6C9F,5ISO,4CFF,4CFE,7MYJ,6B2E,6B1U,5EZV,4ZHX,6C9J,7M74,7JHH,7JHG,4REW,4RER,7JIJ,2UV5,2UV4 5'-AMP-activated protein kinase subunit gamma-1 AAKG1_HUMAN P54619 B4DDT7 Q8N7V9 MRRLSSWRKMATAEKQKHDGRVKIGHYILGDTLGVGTFGKVKVGKHELTGHKVAVKILNRQKIRSLDVVGKIRREIQNLKLFRHPHIIKLYQVISTPSDIFMVMEYVSGGELFDYICKNGRLDEKESRRLFQQILSGVDYCHRHMVVHRDLKPENVLLDAHMNAKIADFGLSNMMSDGEFLRTSCGSPNYAAPEVISGRLYAGPEVDIWSSGVILYALLCGTLPFDDDHVPTLFKKICDGIFYTPQYLNPSVISLLKHMLQVDPMKRATIKDIREHEWFKQDLPKYLFPEDPSYSSTMIDDEALKEVCEKFECSEEEVLSCLYNRNHQDPLAVAYHLIIDNRRIMNEAKDFYLATSPPDSFLDDHHLTRPHPERVPFLVAETPRARHTLDELNPQKSKHQGVRKAKWHLGIRSQSRPNDIMAEVCRAIKQLDYEWKVVNPYYLRVRRKNPVTSTYSKMSLQLYQVDSRTYLLDFRSIDDEITEAKSGTATPQRSGSVSNYRSCQRSDSDAEAQGKSSEVSLTSSVTSLDSSPVDLTPRPGSHTIEFFEMCANLIKILAQ 4REW,4RER,7M74,7JIJ,7JHH,7JHG 5'-AMP-activated protein kinase catalytic subunit alpha-1 AAPK1_HUMAN Q13131 A8MTQ6 B2R7E1 O00286 Q5D0E1 Q86VS1 Q9UNQ4 51219553 c1ccc(c(c1)c2ccc(cc2)c3csc4c3C(=C(C(=O)N4)C#N)O)O InChI=1S/C20H12N2O3S/c21-9-14-18(24)17-15(10-26-20(17)22-19(14)25)12-7-5-11(6-8-12)13-3-1-2-4-16(13)23/h1-8,10,23H,(H2,22,24,25) CTESJDQKVOEUOY-UHFFFAOYSA-N 50242401 A-769662::4-hydroxy-3-(2'-hydroxybiphenyl-4-yl)-6-oxo-6,7-dihydrothieno[2,3-b]pyridine-5-carbonitrile::CHEMBL512504 5'-AMP-activated protein kinase catalytic subunit alpha-1/subunit beta-2/subunit gamma-1 Homo sapiens 14500 ChEMBL 10.1021/acs.jmedchem.5b01201 10.7270/Q26976KB 26510622 Miglianico, M; Nicolaes, GA; Neumann, D 4/14/2016 9/4/2020 Maastricht University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50242401 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50004248&target=5%27-AMP-activated+protein+kinase+catalytic+subunit+alpha-1%2Fsubunit+beta-2%2Fsubunit+gamma-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50242401&enzyme=5%27-AMP-activated+protein+kinase+catalytic+subunit+alpha-1%2Fsubunit+beta-2%2Fsubunit+gamma-1&column=ki&startPg=0&Increment=50&submit=Search C1V 4CFF,4ZHX,5EZV 54708532 104099049 CHEMBL512504 3 METVISSDSSPAVENEHPQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDENDVVKGIVSLSDILQALVLTGGEKKP 8BIK,6C9H,6C9G,6C9F,5ISO,4CFF,4CFE,7MYJ,6B2E,6B1U,5EZV,4ZHX,6C9J,7M74,7JHH,7JHG,4REW,4RER,7JIJ,2UV5,2UV4 5'-AMP-activated protein kinase subunit gamma-1 AAKG1_HUMAN P54619 B4DDT7 Q8N7V9 MRRLSSWRKMATAEKQKHDGRVKIGHYILGDTLGVGTFGKVKVGKHELTGHKVAVKILNRQKIRSLDVVGKIRREIQNLKLFRHPHIIKLYQVISTPSDIFMVMEYVSGGELFDYICKNGRLDEKESRRLFQQILSGVDYCHRHMVVHRDLKPENVLLDAHMNAKIADFGLSNMMSDGEFLRTSCGSPNYAAPEVISGRLYAGPEVDIWSSGVILYALLCGTLPFDDDHVPTLFKKICDGIFYTPQYLNPSVISLLKHMLQVDPMKRATIKDIREHEWFKQDLPKYLFPEDPSYSSTMIDDEALKEVCEKFECSEEEVLSCLYNRNHQDPLAVAYHLIIDNRRIMNEAKDFYLATSPPDSFLDDHHLTRPHPERVPFLVAETPRARHTLDELNPQKSKHQGVRKAKWHLGIRSQSRPNDIMAEVCRAIKQLDYEWKVVNPYYLRVRRKNPVTSTYSKMSLQLYQVDSRTYLLDFRSIDDEITEAKSGTATPQRSGSVSNYRSCQRSDSDAEAQGKSSEVSLTSSVTSLDSSPVDLTPRPGSHTIEFFEMCANLIKILAQ 4REW,4RER,7M74,7JIJ,7JHH,7JHG 5'-AMP-activated protein kinase catalytic subunit alpha-1 AAPK1_HUMAN Q13131 A8MTQ6 B2R7E1 O00286 Q5D0E1 Q86VS1 Q9UNQ4 MGNTTSDRVSGERHGAKAARSEGAGGHAPGKEHKIMVGSTDDPSVFSLPDSKLPGDKEFVSWQQDLEDSVKPTQQARPTVIRWSEGGKEVFISGSFNNWSTKIPLIKSHNDFVAILDLPEGEHQYKFFVDGQWVHDPSEPVVTSQLGTINNLIHVKKSDFEVFDALKLDSMESSETSCRDLSSSPPGPYGQEMYAFRSEERFKSPPILPPHLLQVILNKDTNISCDPALLPEPNHVMLNHLYALSIKDSVMVLSATHRYKKKYVTTLLYKPI 6B2E,4REW,4RER,2LU4,2LU3,2F15,4CFH,2YA3,2Y8Q,2Y8L,2V9J,2V92,2V8Q,4EAJ,4EAI 5'-AMP-activated protein kinase subunit beta-2 AAKB2_HUMAN O43741 A8K9V5 B4DH06 Q5VXY0 51253823 c1ccc(c(c1)c2ccc(cc2)c3csc4c3C(=C(C(=O)N4)C#N)O)O InChI=1S/C20H12N2O3S/c21-9-14-18(24)17-15(10-26-20(17)22-19(14)25)12-7-5-11(6-8-12)13-3-1-2-4-16(13)23/h1-8,10,23H,(H2,22,24,25) CTESJDQKVOEUOY-UHFFFAOYSA-N 50242401 A-769662::4-hydroxy-3-(2'-hydroxybiphenyl-4-yl)-6-oxo-6,7-dihydrothieno[2,3-b]pyridine-5-carbonitrile::CHEMBL512504 5'-AMP-activated protein kinase catalytic subunit alpha-1/subunit beta-1/subunit gamma-1 Homo sapiens 800 ChEMBL 10.1016/j.bmcl.2019.07.035 10.7270/Q2QF8X6H 31358465 Babkov, DA; Zhukowskaya, ON; Borisov, AV; Babkova, VA; Sokolova, EV; Brigadirova, AA; Litvinov, RA; Kolodina, AA; Morkovnik, AS; Sochnev, VS; Borodkin, GS; Spasov, AA 9/1/2019 2/20/2021 Volgograd State Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50242401 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=14&target=5%27-AMP-activated+protein+kinase+catalytic+subunit+alpha-1%2Fsubunit+beta-1%2Fsubunit+gamma-1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50242401&enzyme=5%27-AMP-activated+protein+kinase+catalytic+subunit+alpha-1%2Fsubunit+beta-1%2Fsubunit+gamma-1&column=ki&startPg=0&Increment=50&submit=Search C1V 4CFF,4ZHX,5EZV 54708532 104099049 CHEMBL512504 3 MGNTSSERAALERHGGHKTPRRDSSGGTKDGDRPKILMDSPEDADLFHSEEIKAPEKEEFLAWQHDLEVNDKAPAQARPTVFRWTGGGKEVYLSGSFNNWSKLPLTRSHNNFVAILDLPEGEHQYKFFVDGQWTHDPSEPIVTSQLGTVNNIIQVKKTDFEVFDALMVDSQKCSDVSELSSSPPGPYHQEPYVCKPEERFRAPPILPPHLLQVILNKDTGISCDPALLPEPNHVMLNHLYALSIKDGVMVLSATHRYKKKYVTTLLYKPI 8BIK,7MYJ,6B1U,5EZV,4ZHX,5ISO,4CFF,4CFE,6C9J,6C9H,6C9G,6C9F 5'-AMP-activated protein kinase subunit beta-1 AAKB1_HUMAN Q9Y478 Q9UBV0 Q9UE20 Q9UEX2 Q9Y6V8 METVISSDSSPAVENEHPQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDENDVVKGIVSLSDILQALVLTGGEKKP 8BIK,6C9H,6C9G,6C9F,5ISO,4CFF,4CFE,7MYJ,6B2E,6B1U,5EZV,4ZHX,6C9J,7M74,7JHH,7JHG,4REW,4RER,7JIJ,2UV5,2UV4 5'-AMP-activated protein kinase subunit gamma-1 AAKG1_HUMAN P54619 B4DDT7 Q8N7V9 MRRLSSWRKMATAEKQKHDGRVKIGHYILGDTLGVGTFGKVKVGKHELTGHKVAVKILNRQKIRSLDVVGKIRREIQNLKLFRHPHIIKLYQVISTPSDIFMVMEYVSGGELFDYICKNGRLDEKESRRLFQQILSGVDYCHRHMVVHRDLKPENVLLDAHMNAKIADFGLSNMMSDGEFLRTSCGSPNYAAPEVISGRLYAGPEVDIWSSGVILYALLCGTLPFDDDHVPTLFKKICDGIFYTPQYLNPSVISLLKHMLQVDPMKRATIKDIREHEWFKQDLPKYLFPEDPSYSSTMIDDEALKEVCEKFECSEEEVLSCLYNRNHQDPLAVAYHLIIDNRRIMNEAKDFYLATSPPDSFLDDHHLTRPHPERVPFLVAETPRARHTLDELNPQKSKHQGVRKAKWHLGIRSQSRPNDIMAEVCRAIKQLDYEWKVVNPYYLRVRRKNPVTSTYSKMSLQLYQVDSRTYLLDFRSIDDEITEAKSGTATPQRSGSVSNYRSCQRSDSDAEAQGKSSEVSLTSSVTSLDSSPVDLTPRPGSHTIEFFEMCANLIKILAQ 4REW,4RER,7M74,7JIJ,7JHH,7JHG 5'-AMP-activated protein kinase catalytic subunit alpha-1 AAPK1_HUMAN Q13131 A8MTQ6 B2R7E1 O00286 Q5D0E1 Q86VS1 Q9UNQ4 50060673 CC[C@@]1(C2=C(COC1=O)C(=O)N3Cc4cc5ccccc5nc4C3=C2)O InChI=1S/C20H16N2O4/c1-2-20(25)14-8-16-17-12(7-11-5-3-4-6-15(11)21-17)9-22(16)18(23)13(14)10-26-19(20)24/h3-8,25H,2,9-10H2,1H3 VSJKWCGYPAHWDS-UHFFFAOYSA-N 50045363 4-ethyl-4-hydroxy-1,12-dihydro-4H-2-oxa-6,12a-diaza-dibenzo[b,h]fluorene-3,13-dione::(20R)-4-Ethyl-4-hydroxy-1,12-dihydro-4H-2-oxa-6,12a-diaza-dibenzo[b,h]fluorene-3,13-dione::4-ethyl-4-hydroxy-3,4,12,14-tetrahydro-1H-pyrano[3',4':6,7]indolizino[1,2-b]quinoline-3,14-dione::(20RS)-4-Ethyl-4-hydroxy-1,12-dihydro-4H-2-oxa-6,12a-diaza-dibenzo[b,h]fluorene-3,13-dione::CHEMBL276820 DNA topoisomerase 1 Homo sapiens 1400 ChEMBL 10.1021/jm00070a013 10.7270/Q2KP82RH 8410981 Wall, ME; Wani, MC; Nicholas, AW; Manikumar, G; Tele, C; Moore, L; Truesdale, A; Leitner, P; Besterman, JM 10/29/1993 10/25/2012 Research Triangle Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50045363 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10784&target=DNA+topoisomerase+1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50045363&enzyme=DNA+topoisomerase+1&column=ki&startPg=0&Increment=50&submit=Search EHD 1T8I 2538 103976412 CHEMBL276820 1 MSGDHLHNDSQIEADFRLNDSHKHKDKHKDREHRHKEHKKEKDREKSKHSNSEHKDSEKKHKEKEKTKHKDGSSEKHKDKHKDRDKEKRKEEKVRASGDAKIKKEKENGFSSPPQIKDEPEDDGYFVPPKEDIKPLKRPRDEDDADYKPKKIKTEDTKKEKKRKLEEEEDGKLKKPKNKDKDKKVPEPDNKKKKPKKEEEQKWKWWEEERYPEGIKWKFLEHKGPVFAPPYEPLPENVKFYYDGKVMKLSPKAEEVATFFAKMLDHEYTTKEIFRKNFFKDWRKEMTNEEKNIITNLSKCDFTQMSQYFKAQTEARKQMSKEEKLKIKEENEKLLKEYGFCIMDNHKERIANFKIEPPGLFRGRGNHPKMGMLKRRIMPEDIIINCSKDAKVPSPPPGHKWKEVRHDNKVTWLVSWTENIQGSIKYIMLNPSSRIKGEKDWQKYETARRLKKCVDKIRNQYREDWKSKEMKVRQRAVALYFIDKLALRAGNEKEEGETADTVGCCSLRVEHINLHPELDGQEYVVEFDFLGKDSIRYYNKVPVEKRVFKNLQLFMENKQPEDDLFDRLNTGILNKHLQDLMEGLTAKVFRTYNASITLQQQLKELTAPDENIPAKILSYNRANRAVAILCNHQRAPPKTFEKSMMNLQTKIDAKKEQLADARRDLKSAKADAKVMKDAKTKKVVESKKKAVQRLEEQLMKLEVQATDREENKQIALGTSKLNYLDPRITVAWCKKWGVPIEKIYNKTQREKFAWAIDMADEDYEF 1TL8,1T8I,1SC7,1K4T,1K4S,1A31,1NH3 DNA topoisomerase 1 TOP1_HUMAN P11387 A8KA78 E1P5W3 O43256 Q12855 Q12856 Q15610 Q5TFY3 Q9UJN0 50671646 CC[C@@]1(C2=C(COC1=O)C(=O)N3Cc4cc5ccccc5nc4C3=C2)O InChI=1S/C20H16N2O4/c1-2-20(25)14-8-16-17-12(7-11-5-3-4-6-15(11)21-17)9-22(16)18(23)13(14)10-26-19(20)24/h3-8,25H,2,9-10H2,1H3 VSJKWCGYPAHWDS-UHFFFAOYSA-N 50045363 4-ethyl-4-hydroxy-1,12-dihydro-4H-2-oxa-6,12a-diaza-dibenzo[b,h]fluorene-3,13-dione::(20R)-4-Ethyl-4-hydroxy-1,12-dihydro-4H-2-oxa-6,12a-diaza-dibenzo[b,h]fluorene-3,13-dione::4-ethyl-4-hydroxy-3,4,12,14-tetrahydro-1H-pyrano[3',4':6,7]indolizino[1,2-b]quinoline-3,14-dione::(20RS)-4-Ethyl-4-hydroxy-1,12-dihydro-4H-2-oxa-6,12a-diaza-dibenzo[b,h]fluorene-3,13-dione::CHEMBL276820 DNA topoisomerase 1 Homo sapiens 1600 ChEMBL 10.1021/jm00070a013 10.7270/Q2KP82RH 8410981 Wall, ME; Wani, MC; Nicholas, AW; Manikumar, G; Tele, C; Moore, L; Truesdale, A; Leitner, P; Besterman, JM 10/29/1993 10/25/2012 Research Triangle Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50045363 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10784&target=DNA+topoisomerase+1&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50045363&enzyme=DNA+topoisomerase+1&column=ki&startPg=0&Increment=50&submit=Search EHD 1T8I 2538 103976412 CHEMBL276820 1 MSGDHLHNDSQIEADFRLNDSHKHKDKHKDREHRHKEHKKEKDREKSKHSNSEHKDSEKKHKEKEKTKHKDGSSEKHKDKHKDRDKEKRKEEKVRASGDAKIKKEKENGFSSPPQIKDEPEDDGYFVPPKEDIKPLKRPRDEDDADYKPKKIKTEDTKKEKKRKLEEEEDGKLKKPKNKDKDKKVPEPDNKKKKPKKEEEQKWKWWEEERYPEGIKWKFLEHKGPVFAPPYEPLPENVKFYYDGKVMKLSPKAEEVATFFAKMLDHEYTTKEIFRKNFFKDWRKEMTNEEKNIITNLSKCDFTQMSQYFKAQTEARKQMSKEEKLKIKEENEKLLKEYGFCIMDNHKERIANFKIEPPGLFRGRGNHPKMGMLKRRIMPEDIIINCSKDAKVPSPPPGHKWKEVRHDNKVTWLVSWTENIQGSIKYIMLNPSSRIKGEKDWQKYETARRLKKCVDKIRNQYREDWKSKEMKVRQRAVALYFIDKLALRAGNEKEEGETADTVGCCSLRVEHINLHPELDGQEYVVEFDFLGKDSIRYYNKVPVEKRVFKNLQLFMENKQPEDDLFDRLNTGILNKHLQDLMEGLTAKVFRTYNASITLQQQLKELTAPDENIPAKILSYNRANRAVAILCNHQRAPPKTFEKSMMNLQTKIDAKKEQLADARRDLKSAKADAKVMKDAKTKKVVESKKKAVQRLEEQLMKLEVQATDREENKQIALGTSKLNYLDPRITVAWCKKWGVPIEKIYNKTQREKFAWAIDMADEDYEF 1TL8,1T8I,1SC7,1K4T,1K4S,1A31,1NH3 DNA topoisomerase 1 TOP1_HUMAN P11387 A8KA78 E1P5W3 O43256 Q12855 Q12856 Q15610 Q5TFY3 Q9UJN0 50404083 CSC[C@@H]1CN(Cc2c[nH]c3c(N)ncnc23)C[C@H]1O InChI=1S/C13H19N5OS/c1-20-6-9-4-18(5-10(9)19)3-8-2-15-12-11(8)16-7-17-13(12)14/h2,7,9-10,15,19H,3-6H2,1H3,(H2,14,16,17) NTHMDFGHOCNNOE-UHFFFAOYSA-N 50116357 CHEMBL3604360 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase Escherichia coli 4.5 ChEMBL 10.1016/j.bmc.2015.07.059 10.7270/Q2HX1FF5 26260335 Evans, GB; Cameron, SA; Luxenburger, A; Guan, R; Suarez, J; Thomas, K; Schramm, VL; Tyler, PC 8/31/2015 11/26/2016 Victoria University of Wellington http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50116357 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50006954&target=5%27-methylthioadenosine%2FS-adenosylhomocysteine+nucleosidase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50116357&enzyme=5%27-methylthioadenosine%2FS-adenosylhomocysteine+nucleosidase&column=ki&startPg=0&Increment=50&submit=Search 4F0 4YML 91827502 319494239 CHEMBL3604360 1 MKIGIIGAMEEEVTLLRDKIEKRQTISLGGCEIYTGQLNGTEVALLKSGIGKVAAALGATLLLEHCKPDVIINTGSAGGLAPTLKVGDIVVSDEARYHDADVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNLNAVRGLIVSGDAFINGSVGLAKIRHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVESLVQKLAHG N/A J7QX79 50237675 CN1CCC(c2c[nH]c3ccc(NC(=O)c4ccc(F)cc4)cc23)CC1 InChI=1S/C21H22FN3O/c1-25-10-8-14(9-11-25)19-13-23-20-7-6-17(12-18(19)20)24-21(26)15-2-4-16(22)5-3-15/h2-7,12-14,23H,8-11H2,1H3,(H,24,26) MDMJLMDBRQXOOI-UHFFFAOYSA-N 50130461 LY-334370::4-Fluoro-N-[3-(1-methyl-piperidin-4-yl)-1H-indol-5-yl]-benzamide::4-Fluoro-N-[3-(1-methyl-4-piperidinyl)-1H-indol-5-yl]benzamide::CHEMBL101690 5-hydroxytryptamine receptor 1F Homo sapiens 2.1 ChEMBL 10.1021/jm030020m 10.7270/Q21V5DCB 12825944 Filla, SA; Mathes, BM; Johnson, KW; Phebus, LA; Cohen, ML; Nelson, DL; Zgombick, JM; Erickson, JA; Schenck, KW; Wainscott, DB; Branchek, TA; Schaus, JM 6/26/2003 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50130461 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=49000035&target=5-hydroxytryptamine+receptor+1F&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50130461&enzyme=5-hydroxytryptamine+receptor+1F&column=ki&startPg=0&Increment=50&submit=Search A1E2G 21AG,21AH 5311258 104021837 CHEMBL101690 1 MDFLNSSDQNLTSEELLNRMPSKILVSLTLSGLALMTTTINSLVIAAIIVTRKLHHPANYLICSLAVTDFLVAVLVMPFSIVYIVRESWIMGQVVCDIWLSVDITCCTCSILHLSAIALDRYRAITDAVEYARKRTPKHAGIMITIVWIISVFISMPPLFWRHQGTSRDDECIIKHDHIVSTIYSTFGAFYIPLALILILYYKIYRAAKTLYHKRQASRIAKEEVNGQVLLESGEKSTKSVSTSYVLEKSLSDPSTDFDKIHSTVRSLRSEFKHEKSWRRQKISGTRERKAATTLGLILGAFVICWLPFFVKELVVNVCDKCKISEEMSNFLAWLGYLNSLINPLIYTIFNEDFKKAFQKLVRCRC 7EXD,21AH,21AG 5-hydroxytryptamine receptor 1F 5HT1F_HUMAN P30939 50252050 CN1CCC(c2c[nH]c3ccc(NC(=O)c4ccc(F)cc4)cc23)CC1 InChI=1S/C21H22FN3O/c1-25-10-8-14(9-11-25)19-13-23-20-7-6-17(12-18(19)20)24-21(26)15-2-4-16(22)5-3-15/h2-7,12-14,23H,8-11H2,1H3,(H,24,26) MDMJLMDBRQXOOI-UHFFFAOYSA-N 50130461 LY-334370::4-Fluoro-N-[3-(1-methyl-piperidin-4-yl)-1H-indol-5-yl]-benzamide::4-Fluoro-N-[3-(1-methyl-4-piperidinyl)-1H-indol-5-yl]benzamide::CHEMBL101690 5-hydroxytryptamine receptor 1F Homo sapiens 1.6 ChEMBL 10.1016/j.bmcl.2003.09.091 10.7270/Q2S46RCF 14684321 Mathes, BM; Hudziak, KJ; Schaus, JM; Xu, YC; Nelson, DL; Wainscott, DB; Nutter, SE; Gough, WH; Branchek, TA; Zgombick, JM; Filla, SA 12/19/2003 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50130461 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=49000035&target=5-hydroxytryptamine+receptor+1F&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50130461&enzyme=5-hydroxytryptamine+receptor+1F&column=ki&startPg=0&Increment=50&submit=Search A1E2G 21AG,21AH 5311258 104021837 CHEMBL101690 1 MDFLNSSDQNLTSEELLNRMPSKILVSLTLSGLALMTTTINSLVIAAIIVTRKLHHPANYLICSLAVTDFLVAVLVMPFSIVYIVRESWIMGQVVCDIWLSVDITCCTCSILHLSAIALDRYRAITDAVEYARKRTPKHAGIMITIVWIISVFISMPPLFWRHQGTSRDDECIIKHDHIVSTIYSTFGAFYIPLALILILYYKIYRAAKTLYHKRQASRIAKEEVNGQVLLESGEKSTKSVSTSYVLEKSLSDPSTDFDKIHSTVRSLRSEFKHEKSWRRQKISGTRERKAATTLGLILGAFVICWLPFFVKELVVNVCDKCKISEEMSNFLAWLGYLNSLINPLIYTIFNEDFKKAFQKLVRCRC 7EXD,21AH,21AG 5-hydroxytryptamine receptor 1F 5HT1F_HUMAN P30939 50287304 CN1CCC(c2c[nH]c3ccc(NC(=O)c4ccc(F)cc4)cc23)CC1 InChI=1S/C21H22FN3O/c1-25-10-8-14(9-11-25)19-13-23-20-7-6-17(12-18(19)20)24-21(26)15-2-4-16(22)5-3-15/h2-7,12-14,23H,8-11H2,1H3,(H,24,26) MDMJLMDBRQXOOI-UHFFFAOYSA-N 50130461 LY-334370::4-Fluoro-N-[3-(1-methyl-piperidin-4-yl)-1H-indol-5-yl]-benzamide::4-Fluoro-N-[3-(1-methyl-4-piperidinyl)-1H-indol-5-yl]benzamide::CHEMBL101690 5-hydroxytryptamine receptor 1F Homo sapiens 2.1 ChEMBL 10.1016/j.bmcl.2004.09.079 10.7270/Q23J3CFK 15546719 Zhang, D; Kohlman, D; Krushinski, J; Liang, S; Ying, BP; Reilly, JE; Dinn, SR; Wainscott, DB; Nutter, S; Gough, W; Nelson, DL; Schaus, JM; Xu, YC 11/19/2004 11/10/2009 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50130461 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=49000035&target=5-hydroxytryptamine+receptor+1F&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50130461&enzyme=5-hydroxytryptamine+receptor+1F&column=ki&startPg=0&Increment=50&submit=Search A1E2G 21AG,21AH 5311258 104021837 CHEMBL101690 1 MDFLNSSDQNLTSEELLNRMPSKILVSLTLSGLALMTTTINSLVIAAIIVTRKLHHPANYLICSLAVTDFLVAVLVMPFSIVYIVRESWIMGQVVCDIWLSVDITCCTCSILHLSAIALDRYRAITDAVEYARKRTPKHAGIMITIVWIISVFISMPPLFWRHQGTSRDDECIIKHDHIVSTIYSTFGAFYIPLALILILYYKIYRAAKTLYHKRQASRIAKEEVNGQVLLESGEKSTKSVSTSYVLEKSLSDPSTDFDKIHSTVRSLRSEFKHEKSWRRQKISGTRERKAATTLGLILGAFVICWLPFFVKELVVNVCDKCKISEEMSNFLAWLGYLNSLINPLIYTIFNEDFKKAFQKLVRCRC 7EXD,21AH,21AG 5-hydroxytryptamine receptor 1F 5HT1F_HUMAN P30939 50409712 CN1CCC(c2c[nH]c3ccc(NC(=O)c4ccc(F)cc4)cc23)CC1 InChI=1S/C21H22FN3O/c1-25-10-8-14(9-11-25)19-13-23-20-7-6-17(12-18(19)20)24-21(26)15-2-4-16(22)5-3-15/h2-7,12-14,23H,8-11H2,1H3,(H,24,26) MDMJLMDBRQXOOI-UHFFFAOYSA-N 50130461 LY-334370::4-Fluoro-N-[3-(1-methyl-piperidin-4-yl)-1H-indol-5-yl]-benzamide::4-Fluoro-N-[3-(1-methyl-4-piperidinyl)-1H-indol-5-yl]benzamide::CHEMBL101690 5-hydroxytryptamine receptor 1F Homo sapiens 2.1 ChEMBL 10.1016/j.bmcl.2015.07.042 10.7270/Q2NC630T 26271587 Zhang, D; Blanco, MJ; Ying, BP; Kohlman, D; Liang, SX; Victor, F; Chen, Q; Krushinski, J; Filla, SA; Hudziak, KJ; Mathes, BM; Cohen, MP; Zacherl, D; Nelson, DL; Wainscott, DB; Nutter, SE; Gough, WH; Schaus, JM; Xu, YC 9/10/2015 12/2/2016 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50130461 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=49000035&target=5-hydroxytryptamine+receptor+1F&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50130461&enzyme=5-hydroxytryptamine+receptor+1F&column=ki&startPg=0&Increment=50&submit=Search A1E2G 21AG,21AH 5311258 104021837 CHEMBL101690 1 MDFLNSSDQNLTSEELLNRMPSKILVSLTLSGLALMTTTINSLVIAAIIVTRKLHHPANYLICSLAVTDFLVAVLVMPFSIVYIVRESWIMGQVVCDIWLSVDITCCTCSILHLSAIALDRYRAITDAVEYARKRTPKHAGIMITIVWIISVFISMPPLFWRHQGTSRDDECIIKHDHIVSTIYSTFGAFYIPLALILILYYKIYRAAKTLYHKRQASRIAKEEVNGQVLLESGEKSTKSVSTSYVLEKSLSDPSTDFDKIHSTVRSLRSEFKHEKSWRRQKISGTRERKAATTLGLILGAFVICWLPFFVKELVVNVCDKCKISEEMSNFLAWLGYLNSLINPLIYTIFNEDFKKAFQKLVRCRC 7EXD,21AH,21AG 5-hydroxytryptamine receptor 1F 5HT1F_HUMAN P30939 50415940 CN1CCC(c2c[nH]c3ccc(NC(=O)c4ccc(F)cc4)cc23)CC1 InChI=1S/C21H22FN3O/c1-25-10-8-14(9-11-25)19-13-23-20-7-6-17(12-18(19)20)24-21(26)15-2-4-16(22)5-3-15/h2-7,12-14,23H,8-11H2,1H3,(H,24,26) MDMJLMDBRQXOOI-UHFFFAOYSA-N 50130461 LY-334370::4-Fluoro-N-[3-(1-methyl-piperidin-4-yl)-1H-indol-5-yl]-benzamide::4-Fluoro-N-[3-(1-methyl-4-piperidinyl)-1H-indol-5-yl]benzamide::CHEMBL101690 5-hydroxytryptamine receptor 1F Homo sapiens 1.6 ChEMBL 10.1021/jm7011722 10.7270/Q26T0MDK 18507369 Choi, SK; Green, D; Ho, A; Klein, U; Marquess, D; Taylor, R; Turner, SD 6/19/2008 1/11/2010 Theravance http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50130461 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=49000035&target=5-hydroxytryptamine+receptor+1F&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50130461&enzyme=5-hydroxytryptamine+receptor+1F&column=ki&startPg=0&Increment=50&submit=Search A1E2G 21AG,21AH 5311258 104021837 CHEMBL101690 1 MDFLNSSDQNLTSEELLNRMPSKILVSLTLSGLALMTTTINSLVIAAIIVTRKLHHPANYLICSLAVTDFLVAVLVMPFSIVYIVRESWIMGQVVCDIWLSVDITCCTCSILHLSAIALDRYRAITDAVEYARKRTPKHAGIMITIVWIISVFISMPPLFWRHQGTSRDDECIIKHDHIVSTIYSTFGAFYIPLALILILYYKIYRAAKTLYHKRQASRIAKEEVNGQVLLESGEKSTKSVSTSYVLEKSLSDPSTDFDKIHSTVRSLRSEFKHEKSWRRQKISGTRERKAATTLGLILGAFVICWLPFFVKELVVNVCDKCKISEEMSNFLAWLGYLNSLINPLIYTIFNEDFKKAFQKLVRCRC 7EXD,21AH,21AG 5-hydroxytryptamine receptor 1F 5HT1F_HUMAN P30939 159537 COc1ccc2[nH]cc(CCN)c2c1 InChI=1S/C11H14N2O/c1-14-9-2-3-11-10(6-9)8(4-5-12)7-13-11/h2-3,6-7,13H,4-5,12H2,1H3 JTEJPPKMYBDEMY-UHFFFAOYSA-N 82087 tryptamine, 5-Methoxy::5-Methoxytryptamine hydrochloride::CAS_66-83-1::2-(5-methoxy-1H-indol-3-yl)ethanamine::5-MT 5-hydroxytryptamine receptor 2A Rattus norvegicus 647 PDSP Ki 10.1016/0024-3205(83)90740-3 10.7270/Q2DR2T0M 6645787 Battaglia, G; Shannon, M; Borgundvaag, B; Titeler, M 12/14/1983 12/20/2011 University of Toronto http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=82087 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=82087&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search F5U 7BRX,7BS4,7DAK,7WB8,9J87 1833 131342661 C05659 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 159538 COc1ccc2[nH]cc(CCN)c2c1 InChI=1S/C11H14N2O/c1-14-9-2-3-11-10(6-9)8(4-5-12)7-13-11/h2-3,6-7,13H,4-5,12H2,1H3 JTEJPPKMYBDEMY-UHFFFAOYSA-N 82087 tryptamine, 5-Methoxy::5-Methoxytryptamine hydrochloride::CAS_66-83-1::2-(5-methoxy-1H-indol-3-yl)ethanamine::5-MT 5-hydroxytryptamine receptor 2A Rattus norvegicus 215 PDSP Ki 10.1016/0024-3205(83)90740-3 10.7270/Q2DR2T0M 6645787 Battaglia, G; Shannon, M; Borgundvaag, B; Titeler, M 12/14/1983 12/20/2011 University of Toronto http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=82087 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=82087&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search F5U 7BRX,7BS4,7DAK,7WB8,9J87 1833 131342661 C05659 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 159539 COc1ccc2[nH]cc(CCN)c2c1 InChI=1S/C11H14N2O/c1-14-9-2-3-11-10(6-9)8(4-5-12)7-13-11/h2-3,6-7,13H,4-5,12H2,1H3 JTEJPPKMYBDEMY-UHFFFAOYSA-N 82087 tryptamine, 5-Methoxy::5-Methoxytryptamine hydrochloride::CAS_66-83-1::2-(5-methoxy-1H-indol-3-yl)ethanamine::5-MT 5-hydroxytryptamine receptor 2A Rattus norvegicus 92 PDSP Ki 10.1016/0024-3205(83)90740-3 10.7270/Q2DR2T0M 6645787 Battaglia, G; Shannon, M; Borgundvaag, B; Titeler, M 12/14/1983 12/20/2011 University of Toronto http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=82087 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=82087&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search F5U 7BRX,7BS4,7DAK,7WB8,9J87 1833 131342661 C05659 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 171157 COc1ccc2[nH]cc(CCN)c2c1 InChI=1S/C11H14N2O/c1-14-9-2-3-11-10(6-9)8(4-5-12)7-13-11/h2-3,6-7,13H,4-5,12H2,1H3 JTEJPPKMYBDEMY-UHFFFAOYSA-N 82087 tryptamine, 5-Methoxy::5-Methoxytryptamine hydrochloride::CAS_66-83-1::2-(5-methoxy-1H-indol-3-yl)ethanamine::5-MT 5-hydroxytryptamine receptor 2A Sus scrofa 923 PDSP Ki 10.7270/Q2833QJ4 8510008 Nelson, DL; Lucaites, VL; Audia, JE; Nissen, JS; Wainscott, DB 12/28/1993 2/17/2012 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=82087 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=49000039&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=82087&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search F5U 7BRX,7BS4,7DAK,7WB8,9J87 1833 131342661 C05659 1 MDVLCEENTSLSSPTNSFMQLNDDTRLYHNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPPCFSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHRRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQTGQKENSKQDDKATENDCTMVALGKQHSEDAPADNSNTVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_PIG P50129 Q29004 171158 COc1ccc2[nH]cc(CCN)c2c1 InChI=1S/C11H14N2O/c1-14-9-2-3-11-10(6-9)8(4-5-12)7-13-11/h2-3,6-7,13H,4-5,12H2,1H3 JTEJPPKMYBDEMY-UHFFFAOYSA-N 82087 tryptamine, 5-Methoxy::5-Methoxytryptamine hydrochloride::CAS_66-83-1::2-(5-methoxy-1H-indol-3-yl)ethanamine::5-MT 5-hydroxytryptamine receptor 2A Rattus norvegicus 3791 PDSP Ki 10.7270/Q2833QJ4 8510008 Nelson, DL; Lucaites, VL; Audia, JE; Nissen, JS; Wainscott, DB 12/28/1993 2/17/2012 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=82087 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=82087&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search F5U 7BRX,7BS4,7DAK,7WB8,9J87 1833 131342661 C05659 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 174430 COc1ccc2[nH]cc(CCN)c2c1 InChI=1S/C11H14N2O/c1-14-9-2-3-11-10(6-9)8(4-5-12)7-13-11/h2-3,6-7,13H,4-5,12H2,1H3 JTEJPPKMYBDEMY-UHFFFAOYSA-N 82087 tryptamine, 5-Methoxy::5-Methoxytryptamine hydrochloride::CAS_66-83-1::2-(5-methoxy-1H-indol-3-yl)ethanamine::5-MT 5-hydroxytryptamine receptor 2A Homo sapiens 61.65 PDSP Ki 10.1016/s0028-3908(97)00049-x 10.7270/Q2NV9GSN 9225287 Bonhaus, DW; Weinhardt, KK; Taylor, M; DeSouza, A; McNeeley, PM; Szczepanski, K; Fontana, DJ; Trinh, J; Rocha, CL; Dawson, MW; Flippin, LA; Eglen, RM 12/28/1997 2/26/2012 Roche Bioscience http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=82087 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=82087&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search F5U 7BRX,7BS4,7DAK,7WB8,9J87 1833 131342661 C05659 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 174431 COc1ccc2[nH]cc(CCN)c2c1 InChI=1S/C11H14N2O/c1-14-9-2-3-11-10(6-9)8(4-5-12)7-13-11/h2-3,6-7,13H,4-5,12H2,1H3 JTEJPPKMYBDEMY-UHFFFAOYSA-N 82087 tryptamine, 5-Methoxy::5-Methoxytryptamine hydrochloride::CAS_66-83-1::2-(5-methoxy-1H-indol-3-yl)ethanamine::5-MT 5-hydroxytryptamine receptor 2A Rattus norvegicus 141.25 PDSP Ki 10.1016/s0028-3908(97)00049-x 10.7270/Q2NV9GSN 9225287 Bonhaus, DW; Weinhardt, KK; Taylor, M; DeSouza, A; McNeeley, PM; Szczepanski, K; Fontana, DJ; Trinh, J; Rocha, CL; Dawson, MW; Flippin, LA; Eglen, RM 12/28/1997 2/26/2012 Roche Bioscience http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=82087 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=82087&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search F5U 7BRX,7BS4,7DAK,7WB8,9J87 1833 131342661 C05659 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 180065 COc1ccc2[nH]cc(CCN)c2c1 InChI=1S/C11H14N2O/c1-14-9-2-3-11-10(6-9)8(4-5-12)7-13-11/h2-3,6-7,13H,4-5,12H2,1H3 JTEJPPKMYBDEMY-UHFFFAOYSA-N 82087 tryptamine, 5-Methoxy::5-Methoxytryptamine hydrochloride::CAS_66-83-1::2-(5-methoxy-1H-indol-3-yl)ethanamine::5-MT 5-hydroxytryptamine receptor 2A Homo sapiens 38 PDSP Ki 10.1002/(SICI)1098-2396(200002)35:2<144::AID-SYN7>3.0.CO;2-K 10.7270/Q2ST7NDX 10611640 Egan, C; Grinde, E; Dupre, A; Roth, BL; Hake, M; Teitler, M; Herrick-Davis, K 12/28/2000 4/17/2012 Albany Medical College http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=82087 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=82087&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search F5U 7BRX,7BS4,7DAK,7WB8,9J87 1833 131342661 C05659 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 180066 COc1ccc2[nH]cc(CCN)c2c1 InChI=1S/C11H14N2O/c1-14-9-2-3-11-10(6-9)8(4-5-12)7-13-11/h2-3,6-7,13H,4-5,12H2,1H3 JTEJPPKMYBDEMY-UHFFFAOYSA-N 82087 tryptamine, 5-Methoxy::5-Methoxytryptamine hydrochloride::CAS_66-83-1::2-(5-methoxy-1H-indol-3-yl)ethanamine::5-MT 5-hydroxytryptamine receptor 2A Homo sapiens 724 PDSP Ki 10.1002/(SICI)1098-2396(200002)35:2<144::AID-SYN7>3.0.CO;2-K 10.7270/Q2ST7NDX 10611640 Egan, C; Grinde, E; Dupre, A; Roth, BL; Hake, M; Teitler, M; Herrick-Davis, K 12/28/2000 4/17/2012 Albany Medical College http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=82087 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=82087&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search F5U 7BRX,7BS4,7DAK,7WB8,9J87 1833 131342661 C05659 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 50035893 COc1ccc2[nH]cc(CCN)c2c1 InChI=1S/C11H14N2O/c1-14-9-2-3-11-10(6-9)8(4-5-12)7-13-11/h2-3,6-7,13H,4-5,12H2,1H3 JTEJPPKMYBDEMY-UHFFFAOYSA-N 82087 tryptamine, 5-Methoxy::5-Methoxytryptamine hydrochloride::CAS_66-83-1::2-(5-methoxy-1H-indol-3-yl)ethanamine::5-MT 5-hydroxytryptamine receptor 2A Homo sapiens 300 ChEMBL 10.1021/jm00039a004 10.7270/Q2GQ6WT0 8027974 Glennon, RA; Dukat, M; el-Bermawy, M; Law, H; De los Angeles, J; Teitler, M; King, A; Herrick-Davis, K 8/9/1994 11/10/2009 Virginia Commonwealth University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=82087 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=82087&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search F5U 7BRX,7BS4,7DAK,7WB8,9J87 1833 131342661 C05659 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 50060608 COc1ccc2[nH]cc(CCN)c2c1 InChI=1S/C11H14N2O/c1-14-9-2-3-11-10(6-9)8(4-5-12)7-13-11/h2-3,6-7,13H,4-5,12H2,1H3 JTEJPPKMYBDEMY-UHFFFAOYSA-N 82087 tryptamine, 5-Methoxy::5-Methoxytryptamine hydrochloride::CAS_66-83-1::2-(5-methoxy-1H-indol-3-yl)ethanamine::5-MT 5-hydroxytryptamine receptor 2A Homo sapiens 4.8 ChEMBL 10.1021/jm00039a004 10.7270/Q2GQ6WT0 8027974 Glennon, RA; Dukat, M; el-Bermawy, M; Law, H; De los Angeles, J; Teitler, M; King, A; Herrick-Davis, K 8/9/1994 11/10/2009 Virginia Commonwealth University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=82087 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=82087&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search F5U 7BRX,7BS4,7DAK,7WB8,9J87 1833 131342661 C05659 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 50031610 COc1ccc2[nH]cc(CCN)c2c1 InChI=1S/C11H14N2O/c1-14-9-2-3-11-10(6-9)8(4-5-12)7-13-11/h2-3,6-7,13H,4-5,12H2,1H3 JTEJPPKMYBDEMY-UHFFFAOYSA-N 82087 tryptamine, 5-Methoxy::5-Methoxytryptamine hydrochloride::CAS_66-83-1::2-(5-methoxy-1H-indol-3-yl)ethanamine::5-MT Serotonin 2 (5-HT2) receptor Rattus norvegicus 305 ChEMBL 10.1021/jm00399a031 10.7270/Q2QN65SB 2965244 Glennon, RA; Titeler, M; Lyon, RA; Slusher, RM 5/10/1988 11/10/2009 Virginia Commonwealth University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=82087 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000484&target=Serotonin+2+%285-HT2%29+receptor&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=82087&enzyme=Serotonin+2+%285-HT2%29+receptor&column=ki&startPg=0&Increment=50&submit=Search F5U 7BRX,7BS4,7DAK,7WB8,9J87 1833 131342661 C05659 3 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 MVNLGNAVRSLLMHLIGLLVWQFDISISPVAAIVTDTFNSSDGGRLFQFPDGVQNWPALSIVVIIIMTIGGNILVIMAVSMEKKLHNATNYFLMSLAIADMLVGLLVMPLSLLAILYDYVWPLPRYLCPVWISLDVLFSTASIMHLCAISLDRYVAIRNPIEHSRFNSRTKAIMKIAIVWAISIGVSVPIPVIGLRDESKVFVNNTTCVLNDPNFVLIGSFVAFFIPLTIMVITYFLTIYVLRRQTLMLLRGHTEEELANMSLNFLNCCCKKNGGEEENAPNPNPDQKPRRKKKEKRPRGTMQAINNEKKASKVLGIVFFVFLIMWCPFFITNILSVLCGKACNQKLMEKLLNVFVWIGYVCSGINPLVYTLFNKIYRRAFSKYLRCDYKPDKKPPVRQIPRVAATALSGRELNVNIYRHTNERVARKANDPEPGIEMQVENLELPVNPSNVVSERISSV 5-hydroxytryptamine receptor 2C 5HT2C_RAT P08909 MASSYKMSEQSTISEHILQKTCDHLILTDRSGLKAESAAEEMKQTAENQGNTVHWAALLIFAVIIPTIGGNILVILAVSLEKRLQYATNYFLMSLAVADLLVGLFVMPIALLTIMFEATWPLPLALCPAWLFLDVLFSTASIMHLCAISLDRYIAIKKPIQANQCNSRTTAFVKITVVWLISIGIAIPVPIKGIEADVVNAHNITCELTKDRFGSFMLFGSLAAFFAPLTIMIVTYFLTIHALRKKAYLVRNRPPQRLTRWTVSTVLQREDSSFSSPEKMVMLDGSHKDKILPNSTDETLMRRMSSAGKKPAQTISNEQRASKVLGIVFLFFLLMWCPFFITNVTLALCDSCNQTTLKTLLQIFVWVGYVSSGVNPLIYTLFNKTFREAFGRYITCNYQATKSVKVLRKCSSTLYFGNSMVENSKFFTKHGIRNGINPAMYQSPVRLRSSTIQSSSIILLNTFLTENDGDKVEDQVSYI 5-hydroxytryptamine receptor 2B 5HT2B_RAT P30994 Q9QW44 50031621 COc1ccc2[nH]cc(CCN)c2c1 InChI=1S/C11H14N2O/c1-14-9-2-3-11-10(6-9)8(4-5-12)7-13-11/h2-3,6-7,13H,4-5,12H2,1H3 JTEJPPKMYBDEMY-UHFFFAOYSA-N 82087 tryptamine, 5-Methoxy::5-Methoxytryptamine hydrochloride::CAS_66-83-1::2-(5-methoxy-1H-indol-3-yl)ethanamine::5-MT Serotonin 2 (5-HT2) receptor Rattus norvegicus 4.8 ChEMBL 10.1021/jm00399a031 10.7270/Q2QN65SB 2965244 Glennon, RA; Titeler, M; Lyon, RA; Slusher, RM 5/10/1988 11/10/2009 Virginia Commonwealth University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=82087 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000484&target=Serotonin+2+%285-HT2%29+receptor&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=82087&enzyme=Serotonin+2+%285-HT2%29+receptor&column=ki&startPg=0&Increment=50&submit=Search F5U 7BRX,7BS4,7DAK,7WB8,9J87 1833 131342661 C05659 3 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 MVNLGNAVRSLLMHLIGLLVWQFDISISPVAAIVTDTFNSSDGGRLFQFPDGVQNWPALSIVVIIIMTIGGNILVIMAVSMEKKLHNATNYFLMSLAIADMLVGLLVMPLSLLAILYDYVWPLPRYLCPVWISLDVLFSTASIMHLCAISLDRYVAIRNPIEHSRFNSRTKAIMKIAIVWAISIGVSVPIPVIGLRDESKVFVNNTTCVLNDPNFVLIGSFVAFFIPLTIMVITYFLTIYVLRRQTLMLLRGHTEEELANMSLNFLNCCCKKNGGEEENAPNPNPDQKPRRKKKEKRPRGTMQAINNEKKASKVLGIVFFVFLIMWCPFFITNILSVLCGKACNQKLMEKLLNVFVWIGYVCSGINPLVYTLFNKIYRRAFSKYLRCDYKPDKKPPVRQIPRVAATALSGRELNVNIYRHTNERVARKANDPEPGIEMQVENLELPVNPSNVVSERISSV 5-hydroxytryptamine receptor 2C 5HT2C_RAT P08909 MASSYKMSEQSTISEHILQKTCDHLILTDRSGLKAESAAEEMKQTAENQGNTVHWAALLIFAVIIPTIGGNILVILAVSLEKRLQYATNYFLMSLAVADLLVGLFVMPIALLTIMFEATWPLPLALCPAWLFLDVLFSTASIMHLCAISLDRYIAIKKPIQANQCNSRTTAFVKITVVWLISIGIAIPVPIKGIEADVVNAHNITCELTKDRFGSFMLFGSLAAFFAPLTIMIVTYFLTIHALRKKAYLVRNRPPQRLTRWTVSTVLQREDSSFSSPEKMVMLDGSHKDKILPNSTDETLMRRMSSAGKKPAQTISNEQRASKVLGIVFLFFLLMWCPFFITNVTLALCDSCNQTTLKTLLQIFVWVGYVSSGVNPLIYTLFNKTFREAFGRYITCNYQATKSVKVLRKCSSTLYFGNSMVENSKFFTKHGIRNGINPAMYQSPVRLRSSTIQSSSIILLNTFLTENDGDKVEDQVSYI 5-hydroxytryptamine receptor 2B 5HT2B_RAT P30994 Q9QW44 50616379 COc1ccc2[nH]cc(CCN)c2c1 InChI=1S/C11H14N2O/c1-14-9-2-3-11-10(6-9)8(4-5-12)7-13-11/h2-3,6-7,13H,4-5,12H2,1H3 JTEJPPKMYBDEMY-UHFFFAOYSA-N 82087 tryptamine, 5-Methoxy::5-Methoxytryptamine hydrochloride::CAS_66-83-1::2-(5-methoxy-1H-indol-3-yl)ethanamine::5-MT Serotonin 2 (5-HT2) receptor Rattus norvegicus 14 ChEMBL 10.1021/jm00384a001 10.7270/Q29K4BS7 3543362 Glennon, RA 2/24/1987 10/15/2012 TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=82087 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000484&target=Serotonin+2+%285-HT2%29+receptor&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=82087&enzyme=Serotonin+2+%285-HT2%29+receptor&column=ki&startPg=0&Increment=50&submit=Search F5U 7BRX,7BS4,7DAK,7WB8,9J87 1833 131342661 C05659 3 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 MVNLGNAVRSLLMHLIGLLVWQFDISISPVAAIVTDTFNSSDGGRLFQFPDGVQNWPALSIVVIIIMTIGGNILVIMAVSMEKKLHNATNYFLMSLAIADMLVGLLVMPLSLLAILYDYVWPLPRYLCPVWISLDVLFSTASIMHLCAISLDRYVAIRNPIEHSRFNSRTKAIMKIAIVWAISIGVSVPIPVIGLRDESKVFVNNTTCVLNDPNFVLIGSFVAFFIPLTIMVITYFLTIYVLRRQTLMLLRGHTEEELANMSLNFLNCCCKKNGGEEENAPNPNPDQKPRRKKKEKRPRGTMQAINNEKKASKVLGIVFFVFLIMWCPFFITNILSVLCGKACNQKLMEKLLNVFVWIGYVCSGINPLVYTLFNKIYRRAFSKYLRCDYKPDKKPPVRQIPRVAATALSGRELNVNIYRHTNERVARKANDPEPGIEMQVENLELPVNPSNVVSERISSV 5-hydroxytryptamine receptor 2C 5HT2C_RAT P08909 MASSYKMSEQSTISEHILQKTCDHLILTDRSGLKAESAAEEMKQTAENQGNTVHWAALLIFAVIIPTIGGNILVILAVSLEKRLQYATNYFLMSLAVADLLVGLFVMPIALLTIMFEATWPLPLALCPAWLFLDVLFSTASIMHLCAISLDRYIAIKKPIQANQCNSRTTAFVKITVVWLISIGIAIPVPIKGIEADVVNAHNITCELTKDRFGSFMLFGSLAAFFAPLTIMIVTYFLTIHALRKKAYLVRNRPPQRLTRWTVSTVLQREDSSFSSPEKMVMLDGSHKDKILPNSTDETLMRRMSSAGKKPAQTISNEQRASKVLGIVFLFFLLMWCPFFITNVTLALCDSCNQTTLKTLLQIFVWVGYVSSGVNPLIYTLFNKTFREAFGRYITCNYQATKSVKVLRKCSSTLYFGNSMVENSKFFTKHGIRNGINPAMYQSPVRLRSSTIQSSSIILLNTFLTENDGDKVEDQVSYI 5-hydroxytryptamine receptor 2B 5HT2B_RAT P30994 Q9QW44 50616874 COc1ccc2[nH]cc(CCN)c2c1 InChI=1S/C11H14N2O/c1-14-9-2-3-11-10(6-9)8(4-5-12)7-13-11/h2-3,6-7,13H,4-5,12H2,1H3 JTEJPPKMYBDEMY-UHFFFAOYSA-N 82087 tryptamine, 5-Methoxy::5-Methoxytryptamine hydrochloride::CAS_66-83-1::2-(5-methoxy-1H-indol-3-yl)ethanamine::5-MT Serotonin 2 (5-HT2) receptor Rattus norvegicus 2570 ChEMBL 10.1021/jm00384a001 10.7270/Q29K4BS7 3543362 Glennon, RA 2/24/1987 10/15/2012 TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=82087 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000484&target=Serotonin+2+%285-HT2%29+receptor&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=82087&enzyme=Serotonin+2+%285-HT2%29+receptor&column=ki&startPg=0&Increment=50&submit=Search F5U 7BRX,7BS4,7DAK,7WB8,9J87 1833 131342661 C05659 3 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 MVNLGNAVRSLLMHLIGLLVWQFDISISPVAAIVTDTFNSSDGGRLFQFPDGVQNWPALSIVVIIIMTIGGNILVIMAVSMEKKLHNATNYFLMSLAIADMLVGLLVMPLSLLAILYDYVWPLPRYLCPVWISLDVLFSTASIMHLCAISLDRYVAIRNPIEHSRFNSRTKAIMKIAIVWAISIGVSVPIPVIGLRDESKVFVNNTTCVLNDPNFVLIGSFVAFFIPLTIMVITYFLTIYVLRRQTLMLLRGHTEEELANMSLNFLNCCCKKNGGEEENAPNPNPDQKPRRKKKEKRPRGTMQAINNEKKASKVLGIVFFVFLIMWCPFFITNILSVLCGKACNQKLMEKLLNVFVWIGYVCSGINPLVYTLFNKIYRRAFSKYLRCDYKPDKKPPVRQIPRVAATALSGRELNVNIYRHTNERVARKANDPEPGIEMQVENLELPVNPSNVVSERISSV 5-hydroxytryptamine receptor 2C 5HT2C_RAT P08909 MASSYKMSEQSTISEHILQKTCDHLILTDRSGLKAESAAEEMKQTAENQGNTVHWAALLIFAVIIPTIGGNILVILAVSLEKRLQYATNYFLMSLAVADLLVGLFVMPIALLTIMFEATWPLPLALCPAWLFLDVLFSTASIMHLCAISLDRYIAIKKPIQANQCNSRTTAFVKITVVWLISIGIAIPVPIKGIEADVVNAHNITCELTKDRFGSFMLFGSLAAFFAPLTIMIVTYFLTIHALRKKAYLVRNRPPQRLTRWTVSTVLQREDSSFSSPEKMVMLDGSHKDKILPNSTDETLMRRMSSAGKKPAQTISNEQRASKVLGIVFLFFLLMWCPFFITNVTLALCDSCNQTTLKTLLQIFVWVGYVSSGVNPLIYTLFNKTFREAFGRYITCNYQATKSVKVLRKCSSTLYFGNSMVENSKFFTKHGIRNGINPAMYQSPVRLRSSTIQSSSIILLNTFLTENDGDKVEDQVSYI 5-hydroxytryptamine receptor 2B 5HT2B_RAT P30994 Q9QW44 50616875 COc1ccc2[nH]cc(CCN)c2c1 InChI=1S/C11H14N2O/c1-14-9-2-3-11-10(6-9)8(4-5-12)7-13-11/h2-3,6-7,13H,4-5,12H2,1H3 JTEJPPKMYBDEMY-UHFFFAOYSA-N 82087 tryptamine, 5-Methoxy::5-Methoxytryptamine hydrochloride::CAS_66-83-1::2-(5-methoxy-1H-indol-3-yl)ethanamine::5-MT Serotonin 2 (5-HT2) receptor Rattus norvegicus 690 ChEMBL 10.1021/jm00384a001 10.7270/Q29K4BS7 3543362 Glennon, RA 2/24/1987 10/15/2012 TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=82087 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000484&target=Serotonin+2+%285-HT2%29+receptor&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=82087&enzyme=Serotonin+2+%285-HT2%29+receptor&column=ki&startPg=0&Increment=50&submit=Search F5U 7BRX,7BS4,7DAK,7WB8,9J87 1833 131342661 C05659 3 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 MVNLGNAVRSLLMHLIGLLVWQFDISISPVAAIVTDTFNSSDGGRLFQFPDGVQNWPALSIVVIIIMTIGGNILVIMAVSMEKKLHNATNYFLMSLAIADMLVGLLVMPLSLLAILYDYVWPLPRYLCPVWISLDVLFSTASIMHLCAISLDRYVAIRNPIEHSRFNSRTKAIMKIAIVWAISIGVSVPIPVIGLRDESKVFVNNTTCVLNDPNFVLIGSFVAFFIPLTIMVITYFLTIYVLRRQTLMLLRGHTEEELANMSLNFLNCCCKKNGGEEENAPNPNPDQKPRRKKKEKRPRGTMQAINNEKKASKVLGIVFFVFLIMWCPFFITNILSVLCGKACNQKLMEKLLNVFVWIGYVCSGINPLVYTLFNKIYRRAFSKYLRCDYKPDKKPPVRQIPRVAATALSGRELNVNIYRHTNERVARKANDPEPGIEMQVENLELPVNPSNVVSERISSV 5-hydroxytryptamine receptor 2C 5HT2C_RAT P08909 MASSYKMSEQSTISEHILQKTCDHLILTDRSGLKAESAAEEMKQTAENQGNTVHWAALLIFAVIIPTIGGNILVILAVSLEKRLQYATNYFLMSLAVADLLVGLFVMPIALLTIMFEATWPLPLALCPAWLFLDVLFSTASIMHLCAISLDRYIAIKKPIQANQCNSRTTAFVKITVVWLISIGIAIPVPIKGIEADVVNAHNITCELTKDRFGSFMLFGSLAAFFAPLTIMIVTYFLTIHALRKKAYLVRNRPPQRLTRWTVSTVLQREDSSFSSPEKMVMLDGSHKDKILPNSTDETLMRRMSSAGKKPAQTISNEQRASKVLGIVFLFFLLMWCPFFITNVTLALCDSCNQTTLKTLLQIFVWVGYVSSGVNPLIYTLFNKTFREAFGRYITCNYQATKSVKVLRKCSSTLYFGNSMVENSKFFTKHGIRNGINPAMYQSPVRLRSSTIQSSSIILLNTFLTENDGDKVEDQVSYI 5-hydroxytryptamine receptor 2B 5HT2B_RAT P30994 Q9QW44 50616879 COc1ccc2[nH]cc(CCN)c2c1 InChI=1S/C11H14N2O/c1-14-9-2-3-11-10(6-9)8(4-5-12)7-13-11/h2-3,6-7,13H,4-5,12H2,1H3 JTEJPPKMYBDEMY-UHFFFAOYSA-N 82087 tryptamine, 5-Methoxy::5-Methoxytryptamine hydrochloride::CAS_66-83-1::2-(5-methoxy-1H-indol-3-yl)ethanamine::5-MT Serotonin 2 (5-HT2) receptor Rattus norvegicus 14 ChEMBL 10.1021/jm00384a001 10.7270/Q29K4BS7 3543362 Glennon, RA 2/24/1987 10/15/2012 TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=82087 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000484&target=Serotonin+2+%285-HT2%29+receptor&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=82087&enzyme=Serotonin+2+%285-HT2%29+receptor&column=ki&startPg=0&Increment=50&submit=Search F5U 7BRX,7BS4,7DAK,7WB8,9J87 1833 131342661 C05659 3 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 MVNLGNAVRSLLMHLIGLLVWQFDISISPVAAIVTDTFNSSDGGRLFQFPDGVQNWPALSIVVIIIMTIGGNILVIMAVSMEKKLHNATNYFLMSLAIADMLVGLLVMPLSLLAILYDYVWPLPRYLCPVWISLDVLFSTASIMHLCAISLDRYVAIRNPIEHSRFNSRTKAIMKIAIVWAISIGVSVPIPVIGLRDESKVFVNNTTCVLNDPNFVLIGSFVAFFIPLTIMVITYFLTIYVLRRQTLMLLRGHTEEELANMSLNFLNCCCKKNGGEEENAPNPNPDQKPRRKKKEKRPRGTMQAINNEKKASKVLGIVFFVFLIMWCPFFITNILSVLCGKACNQKLMEKLLNVFVWIGYVCSGINPLVYTLFNKIYRRAFSKYLRCDYKPDKKPPVRQIPRVAATALSGRELNVNIYRHTNERVARKANDPEPGIEMQVENLELPVNPSNVVSERISSV 5-hydroxytryptamine receptor 2C 5HT2C_RAT P08909 MASSYKMSEQSTISEHILQKTCDHLILTDRSGLKAESAAEEMKQTAENQGNTVHWAALLIFAVIIPTIGGNILVILAVSLEKRLQYATNYFLMSLAVADLLVGLFVMPIALLTIMFEATWPLPLALCPAWLFLDVLFSTASIMHLCAISLDRYIAIKKPIQANQCNSRTTAFVKITVVWLISIGIAIPVPIKGIEADVVNAHNITCELTKDRFGSFMLFGSLAAFFAPLTIMIVTYFLTIHALRKKAYLVRNRPPQRLTRWTVSTVLQREDSSFSSPEKMVMLDGSHKDKILPNSTDETLMRRMSSAGKKPAQTISNEQRASKVLGIVFLFFLLMWCPFFITNVTLALCDSCNQTTLKTLLQIFVWVGYVSSGVNPLIYTLFNKTFREAFGRYITCNYQATKSVKVLRKCSSTLYFGNSMVENSKFFTKHGIRNGINPAMYQSPVRLRSSTIQSSSIILLNTFLTENDGDKVEDQVSYI 5-hydroxytryptamine receptor 2B 5HT2B_RAT P30994 Q9QW44 50622648 COc1ccc2[nH]cc(CCN)c2c1 InChI=1S/C11H14N2O/c1-14-9-2-3-11-10(6-9)8(4-5-12)7-13-11/h2-3,6-7,13H,4-5,12H2,1H3 JTEJPPKMYBDEMY-UHFFFAOYSA-N 82087 tryptamine, 5-Methoxy::5-Methoxytryptamine hydrochloride::CAS_66-83-1::2-(5-methoxy-1H-indol-3-yl)ethanamine::5-MT Serotonin 2 (5-HT2) receptor Rattus norvegicus 1023 ChEMBL 10.1021/jm00402a026 10.7270/Q2JD500M 3385733 Nichols, DE; Lloyd, DH; Johnson, MP; Hoffman, AJ 7/28/1988 1/2/2019 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=82087 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000484&target=Serotonin+2+%285-HT2%29+receptor&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=82087&enzyme=Serotonin+2+%285-HT2%29+receptor&column=ki&startPg=0&Increment=50&submit=Search F5U 7BRX,7BS4,7DAK,7WB8,9J87 1833 131342661 C05659 3 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 MVNLGNAVRSLLMHLIGLLVWQFDISISPVAAIVTDTFNSSDGGRLFQFPDGVQNWPALSIVVIIIMTIGGNILVIMAVSMEKKLHNATNYFLMSLAIADMLVGLLVMPLSLLAILYDYVWPLPRYLCPVWISLDVLFSTASIMHLCAISLDRYVAIRNPIEHSRFNSRTKAIMKIAIVWAISIGVSVPIPVIGLRDESKVFVNNTTCVLNDPNFVLIGSFVAFFIPLTIMVITYFLTIYVLRRQTLMLLRGHTEEELANMSLNFLNCCCKKNGGEEENAPNPNPDQKPRRKKKEKRPRGTMQAINNEKKASKVLGIVFFVFLIMWCPFFITNILSVLCGKACNQKLMEKLLNVFVWIGYVCSGINPLVYTLFNKIYRRAFSKYLRCDYKPDKKPPVRQIPRVAATALSGRELNVNIYRHTNERVARKANDPEPGIEMQVENLELPVNPSNVVSERISSV 5-hydroxytryptamine receptor 2C 5HT2C_RAT P08909 MASSYKMSEQSTISEHILQKTCDHLILTDRSGLKAESAAEEMKQTAENQGNTVHWAALLIFAVIIPTIGGNILVILAVSLEKRLQYATNYFLMSLAVADLLVGLFVMPIALLTIMFEATWPLPLALCPAWLFLDVLFSTASIMHLCAISLDRYIAIKKPIQANQCNSRTTAFVKITVVWLISIGIAIPVPIKGIEADVVNAHNITCELTKDRFGSFMLFGSLAAFFAPLTIMIVTYFLTIHALRKKAYLVRNRPPQRLTRWTVSTVLQREDSSFSSPEKMVMLDGSHKDKILPNSTDETLMRRMSSAGKKPAQTISNEQRASKVLGIVFLFFLLMWCPFFITNVTLALCDSCNQTTLKTLLQIFVWVGYVSSGVNPLIYTLFNKTFREAFGRYITCNYQATKSVKVLRKCSSTLYFGNSMVENSKFFTKHGIRNGINPAMYQSPVRLRSSTIQSSSIILLNTFLTENDGDKVEDQVSYI 5-hydroxytryptamine receptor 2B 5HT2B_RAT P30994 Q9QW44 50628291 COc1ccc2[nH]cc(CCN)c2c1 InChI=1S/C11H14N2O/c1-14-9-2-3-11-10(6-9)8(4-5-12)7-13-11/h2-3,6-7,13H,4-5,12H2,1H3 JTEJPPKMYBDEMY-UHFFFAOYSA-N 82087 tryptamine, 5-Methoxy::5-Methoxytryptamine hydrochloride::CAS_66-83-1::2-(5-methoxy-1H-indol-3-yl)ethanamine::5-MT Serotonin 2 (5-HT2) receptor Rattus norvegicus 302 ChEMBL 10.1021/jm00172a016 10.7270/Q2GX49JP 2213830 Glennon, RA; Chaurasia, C; Titeler, M 11/20/1990 11/10/2009 Virginia Commonwealth University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=82087 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000484&target=Serotonin+2+%285-HT2%29+receptor&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=82087&enzyme=Serotonin+2+%285-HT2%29+receptor&column=ki&startPg=0&Increment=50&submit=Search F5U 7BRX,7BS4,7DAK,7WB8,9J87 1833 131342661 C05659 3 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 MVNLGNAVRSLLMHLIGLLVWQFDISISPVAAIVTDTFNSSDGGRLFQFPDGVQNWPALSIVVIIIMTIGGNILVIMAVSMEKKLHNATNYFLMSLAIADMLVGLLVMPLSLLAILYDYVWPLPRYLCPVWISLDVLFSTASIMHLCAISLDRYVAIRNPIEHSRFNSRTKAIMKIAIVWAISIGVSVPIPVIGLRDESKVFVNNTTCVLNDPNFVLIGSFVAFFIPLTIMVITYFLTIYVLRRQTLMLLRGHTEEELANMSLNFLNCCCKKNGGEEENAPNPNPDQKPRRKKKEKRPRGTMQAINNEKKASKVLGIVFFVFLIMWCPFFITNILSVLCGKACNQKLMEKLLNVFVWIGYVCSGINPLVYTLFNKIYRRAFSKYLRCDYKPDKKPPVRQIPRVAATALSGRELNVNIYRHTNERVARKANDPEPGIEMQVENLELPVNPSNVVSERISSV 5-hydroxytryptamine receptor 2C 5HT2C_RAT P08909 MASSYKMSEQSTISEHILQKTCDHLILTDRSGLKAESAAEEMKQTAENQGNTVHWAALLIFAVIIPTIGGNILVILAVSLEKRLQYATNYFLMSLAVADLLVGLFVMPIALLTIMFEATWPLPLALCPAWLFLDVLFSTASIMHLCAISLDRYIAIKKPIQANQCNSRTTAFVKITVVWLISIGIAIPVPIKGIEADVVNAHNITCELTKDRFGSFMLFGSLAAFFAPLTIMIVTYFLTIHALRKKAYLVRNRPPQRLTRWTVSTVLQREDSSFSSPEKMVMLDGSHKDKILPNSTDETLMRRMSSAGKKPAQTISNEQRASKVLGIVFLFFLLMWCPFFITNVTLALCDSCNQTTLKTLLQIFVWVGYVSSGVNPLIYTLFNKTFREAFGRYITCNYQATKSVKVLRKCSSTLYFGNSMVENSKFFTKHGIRNGINPAMYQSPVRLRSSTIQSSSIILLNTFLTENDGDKVEDQVSYI 5-hydroxytryptamine receptor 2B 5HT2B_RAT P30994 Q9QW44 157453 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Rattus norvegicus 12 PDSP Ki 10.7270/Q2FX77Z2 2795135 McKenna, DJ; Peroutka, SJ 12/28/1989 11/22/2011 Stanford University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 391564 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens 21 Curated from the literature by BindingDB 10.7270/Q2ZG6XSW 20126400 aid2060762 Ray, TS 2/2/2010 4/24/2025 University of Oklahoma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 391566 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens 25.51 Curated from the literature by BindingDB 10.7270/Q2ZG6XSW 20126400 aid2060762 Ray, TS 2/2/2010 4/24/2025 University of Oklahoma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 391569 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens 161.5 Curated from the literature by BindingDB 10.7270/Q2ZG6XSW 20126400 aid2060762 Ray, TS 2/2/2010 4/24/2025 University of Oklahoma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1203705 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens <500 US Patent 10.7270/Q2CJ8HQ6 aid1806784 US11427604 Slassi, A; Araujo, J 8/30/2022 11/7/2022 Mindset Pharma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1203708 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens <500 US Patent 10.7270/Q2CJ8HQ6 aid1806784 US11427604 Slassi, A; Araujo, J 8/30/2022 11/7/2022 Mindset Pharma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1210527 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens <1000 US Patent 10.7270/Q2K077JM aid1806844 US11453689 Slassi, A; Araujo, J 9/27/2022 12/4/2022 Mindset Pharma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1210548 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens <500 US Patent 10.7270/Q2K077JM aid1806844 US11453689 Slassi, A; Araujo, J 9/27/2022 12/4/2022 Mindset Pharma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1263876 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens 112 US Patent 10.7270/Q2CC14MX aid1919325 US11591353 Slassi, A; Araujo, J 2/28/2023 4/14/2023 Mindset Pharma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1263878 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens 352 US Patent 10.7270/Q2CC14MX aid1919325 US11591353 Slassi, A; Araujo, J 2/28/2023 4/14/2023 Mindset Pharma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1265156 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens <500 US Patent 10.7270/Q2G44V7B US11597738 Slassi, A; Araujo, J 3/7/2023 4/23/2023 Mindset Pharma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1265159 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens <500 US Patent 10.7270/Q2G44V7B US11597738 Slassi, A; Araujo, J 3/7/2023 4/23/2023 Mindset Pharma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1274368 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens 340 US Patent 10.7270/Q2S46WX8 aid1919423 US11642336 Kristensen, JL; Jensen, AA; Marcher-Rorsted, E; Leth-Petersen, S 5/9/2023 6/11/2023 Lophora http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1376374 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens <1000 US Patent 10.7270/Q2QF8Z24 aid1963391 US20240051978 Slassi, A; Araujo, J; Higgins, G 2/15/2024 4/23/2024 Mindset Pharma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1415156 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens 58.6 US Patent 10.7270/Q2R49W2W aid1963741 US20240166618 KRUEGEL, AC 5/23/2024 8/26/2024 Gilgamesh Pharmaceuticals http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1466047 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens 339.600000 Curated from the literature by BindingDB 10.7270/Q2ZG6XSW 20126400 aid2060761 Ray, TS 2/2/2010 4/24/2025 University of Oklahoma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 50143175 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Rattus norvegicus 390 ChEMBL 10.1021/jm990325u 10.7270/Q2FX78PW 10514296 Gerasimov, M; Marona-Lewicka, D; Kurrasch-Orbaugh, DM; Qandil, AM; Nichols, DE 11/4/1999 11/10/2009 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 50239819 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Rattus norvegicus 2300 ChEMBL 10.1021/jm030064v 10.7270/Q20P0ZC1 12877591 Chambers, JJ; Parrish, JC; Jensen, NH; Kurrasch-Orbaugh, DM; Marona-Lewicka, D; Nichols, DE 7/24/2003 11/10/2009 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 50239821 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Rattus norvegicus 25 ChEMBL 10.1021/jm030064v 10.7270/Q20P0ZC1 12877591 Chambers, JJ; Parrish, JC; Jensen, NH; Kurrasch-Orbaugh, DM; Marona-Lewicka, D; Nichols, DE 7/24/2003 11/10/2009 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 50315802 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens 24 ChEMBL 10.1016/j.bmcl.2005.06.104 10.7270/Q2PZ58B5 16061378 Sard, H; Kumaran, G; Morency, C; Roth, BL; Toth, BA; He, P; Shuster, L 9/12/2005 11/10/2009 Organix http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 50411376 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Rattus norvegicus 323 ChEMBL 10.1016/j.bmc.2008.02.033 10.7270/Q25D8RNZ 18296055 Parker, MA; Kurrasch, DM; Nichols, DE 4/24/2008 1/11/2010 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 51329470 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens 4.3 ChEMBL 10.1021/acs.jnatprod.9b01061 10.7270/Q2RX9GM1 32077284 Sherwood, AM; Halberstadt, AL; Klein, AK; McCorvy, JD; Kaylo, KW; Kargbo, RB; Meisenheimer, P 2/28/2020 8/11/2021 Usona Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51329471 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens 4.3 ChEMBL 10.1021/acs.jnatprod.9b01061 10.7270/Q2RX9GM1 32077284 Sherwood, AM; Halberstadt, AL; Klein, AK; McCorvy, JD; Kaylo, KW; Kargbo, RB; Meisenheimer, P 2/28/2020 8/11/2021 Usona Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51329472 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Mus musculus 9.9 ChEMBL 10.1021/acs.jnatprod.9b01061 10.7270/Q2RX9GM1 32077284 Sherwood, AM; Halberstadt, AL; Klein, AK; McCorvy, JD; Kaylo, KW; Kargbo, RB; Meisenheimer, P 2/28/2020 8/11/2021 Usona Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=7883&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MEILCEDNISLSSIPNSLMQLGDDSRLYPNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLSSFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPTLAYKSSQLQVGQKKNSQEDAEPTANDCSMVTLGNQHSEEMCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_MOUSE P35363 51329473 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Mus musculus 9.8 ChEMBL 10.1021/acs.jnatprod.9b01061 10.7270/Q2RX9GM1 32077284 Sherwood, AM; Halberstadt, AL; Klein, AK; McCorvy, JD; Kaylo, KW; Kargbo, RB; Meisenheimer, P 2/28/2020 8/11/2021 Usona Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=7883&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MEILCEDNISLSSIPNSLMQLGDDSRLYPNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLSSFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPTLAYKSSQLQVGQKKNSQEDAEPTANDCSMVTLGNQHSEEMCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_MOUSE P35363 51419639 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens 75 ChEMBL 10.1021/acsmedchemlett.1c00467 10.7270/Q2TT4VR2 34676027 Kargbo, RB 10/14/2021 8/23/2022 Usona Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51419641 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens 75 ChEMBL 10.1021/acsmedchemlett.1c00467 10.7270/Q2TT4VR2 34676027 Kargbo, RB 10/14/2021 8/23/2022 Usona Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51431967 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens 6.5 ChEMBL 10.1021/acsmedchemlett.1c00577 10.7270/Q2Z89H7T 34917241 Kargbo, RB 12/9/2021 8/24/2022 Usona Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51441329 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens 6.5 ChEMBL 10.1021/acsmedchemlett.2c00129 10.7270/Q23T9N3F 35450349 Kargbo, RB 4/14/2022 3/5/2023 Usona Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51455251 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens 8.3 ChEMBL 10.1021/acsmedchemlett.1c00578 10.7270/Q2BR8X3V 34917242 Kargbo, RB 12/9/2021 3/7/2023 Usona Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51481443 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens <1000 ChEMBL 10.7270/Q2KD22Z5 35586424 Kargbo, RB 5/12/2022 6/22/2023 Usona Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51491805 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens <1000 ChEMBL 10.7270/Q2CC14Q8 36105333 Kargbo, RB 9/8/2022 6/24/2023 Usona Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51549028 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens 107 ChEMBL 10.7270/Q2R49W57 38516602 Vandevelde, M; Simoens, A; Vandekerckhove, B; Stevens, C 3/20/2024 12/17/2024 Ghent University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 157453 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Rattus norvegicus 12 PDSP Ki 10.7270/Q2FX77Z2 2795135 McKenna, DJ; Peroutka, SJ 12/28/1989 11/22/2011 Stanford University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 391564 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens 21 Curated from the literature by BindingDB 10.7270/Q2ZG6XSW 20126400 aid2060762 Ray, TS 2/2/2010 4/24/2025 University of Oklahoma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 391566 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens 25.51 Curated from the literature by BindingDB 10.7270/Q2ZG6XSW 20126400 aid2060762 Ray, TS 2/2/2010 4/24/2025 University of Oklahoma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 391569 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens 161.5 Curated from the literature by BindingDB 10.7270/Q2ZG6XSW 20126400 aid2060762 Ray, TS 2/2/2010 4/24/2025 University of Oklahoma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1203705 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens <500 US Patent 10.7270/Q2CJ8HQ6 aid1806784 US11427604 Slassi, A; Araujo, J 8/30/2022 11/7/2022 Mindset Pharma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1203708 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens <500 US Patent 10.7270/Q2CJ8HQ6 aid1806784 US11427604 Slassi, A; Araujo, J 8/30/2022 11/7/2022 Mindset Pharma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1210527 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens <1000 US Patent 10.7270/Q2K077JM aid1806844 US11453689 Slassi, A; Araujo, J 9/27/2022 12/4/2022 Mindset Pharma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1210548 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens <500 US Patent 10.7270/Q2K077JM aid1806844 US11453689 Slassi, A; Araujo, J 9/27/2022 12/4/2022 Mindset Pharma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1263876 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens 112 US Patent 10.7270/Q2CC14MX aid1919325 US11591353 Slassi, A; Araujo, J 2/28/2023 4/14/2023 Mindset Pharma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1263878 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens 352 US Patent 10.7270/Q2CC14MX aid1919325 US11591353 Slassi, A; Araujo, J 2/28/2023 4/14/2023 Mindset Pharma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1265156 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens <500 US Patent 10.7270/Q2G44V7B US11597738 Slassi, A; Araujo, J 3/7/2023 4/23/2023 Mindset Pharma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1265159 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens <500 US Patent 10.7270/Q2G44V7B US11597738 Slassi, A; Araujo, J 3/7/2023 4/23/2023 Mindset Pharma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1274368 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens 340 US Patent 10.7270/Q2S46WX8 aid1919423 US11642336 Kristensen, JL; Jensen, AA; Marcher-Rorsted, E; Leth-Petersen, S 5/9/2023 6/11/2023 Lophora http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1376374 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens <1000 US Patent 10.7270/Q2QF8Z24 aid1963391 US20240051978 Slassi, A; Araujo, J; Higgins, G 2/15/2024 4/23/2024 Mindset Pharma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1415156 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens 58.6 US Patent 10.7270/Q2R49W2W aid1963741 US20240166618 KRUEGEL, AC 5/23/2024 8/26/2024 Gilgamesh Pharmaceuticals http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1466047 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens 339.600000 Curated from the literature by BindingDB 10.7270/Q2ZG6XSW 20126400 aid2060761 Ray, TS 2/2/2010 4/24/2025 University of Oklahoma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 50143175 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Rattus norvegicus 390 ChEMBL 10.1021/jm990325u 10.7270/Q2FX78PW 10514296 Gerasimov, M; Marona-Lewicka, D; Kurrasch-Orbaugh, DM; Qandil, AM; Nichols, DE 11/4/1999 11/10/2009 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 50239819 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Rattus norvegicus 2300 ChEMBL 10.1021/jm030064v 10.7270/Q20P0ZC1 12877591 Chambers, JJ; Parrish, JC; Jensen, NH; Kurrasch-Orbaugh, DM; Marona-Lewicka, D; Nichols, DE 7/24/2003 11/10/2009 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 50239821 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Rattus norvegicus 25 ChEMBL 10.1021/jm030064v 10.7270/Q20P0ZC1 12877591 Chambers, JJ; Parrish, JC; Jensen, NH; Kurrasch-Orbaugh, DM; Marona-Lewicka, D; Nichols, DE 7/24/2003 11/10/2009 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 50315802 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens 24 ChEMBL 10.1016/j.bmcl.2005.06.104 10.7270/Q2PZ58B5 16061378 Sard, H; Kumaran, G; Morency, C; Roth, BL; Toth, BA; He, P; Shuster, L 9/12/2005 11/10/2009 Organix http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 50411376 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Rattus norvegicus 323 ChEMBL 10.1016/j.bmc.2008.02.033 10.7270/Q25D8RNZ 18296055 Parker, MA; Kurrasch, DM; Nichols, DE 4/24/2008 1/11/2010 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 51329470 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens 4.3 ChEMBL 10.1021/acs.jnatprod.9b01061 10.7270/Q2RX9GM1 32077284 Sherwood, AM; Halberstadt, AL; Klein, AK; McCorvy, JD; Kaylo, KW; Kargbo, RB; Meisenheimer, P 2/28/2020 8/11/2021 Usona Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51329471 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens 4.3 ChEMBL 10.1021/acs.jnatprod.9b01061 10.7270/Q2RX9GM1 32077284 Sherwood, AM; Halberstadt, AL; Klein, AK; McCorvy, JD; Kaylo, KW; Kargbo, RB; Meisenheimer, P 2/28/2020 8/11/2021 Usona Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51329472 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Mus musculus 9.9 ChEMBL 10.1021/acs.jnatprod.9b01061 10.7270/Q2RX9GM1 32077284 Sherwood, AM; Halberstadt, AL; Klein, AK; McCorvy, JD; Kaylo, KW; Kargbo, RB; Meisenheimer, P 2/28/2020 8/11/2021 Usona Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=7883&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MEILCEDNISLSSIPNSLMQLGDDSRLYPNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLSSFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPTLAYKSSQLQVGQKKNSQEDAEPTANDCSMVTLGNQHSEEMCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_MOUSE P35363 51329473 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Mus musculus 9.8 ChEMBL 10.1021/acs.jnatprod.9b01061 10.7270/Q2RX9GM1 32077284 Sherwood, AM; Halberstadt, AL; Klein, AK; McCorvy, JD; Kaylo, KW; Kargbo, RB; Meisenheimer, P 2/28/2020 8/11/2021 Usona Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=7883&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MEILCEDNISLSSIPNSLMQLGDDSRLYPNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLSSFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPTLAYKSSQLQVGQKKNSQEDAEPTANDCSMVTLGNQHSEEMCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_MOUSE P35363 51419639 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens 75 ChEMBL 10.1021/acsmedchemlett.1c00467 10.7270/Q2TT4VR2 34676027 Kargbo, RB 10/14/2021 8/23/2022 Usona Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51419641 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens 75 ChEMBL 10.1021/acsmedchemlett.1c00467 10.7270/Q2TT4VR2 34676027 Kargbo, RB 10/14/2021 8/23/2022 Usona Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51431967 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens 6.5 ChEMBL 10.1021/acsmedchemlett.1c00577 10.7270/Q2Z89H7T 34917241 Kargbo, RB 12/9/2021 8/24/2022 Usona Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51441329 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens 6.5 ChEMBL 10.1021/acsmedchemlett.2c00129 10.7270/Q23T9N3F 35450349 Kargbo, RB 4/14/2022 3/5/2023 Usona Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51455251 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens 8.3 ChEMBL 10.1021/acsmedchemlett.1c00578 10.7270/Q2BR8X3V 34917242 Kargbo, RB 12/9/2021 3/7/2023 Usona Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51481443 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens <1000 ChEMBL 10.7270/Q2KD22Z5 35586424 Kargbo, RB 5/12/2022 6/22/2023 Usona Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51491805 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens <1000 ChEMBL 10.7270/Q2CC14Q8 36105333 Kargbo, RB 9/8/2022 6/24/2023 Usona Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51549028 CN(C)CCc1c[nH]c2cccc(O)c12 InChI=1S/C12H16N2O/c1-14(2)7-6-9-8-13-10-4-3-5-11(15)12(9)10/h3-5,8,13,15H,6-7H2,1-2H3 SPCIYGNTAMCTRO-UHFFFAOYSA-N 50081701 4-hydroxy-N,N-dimethyltryptamine::N,N-dimethyl-4-hydroxytryptamine::Psilocin::CHEMBL65547::3-[2-(dimethylamino)ethyl]-1H-indol-4-ol::US11597738, Example 3::US11453689, Compound Psilocin::US11642336, Compound Psilocin::US11591353, Compound I-45::US11427604, Compound (I-45)::US20240051978, Compound Psilocin::US20240166618, Compound Psilocin::US20240317683, Compound psilocin 5-hydroxytryptamine receptor 2A Homo sapiens 107 ChEMBL 10.7270/Q2R49W57 38516602 Vandevelde, M; Simoens, A; Vandekerckhove, B; Stevens, C 3/20/2024 12/17/2024 Ghent University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50081701 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50081701&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 91Q 7WC5,8DPG,9AS7,9AS8,9LL8 4980 103981649 CHEMBL65547 C08312 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 157450 COc1cc(cc(c1OC)OC)CCN InChI=1S/C11H17NO3/c1-13-9-6-8(4-5-12)7-10(14-2)11(9)15-3/h6-7H,4-5,12H2,1-3H3 RHCSKNNOAZULRK-UHFFFAOYSA-N 50059891 3,4,5-trimethoxyphenylethylamine::3,4,5-trimethoxybenzeneethanamine::TMPEA::1-amino-2-(3,4,5-trimethoxyphenyl)ethane::3,4,5-trimethoxyphenethylamine::mescalina::Meskalin::mezcalina::Mescalin::CHEMBL26687::mescaline::2-(3,4,5-trimethoxyphenyl)ethanamine::US20240166618, Compound Mescaline::US20250270173, Compound Mescaline 5-hydroxytryptamine receptor 2A Rattus norvegicus 150 PDSP Ki 10.7270/Q2FX77Z2 2795135 McKenna, DJ; Peroutka, SJ 12/28/1989 11/22/2011 Stanford University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50059891 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50059891&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFW 9AS5,9AS6 4076 103955666 CHEMBL26687 C06546 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 391487 COc1cc(cc(c1OC)OC)CCN InChI=1S/C11H17NO3/c1-13-9-6-8(4-5-12)7-10(14-2)11(9)15-3/h6-7H,4-5,12H2,1-3H3 RHCSKNNOAZULRK-UHFFFAOYSA-N 50059891 3,4,5-trimethoxyphenylethylamine::3,4,5-trimethoxybenzeneethanamine::TMPEA::1-amino-2-(3,4,5-trimethoxyphenyl)ethane::3,4,5-trimethoxyphenethylamine::mescalina::Meskalin::mezcalina::Mescalin::CHEMBL26687::mescaline::2-(3,4,5-trimethoxyphenyl)ethanamine::US20240166618, Compound Mescaline::US20250270173, Compound Mescaline 5-hydroxytryptamine receptor 2A Homo sapiens 118 Curated from the literature by BindingDB 10.7270/Q2ZG6XSW 20126400 aid2060762 Ray, TS 2/2/2010 4/24/2025 University of Oklahoma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50059891 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50059891&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFW 9AS5,9AS6 4076 103955666 CHEMBL26687 C06546 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 391489 COc1cc(cc(c1OC)OC)CCN InChI=1S/C11H17NO3/c1-13-9-6-8(4-5-12)7-10(14-2)11(9)15-3/h6-7H,4-5,12H2,1-3H3 RHCSKNNOAZULRK-UHFFFAOYSA-N 50059891 3,4,5-trimethoxyphenylethylamine::3,4,5-trimethoxybenzeneethanamine::TMPEA::1-amino-2-(3,4,5-trimethoxyphenyl)ethane::3,4,5-trimethoxyphenethylamine::mescalina::Meskalin::mezcalina::Mescalin::CHEMBL26687::mescaline::2-(3,4,5-trimethoxyphenyl)ethanamine::US20240166618, Compound Mescaline::US20250270173, Compound Mescaline 5-hydroxytryptamine receptor 2A Homo sapiens 208.4 Curated from the literature by BindingDB 10.7270/Q2ZG6XSW 20126400 aid2060762 Ray, TS 2/2/2010 4/24/2025 University of Oklahoma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50059891 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50059891&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFW 9AS5,9AS6 4076 103955666 CHEMBL26687 C06546 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 391491 COc1cc(cc(c1OC)OC)CCN InChI=1S/C11H17NO3/c1-13-9-6-8(4-5-12)7-10(14-2)11(9)15-3/h6-7H,4-5,12H2,1-3H3 RHCSKNNOAZULRK-UHFFFAOYSA-N 50059891 3,4,5-trimethoxyphenylethylamine::3,4,5-trimethoxybenzeneethanamine::TMPEA::1-amino-2-(3,4,5-trimethoxyphenyl)ethane::3,4,5-trimethoxyphenethylamine::mescalina::Meskalin::mezcalina::Mescalin::CHEMBL26687::mescaline::2-(3,4,5-trimethoxyphenyl)ethanamine::US20240166618, Compound Mescaline::US20250270173, Compound Mescaline 5-hydroxytryptamine receptor 2A Homo sapiens 87.6 Curated from the literature by BindingDB 10.7270/Q2ZG6XSW 20126400 aid2060762 Ray, TS 2/2/2010 4/24/2025 University of Oklahoma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50059891 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50059891&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFW 9AS5,9AS6 4076 103955666 CHEMBL26687 C06546 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 869906 COc1cc(cc(c1OC)OC)CCN InChI=1S/C11H17NO3/c1-13-9-6-8(4-5-12)7-10(14-2)11(9)15-3/h6-7H,4-5,12H2,1-3H3 RHCSKNNOAZULRK-UHFFFAOYSA-N 50059891 3,4,5-trimethoxyphenylethylamine::3,4,5-trimethoxybenzeneethanamine::TMPEA::1-amino-2-(3,4,5-trimethoxyphenyl)ethane::3,4,5-trimethoxyphenethylamine::mescalina::Meskalin::mezcalina::Mescalin::CHEMBL26687::mescaline::2-(3,4,5-trimethoxyphenyl)ethanamine::US20240166618, Compound Mescaline::US20250270173, Compound Mescaline 5-hydroxytryptamine receptor 2A Homo sapiens 17400 US Patent 10.7270/Q2TH8SG2 US20250270173 O''NEILL, BT; COE, JW; KRUEGEL, AC 8/28/2025 12/8/2025 Gilgamesh Pharmaceuticals http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50059891 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50059891&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFW 9AS5,9AS6 4076 103955666 CHEMBL26687 C06546 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1415152 COc1cc(cc(c1OC)OC)CCN InChI=1S/C11H17NO3/c1-13-9-6-8(4-5-12)7-10(14-2)11(9)15-3/h6-7H,4-5,12H2,1-3H3 RHCSKNNOAZULRK-UHFFFAOYSA-N 50059891 3,4,5-trimethoxyphenylethylamine::3,4,5-trimethoxybenzeneethanamine::TMPEA::1-amino-2-(3,4,5-trimethoxyphenyl)ethane::3,4,5-trimethoxyphenethylamine::mescalina::Meskalin::mezcalina::Mescalin::CHEMBL26687::mescaline::2-(3,4,5-trimethoxyphenyl)ethanamine::US20240166618, Compound Mescaline::US20250270173, Compound Mescaline 5-hydroxytryptamine receptor 2A Homo sapiens 17400 US Patent 10.7270/Q2R49W2W aid1963741 US20240166618 KRUEGEL, AC 5/23/2024 8/26/2024 Gilgamesh Pharmaceuticals http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50059891 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50059891&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFW 9AS5,9AS6 4076 103955666 CHEMBL26687 C06546 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1465905 COc1cc(cc(c1OC)OC)CCN InChI=1S/C11H17NO3/c1-13-9-6-8(4-5-12)7-10(14-2)11(9)15-3/h6-7H,4-5,12H2,1-3H3 RHCSKNNOAZULRK-UHFFFAOYSA-N 50059891 3,4,5-trimethoxyphenylethylamine::3,4,5-trimethoxybenzeneethanamine::TMPEA::1-amino-2-(3,4,5-trimethoxyphenyl)ethane::3,4,5-trimethoxyphenethylamine::mescalina::Meskalin::mezcalina::Mescalin::CHEMBL26687::mescaline::2-(3,4,5-trimethoxyphenyl)ethanamine::US20240166618, Compound Mescaline::US20250270173, Compound Mescaline 5-hydroxytryptamine receptor 2A Homo sapiens >10000 Curated from the literature by BindingDB 10.7270/Q2ZG6XSW 20126400 aid2060761 Ray, TS 2/2/2010 4/24/2025 University of Oklahoma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50059891 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50059891&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFW 9AS5,9AS6 4076 103955666 CHEMBL26687 C06546 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 50047995 COc1cc(cc(c1OC)OC)CCN InChI=1S/C11H17NO3/c1-13-9-6-8(4-5-12)7-10(14-2)11(9)15-3/h6-7H,4-5,12H2,1-3H3 RHCSKNNOAZULRK-UHFFFAOYSA-N 50059891 3,4,5-trimethoxyphenylethylamine::3,4,5-trimethoxybenzeneethanamine::TMPEA::1-amino-2-(3,4,5-trimethoxyphenyl)ethane::3,4,5-trimethoxyphenethylamine::mescalina::Meskalin::mezcalina::Mescalin::CHEMBL26687::mescaline::2-(3,4,5-trimethoxyphenyl)ethanamine::US20240166618, Compound Mescaline::US20250270173, Compound Mescaline 5-hydroxytryptamine receptor 2A Rattus norvegicus 5500 ChEMBL 10.1021/jm970219x 10.7270/Q2RF5T50 9301661 Monte, AP; Waldman, SR; Marona-Lewicka, D; Wainscott, DB; Nelson, DL; Sanders-Bush, E; Nichols, DE 10/8/1997 11/10/2009 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50059891 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50059891&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFW 9AS5,9AS6 4076 103955666 CHEMBL26687 C06546 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 50100693 COc1cc(cc(c1OC)OC)CCN InChI=1S/C11H17NO3/c1-13-9-6-8(4-5-12)7-10(14-2)11(9)15-3/h6-7H,4-5,12H2,1-3H3 RHCSKNNOAZULRK-UHFFFAOYSA-N 50059891 3,4,5-trimethoxyphenylethylamine::3,4,5-trimethoxybenzeneethanamine::TMPEA::1-amino-2-(3,4,5-trimethoxyphenyl)ethane::3,4,5-trimethoxyphenethylamine::mescalina::Meskalin::mezcalina::Mescalin::CHEMBL26687::mescaline::2-(3,4,5-trimethoxyphenyl)ethanamine::US20240166618, Compound Mescaline::US20250270173, Compound Mescaline 5-hydroxytryptamine receptor 2A Rattus norvegicus 4000 ChEMBL 10.1021/jm970219x 10.7270/Q2RF5T50 9301661 Monte, AP; Waldman, SR; Marona-Lewicka, D; Wainscott, DB; Nelson, DL; Sanders-Bush, E; Nichols, DE 10/8/1997 11/10/2009 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50059891 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50059891&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFW 9AS5,9AS6 4076 103955666 CHEMBL26687 C06546 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 50100706 COc1cc(cc(c1OC)OC)CCN InChI=1S/C11H17NO3/c1-13-9-6-8(4-5-12)7-10(14-2)11(9)15-3/h6-7H,4-5,12H2,1-3H3 RHCSKNNOAZULRK-UHFFFAOYSA-N 50059891 3,4,5-trimethoxyphenylethylamine::3,4,5-trimethoxybenzeneethanamine::TMPEA::1-amino-2-(3,4,5-trimethoxyphenyl)ethane::3,4,5-trimethoxyphenethylamine::mescalina::Meskalin::mezcalina::Mescalin::CHEMBL26687::mescaline::2-(3,4,5-trimethoxyphenyl)ethanamine::US20240166618, Compound Mescaline::US20250270173, Compound Mescaline 5-hydroxytryptamine receptor 2A Homo sapiens 551 ChEMBL 10.1021/jm970219x 10.7270/Q2RF5T50 9301661 Monte, AP; Waldman, SR; Marona-Lewicka, D; Wainscott, DB; Nelson, DL; Sanders-Bush, E; Nichols, DE 10/8/1997 11/10/2009 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50059891 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50059891&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFW 9AS5,9AS6 4076 103955666 CHEMBL26687 C06546 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 50239838 COc1cc(cc(c1OC)OC)CCN InChI=1S/C11H17NO3/c1-13-9-6-8(4-5-12)7-10(14-2)11(9)15-3/h6-7H,4-5,12H2,1-3H3 RHCSKNNOAZULRK-UHFFFAOYSA-N 50059891 3,4,5-trimethoxyphenylethylamine::3,4,5-trimethoxybenzeneethanamine::TMPEA::1-amino-2-(3,4,5-trimethoxyphenyl)ethane::3,4,5-trimethoxyphenethylamine::mescalina::Meskalin::mezcalina::Mescalin::CHEMBL26687::mescaline::2-(3,4,5-trimethoxyphenyl)ethanamine::US20240166618, Compound Mescaline::US20250270173, Compound Mescaline 5-hydroxytryptamine receptor 2A Rattus norvegicus 2600 ChEMBL 10.1021/jm030064v 10.7270/Q20P0ZC1 12877591 Chambers, JJ; Parrish, JC; Jensen, NH; Kurrasch-Orbaugh, DM; Marona-Lewicka, D; Nichols, DE 7/24/2003 11/10/2009 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50059891 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50059891&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFW 9AS5,9AS6 4076 103955666 CHEMBL26687 C06546 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 50352641 COc1cc(cc(c1OC)OC)CCN InChI=1S/C11H17NO3/c1-13-9-6-8(4-5-12)7-10(14-2)11(9)15-3/h6-7H,4-5,12H2,1-3H3 RHCSKNNOAZULRK-UHFFFAOYSA-N 50059891 3,4,5-trimethoxyphenylethylamine::3,4,5-trimethoxybenzeneethanamine::TMPEA::1-amino-2-(3,4,5-trimethoxyphenyl)ethane::3,4,5-trimethoxyphenethylamine::mescalina::Meskalin::mezcalina::Mescalin::CHEMBL26687::mescaline::2-(3,4,5-trimethoxyphenyl)ethanamine::US20240166618, Compound Mescaline::US20250270173, Compound Mescaline 5-hydroxytryptamine receptor 2A Rattus norvegicus 11300 ChEMBL 10.1021/jm060272y 10.7270/Q2PC320K 16821786 McLean, TH; Chambers, JJ; Parrish, JC; Braden, MR; Marona-Lewicka, D; Kurrasch-Orbaugh, D; Nichols, DE 7/6/2006 11/10/2009 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50059891 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50059891&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFW 9AS5,9AS6 4076 103955666 CHEMBL26687 C06546 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 50352649 COc1cc(cc(c1OC)OC)CCN InChI=1S/C11H17NO3/c1-13-9-6-8(4-5-12)7-10(14-2)11(9)15-3/h6-7H,4-5,12H2,1-3H3 RHCSKNNOAZULRK-UHFFFAOYSA-N 50059891 3,4,5-trimethoxyphenylethylamine::3,4,5-trimethoxybenzeneethanamine::TMPEA::1-amino-2-(3,4,5-trimethoxyphenyl)ethane::3,4,5-trimethoxyphenethylamine::mescalina::Meskalin::mezcalina::Mescalin::CHEMBL26687::mescaline::2-(3,4,5-trimethoxyphenyl)ethanamine::US20240166618, Compound Mescaline::US20250270173, Compound Mescaline 5-hydroxytryptamine receptor 2A Rattus norvegicus 360 ChEMBL 10.1021/jm060272y 10.7270/Q2PC320K 16821786 McLean, TH; Chambers, JJ; Parrish, JC; Braden, MR; Marona-Lewicka, D; Kurrasch-Orbaugh, D; Nichols, DE 7/6/2006 11/10/2009 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50059891 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50059891&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFW 9AS5,9AS6 4076 103955666 CHEMBL26687 C06546 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 50411384 COc1cc(cc(c1OC)OC)CCN InChI=1S/C11H17NO3/c1-13-9-6-8(4-5-12)7-10(14-2)11(9)15-3/h6-7H,4-5,12H2,1-3H3 RHCSKNNOAZULRK-UHFFFAOYSA-N 50059891 3,4,5-trimethoxyphenylethylamine::3,4,5-trimethoxybenzeneethanamine::TMPEA::1-amino-2-(3,4,5-trimethoxyphenyl)ethane::3,4,5-trimethoxyphenethylamine::mescalina::Meskalin::mezcalina::Mescalin::CHEMBL26687::mescaline::2-(3,4,5-trimethoxyphenyl)ethanamine::US20240166618, Compound Mescaline::US20250270173, Compound Mescaline 5-hydroxytryptamine receptor 2A Rattus norvegicus 5500 ChEMBL 10.1016/j.bmc.2008.02.033 10.7270/Q25D8RNZ 18296055 Parker, MA; Kurrasch, DM; Nichols, DE 4/24/2008 1/11/2010 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50059891 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50059891&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFW 9AS5,9AS6 4076 103955666 CHEMBL26687 C06546 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 179459 CCN(CC)C(=O)N[C@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H26N4O/c1-4-24(5-2)20(25)22-14-10-16-15-7-6-8-17-19(15)13(11-21-17)9-18(16)23(3)12-14/h6-8,10-11,14,18,21H,4-5,9,12H2,1-3H3,(H,22,25) BKRGVLQUQGGVSM-UHFFFAOYSA-N 50056445 lisuride, (S)::lisuride::N'-((8alpha)-9,10-Didehydro-6-methylergolin-8-yl)-N,N-diethylurea::CHEMBL157138::1,1-diethyl-3-[(8alpha)-6-methyl-9,10-didehydroergolin-8-yl]urea::US20240279226, Example 12 5-hydroxytryptamine receptor 2A Homo sapiens 6918.31 PDSP Ki 10.1038/sj.bjp.0702751 10.7270/Q2GH9GH2 10498829 Porter, RH; Benwell, KR; Lamb, H; Malcolm, CS; Allen, NH; Revell, DF; Adams, DR; Sheardown, MJ 12/28/1999 4/13/2012 Cerebrus http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50056445 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50056445&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search H8G 6DRX,7UM6,7WC7,8UWL 28864 103952701 CHEMBL157138 DB00589 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 391594 CCN(CC)C(=O)N[C@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H26N4O/c1-4-24(5-2)20(25)22-14-10-16-15-7-6-8-17-19(15)13(11-21-17)9-18(16)23(3)12-14/h6-8,10-11,14,18,21H,4-5,9,12H2,1-3H3,(H,22,25) BKRGVLQUQGGVSM-UHFFFAOYSA-N 50056445 lisuride, (S)::lisuride::N'-((8alpha)-9,10-Didehydro-6-methylergolin-8-yl)-N,N-diethylurea::CHEMBL157138::1,1-diethyl-3-[(8alpha)-6-methyl-9,10-didehydroergolin-8-yl]urea::US20240279226, Example 12 5-hydroxytryptamine receptor 2A Homo sapiens 343 Curated from the literature by BindingDB 10.7270/Q2ZG6XSW 20126400 aid2060762 Ray, TS 2/2/2010 4/24/2025 University of Oklahoma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50056445 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50056445&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search H8G 6DRX,7UM6,7WC7,8UWL 28864 103952701 CHEMBL157138 DB00589 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1438680 CCN(CC)C(=O)N[C@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H26N4O/c1-4-24(5-2)20(25)22-14-10-16-15-7-6-8-17-19(15)13(11-21-17)9-18(16)23(3)12-14/h6-8,10-11,14,18,21H,4-5,9,12H2,1-3H3,(H,22,25) BKRGVLQUQGGVSM-UHFFFAOYSA-N 50056445 lisuride, (S)::lisuride::N'-((8alpha)-9,10-Didehydro-6-methylergolin-8-yl)-N,N-diethylurea::CHEMBL157138::1,1-diethyl-3-[(8alpha)-6-methyl-9,10-didehydroergolin-8-yl]urea::US20240279226, Example 12 5-hydroxytryptamine receptor 2A Homo sapiens 0.970 US Patent 10.7270/Q2K93CVW aid1964097 US20240279226 ISAAC, M 8/22/2024 11/26/2024 Diamond Therapeutics Inc. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50056445 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50056445&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search H8G 6DRX,7UM6,7WC7,8UWL 28864 103952701 CHEMBL157138 DB00589 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1466639 CCN(CC)C(=O)N[C@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H26N4O/c1-4-24(5-2)20(25)22-14-10-16-15-7-6-8-17-19(15)13(11-21-17)9-18(16)23(3)12-14/h6-8,10-11,14,18,21H,4-5,9,12H2,1-3H3,(H,22,25) BKRGVLQUQGGVSM-UHFFFAOYSA-N 50056445 lisuride, (S)::lisuride::N'-((8alpha)-9,10-Didehydro-6-methylergolin-8-yl)-N,N-diethylurea::CHEMBL157138::1,1-diethyl-3-[(8alpha)-6-methyl-9,10-didehydroergolin-8-yl]urea::US20240279226, Example 12 5-hydroxytryptamine receptor 2A Homo sapiens 5.400000 Curated from the literature by BindingDB 10.7270/Q2ZG6XSW 20126400 aid2060761 Ray, TS 2/2/2010 4/24/2025 University of Oklahoma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50056445 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50056445&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search H8G 6DRX,7UM6,7WC7,8UWL 28864 103952701 CHEMBL157138 DB00589 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51589767 CCN(CC)C(=O)N[C@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H26N4O/c1-4-24(5-2)20(25)22-14-10-16-15-7-6-8-17-19(15)13(11-21-17)9-18(16)23(3)12-14/h6-8,10-11,14,18,21H,4-5,9,12H2,1-3H3,(H,22,25) BKRGVLQUQGGVSM-UHFFFAOYSA-N 50056445 lisuride, (S)::lisuride::N'-((8alpha)-9,10-Didehydro-6-methylergolin-8-yl)-N,N-diethylurea::CHEMBL157138::1,1-diethyl-3-[(8alpha)-6-methyl-9,10-didehydroergolin-8-yl]urea::US20240279226, Example 12 5-hydroxytryptamine receptor 2A Homo sapiens 5.1 ChEMBL 10.7270/Q21J9GD1 39038276 Dorogan, M; Namballa, HK; Harding, WW //0 10/11/2025 City University of New York http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50056445 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50056445&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search H8G 6DRX,7UM6,7WC7,8UWL 28864 103952701 CHEMBL157138 DB00589 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 50669976 CCN(CC)C(=O)N[C@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H26N4O/c1-4-24(5-2)20(25)22-14-10-16-15-7-6-8-17-19(15)13(11-21-17)9-18(16)23(3)12-14/h6-8,10-11,14,18,21H,4-5,9,12H2,1-3H3,(H,22,25) BKRGVLQUQGGVSM-UHFFFAOYSA-N 50056445 lisuride, (S)::lisuride::N'-((8alpha)-9,10-Didehydro-6-methylergolin-8-yl)-N,N-diethylurea::CHEMBL157138::1,1-diethyl-3-[(8alpha)-6-methyl-9,10-didehydroergolin-8-yl]urea::US20240279226, Example 12 Serotonin 2 (5-HT2) receptor Rattus norvegicus >5012 ChEMBL 10.1021/jm00065a015 10.7270/Q2JS9SNZ 8515429 King, FD; Brown, AM; Gaster, LM; Kaumann, AJ; Medhurst, AD; Parker, SG; Parsons, AA; Patch, TL; Raval, P 6/25/1993 3/1/2019 Smithkline Beecham Pharmaceuticals http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50056445 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000484&target=Serotonin+2+%285-HT2%29+receptor&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50056445&enzyme=Serotonin+2+%285-HT2%29+receptor&column=ki&startPg=0&Increment=50&submit=Search H8G 6DRX,7UM6,7WC7,8UWL 28864 103952701 CHEMBL157138 DB00589 3 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 MVNLGNAVRSLLMHLIGLLVWQFDISISPVAAIVTDTFNSSDGGRLFQFPDGVQNWPALSIVVIIIMTIGGNILVIMAVSMEKKLHNATNYFLMSLAIADMLVGLLVMPLSLLAILYDYVWPLPRYLCPVWISLDVLFSTASIMHLCAISLDRYVAIRNPIEHSRFNSRTKAIMKIAIVWAISIGVSVPIPVIGLRDESKVFVNNTTCVLNDPNFVLIGSFVAFFIPLTIMVITYFLTIYVLRRQTLMLLRGHTEEELANMSLNFLNCCCKKNGGEEENAPNPNPDQKPRRKKKEKRPRGTMQAINNEKKASKVLGIVFFVFLIMWCPFFITNILSVLCGKACNQKLMEKLLNVFVWIGYVCSGINPLVYTLFNKIYRRAFSKYLRCDYKPDKKPPVRQIPRVAATALSGRELNVNIYRHTNERVARKANDPEPGIEMQVENLELPVNPSNVVSERISSV 5-hydroxytryptamine receptor 2C 5HT2C_RAT P08909 MASSYKMSEQSTISEHILQKTCDHLILTDRSGLKAESAAEEMKQTAENQGNTVHWAALLIFAVIIPTIGGNILVILAVSLEKRLQYATNYFLMSLAVADLLVGLFVMPIALLTIMFEATWPLPLALCPAWLFLDVLFSTASIMHLCAISLDRYIAIKKPIQANQCNSRTTAFVKITVVWLISIGIAIPVPIKGIEADVVNAHNITCELTKDRFGSFMLFGSLAAFFAPLTIMIVTYFLTIHALRKKAYLVRNRPPQRLTRWTVSTVLQREDSSFSSPEKMVMLDGSHKDKILPNSTDETLMRRMSSAGKKPAQTISNEQRASKVLGIVFLFFLLMWCPFFITNVTLALCDSCNQTTLKTLLQIFVWVGYVSSGVNPLIYTLFNKTFREAFGRYITCNYQATKSVKVLRKCSSTLYFGNSMVENSKFFTKHGIRNGINPAMYQSPVRLRSSTIQSSSIILLNTFLTENDGDKVEDQVSYI 5-hydroxytryptamine receptor 2B 5HT2B_RAT P30994 Q9QW44 171679 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]c(Br)c(c34)C[C@H]2N(C)C1 InChI=1S/C20H24BrN3O/c1-4-24(5-2)20(25)12-9-14-13-7-6-8-16-18(13)15(19(21)22-16)10-17(14)23(3)11-12/h6-9,12,17,22H,4-5,10-11H2,1-3H3 VKRAXSZEDRWLAG-UHFFFAOYSA-N 50130269 LSD,2-Bromo::(6aR,9R)-5-Bromo-7-methyl-4,6,6a,7,8,9-hexahydro-indolo[4,3-fg]quinoline-9-carboxylic acid diethylamide::CHEMBL274384::5-Bromo-7-methyl-4,6,6a,7,8,9-hexahydro-indolo[4,3-fg]quinoline-9-carboxylic acid diethylamide 5-hydroxytryptamine receptor 2A Homo sapiens 0.48 PDSP Ki 10.7270/Q29W0D1S 8632342 Wainscott, DB; Lucaites, VL; Kursar, JD; Baez, M; Nelson, DL 12/28/1996 2/21/2012 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50130269 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50130269&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFU 9ARZ,9AS0 10171 104021703 CHEMBL274384 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 171679 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]c(Br)c(c34)C[C@H]2N(C)C1 InChI=1S/C20H24BrN3O/c1-4-24(5-2)20(25)12-9-14-13-7-6-8-16-18(13)15(19(21)22-16)10-17(14)23(3)11-12/h6-9,12,17,22H,4-5,10-11H2,1-3H3 VKRAXSZEDRWLAG-UHFFFAOYSA-N 50130269 LSD,2-Bromo::(6aR,9R)-5-Bromo-7-methyl-4,6,6a,7,8,9-hexahydro-indolo[4,3-fg]quinoline-9-carboxylic acid diethylamide::CHEMBL274384::5-Bromo-7-methyl-4,6,6a,7,8,9-hexahydro-indolo[4,3-fg]quinoline-9-carboxylic acid diethylamide 5-hydroxytryptamine receptor 2A Homo sapiens 0.48 PDSP Ki 10.7270/Q29W0D1S 8632342 Wainscott, DB; Lucaites, VL; Kursar, JD; Baez, M; Nelson, DL 12/28/1996 2/21/2012 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50130269 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50130269&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFU 9ARZ,9AS0 10171 104021703 CHEMBL274384 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 157438 CN(C)CCc1c[nH]c2ccccc12 InChI=1S/C12H16N2/c1-14(2)8-7-10-9-13-12-6-4-3-5-11(10)12/h3-6,9,13H,7-8H2,1-2H3 DMULVCHRPCFFGV-UHFFFAOYSA-N 50026868 2-(1H-indol-3-yl)-N,N-dimethylethanamine::DMT::N,N-dimethyltryptamine::CHEMBL12420::N,N-dimethyl-1H-indole-3-ethylamine::3-[2-(dimethylamino)ethyl]indole::3-(2-dimethylaminoethyl)indole::2-(3-indolyl)ethyldimethylamine::WO2023019367, Compound DMT::US20240246911, Compound DMT::US20240166618, Compound DMT::US20240317683, Compound DMT::US20250034106, Compound DMT 5-hydroxytryptamine receptor 2A Rattus norvegicus 42 PDSP Ki 10.7270/Q2FX77Z2 2795135 McKenna, DJ; Peroutka, SJ 12/28/1989 11/22/2011 Stanford University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026868 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026868&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFV 9AS1,9AS2 6089 103936452 CHEMBL12420 DB01488 C08302 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 391590 CN(C)CCc1c[nH]c2ccccc12 InChI=1S/C12H16N2/c1-14(2)8-7-10-9-13-12-6-4-3-5-11(10)12/h3-6,9,13H,7-8H2,1-2H3 DMULVCHRPCFFGV-UHFFFAOYSA-N 50026868 2-(1H-indol-3-yl)-N,N-dimethylethanamine::DMT::N,N-dimethyltryptamine::CHEMBL12420::N,N-dimethyl-1H-indole-3-ethylamine::3-[2-(dimethylamino)ethyl]indole::3-(2-dimethylaminoethyl)indole::2-(3-indolyl)ethyldimethylamine::WO2023019367, Compound DMT::US20240246911, Compound DMT::US20240166618, Compound DMT::US20240317683, Compound DMT::US20250034106, Compound DMT 5-hydroxytryptamine receptor 2A Homo sapiens 181 Curated from the literature by BindingDB 10.7270/Q2ZG6XSW 20126400 aid2060762 Ray, TS 2/2/2010 4/24/2025 University of Oklahoma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026868 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026868&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFV 9AS1,9AS2 6089 103936452 CHEMBL12420 DB01488 C08302 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 391592 CN(C)CCc1c[nH]c2ccccc12 InChI=1S/C12H16N2/c1-14(2)8-7-10-9-13-12-6-4-3-5-11(10)12/h3-6,9,13H,7-8H2,1-2H3 DMULVCHRPCFFGV-UHFFFAOYSA-N 50026868 2-(1H-indol-3-yl)-N,N-dimethylethanamine::DMT::N,N-dimethyltryptamine::CHEMBL12420::N,N-dimethyl-1H-indole-3-ethylamine::3-[2-(dimethylamino)ethyl]indole::3-(2-dimethylaminoethyl)indole::2-(3-indolyl)ethyldimethylamine::WO2023019367, Compound DMT::US20240246911, Compound DMT::US20240166618, Compound DMT::US20240317683, Compound DMT::US20250034106, Compound DMT 5-hydroxytryptamine receptor 2A Homo sapiens 439.9 Curated from the literature by BindingDB 10.7270/Q2ZG6XSW 20126400 aid2060762 Ray, TS 2/2/2010 4/24/2025 University of Oklahoma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026868 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026868&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFV 9AS1,9AS2 6089 103936452 CHEMBL12420 DB01488 C08302 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1237700 CN(C)CCc1c[nH]c2ccccc12 InChI=1S/C12H16N2/c1-14(2)8-7-10-9-13-12-6-4-3-5-11(10)12/h3-6,9,13H,7-8H2,1-2H3 DMULVCHRPCFFGV-UHFFFAOYSA-N 50026868 2-(1H-indol-3-yl)-N,N-dimethylethanamine::DMT::N,N-dimethyltryptamine::CHEMBL12420::N,N-dimethyl-1H-indole-3-ethylamine::3-[2-(dimethylamino)ethyl]indole::3-(2-dimethylaminoethyl)indole::2-(3-indolyl)ethyldimethylamine::WO2023019367, Compound DMT::US20240246911, Compound DMT::US20240166618, Compound DMT::US20240317683, Compound DMT::US20250034106, Compound DMT 5-hydroxytryptamine receptor 2A Homo sapiens <10000 WIPO 10.7270/Q2QN6BNM aid1919199 WO2023019327 Abdelmalik, S; A., AJ; Guy, H 2/23/2023 3/5/2023 Mindset Pharma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026868 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026868&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFV 9AS1,9AS2 6089 103936452 CHEMBL12420 DB01488 C08302 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1415153 CN(C)CCc1c[nH]c2ccccc12 InChI=1S/C12H16N2/c1-14(2)8-7-10-9-13-12-6-4-3-5-11(10)12/h3-6,9,13H,7-8H2,1-2H3 DMULVCHRPCFFGV-UHFFFAOYSA-N 50026868 2-(1H-indol-3-yl)-N,N-dimethylethanamine::DMT::N,N-dimethyltryptamine::CHEMBL12420::N,N-dimethyl-1H-indole-3-ethylamine::3-[2-(dimethylamino)ethyl]indole::3-(2-dimethylaminoethyl)indole::2-(3-indolyl)ethyldimethylamine::WO2023019367, Compound DMT::US20240246911, Compound DMT::US20240166618, Compound DMT::US20240317683, Compound DMT::US20250034106, Compound DMT 5-hydroxytryptamine receptor 2A Homo sapiens 416 US Patent 10.7270/Q2R49W2W aid1963741 US20240166618 KRUEGEL, AC 5/23/2024 8/26/2024 Gilgamesh Pharmaceuticals http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026868 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026868&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFV 9AS1,9AS2 6089 103936452 CHEMBL12420 DB01488 C08302 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1430281 CN(C)CCc1c[nH]c2ccccc12 InChI=1S/C12H16N2/c1-14(2)8-7-10-9-13-12-6-4-3-5-11(10)12/h3-6,9,13H,7-8H2,1-2H3 DMULVCHRPCFFGV-UHFFFAOYSA-N 50026868 2-(1H-indol-3-yl)-N,N-dimethylethanamine::DMT::N,N-dimethyltryptamine::CHEMBL12420::N,N-dimethyl-1H-indole-3-ethylamine::3-[2-(dimethylamino)ethyl]indole::3-(2-dimethylaminoethyl)indole::2-(3-indolyl)ethyldimethylamine::WO2023019367, Compound DMT::US20240246911, Compound DMT::US20240166618, Compound DMT::US20240317683, Compound DMT::US20250034106, Compound DMT 5-hydroxytryptamine receptor 2A Homo sapiens 416 US Patent 10.7270/Q2794904 aid1964011 US20240246911 KRUEGEL, AC 7/25/2024 11/7/2024 Gilgamesh Pharmaceuticals http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026868 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026868&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFV 9AS1,9AS2 6089 103936452 CHEMBL12420 DB01488 C08302 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1459342 CN(C)CCc1c[nH]c2ccccc12 InChI=1S/C12H16N2/c1-14(2)8-7-10-9-13-12-6-4-3-5-11(10)12/h3-6,9,13H,7-8H2,1-2H3 DMULVCHRPCFFGV-UHFFFAOYSA-N 50026868 2-(1H-indol-3-yl)-N,N-dimethylethanamine::DMT::N,N-dimethyltryptamine::CHEMBL12420::N,N-dimethyl-1H-indole-3-ethylamine::3-[2-(dimethylamino)ethyl]indole::3-(2-dimethylaminoethyl)indole::2-(3-indolyl)ethyldimethylamine::WO2023019367, Compound DMT::US20240246911, Compound DMT::US20240166618, Compound DMT::US20240317683, Compound DMT::US20250034106, Compound DMT 5-hydroxytryptamine receptor 2A Homo sapiens <2000 US Patent 10.7270/Q2V129BP aid2060581 US20240376052 Slassi, A; Araujo, JA; Higgins, G 11/14/2024 3/20/2025 Mindset Pharma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026868 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026868&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFV 9AS1,9AS2 6089 103936452 CHEMBL12420 DB01488 C08302 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1466004 CN(C)CCc1c[nH]c2ccccc12 InChI=1S/C12H16N2/c1-14(2)8-7-10-9-13-12-6-4-3-5-11(10)12/h3-6,9,13H,7-8H2,1-2H3 DMULVCHRPCFFGV-UHFFFAOYSA-N 50026868 2-(1H-indol-3-yl)-N,N-dimethylethanamine::DMT::N,N-dimethyltryptamine::CHEMBL12420::N,N-dimethyl-1H-indole-3-ethylamine::3-[2-(dimethylamino)ethyl]indole::3-(2-dimethylaminoethyl)indole::2-(3-indolyl)ethyldimethylamine::WO2023019367, Compound DMT::US20240246911, Compound DMT::US20240166618, Compound DMT::US20240317683, Compound DMT::US20250034106, Compound DMT 5-hydroxytryptamine receptor 2A Homo sapiens 2323.000000 Curated from the literature by BindingDB 10.7270/Q2ZG6XSW 20126400 aid2060761 Ray, TS 2/2/2010 4/24/2025 University of Oklahoma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026868 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026868&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFV 9AS1,9AS2 6089 103936452 CHEMBL12420 DB01488 C08302 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1484103 CN(C)CCc1c[nH]c2ccccc12 InChI=1S/C12H16N2/c1-14(2)8-7-10-9-13-12-6-4-3-5-11(10)12/h3-6,9,13H,7-8H2,1-2H3 DMULVCHRPCFFGV-UHFFFAOYSA-N 50026868 2-(1H-indol-3-yl)-N,N-dimethylethanamine::DMT::N,N-dimethyltryptamine::CHEMBL12420::N,N-dimethyl-1H-indole-3-ethylamine::3-[2-(dimethylamino)ethyl]indole::3-(2-dimethylaminoethyl)indole::2-(3-indolyl)ethyldimethylamine::WO2023019367, Compound DMT::US20240246911, Compound DMT::US20240166618, Compound DMT::US20240317683, Compound DMT::US20250034106, Compound DMT 5-hydroxytryptamine receptor 2A Homo sapiens <500 US Patent 10.7270/Q26D5ZHT aid2060955 US20250034106 Slassi, A; Araujo, JA 1/30/2025 6/5/2025 Mindset Pharma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026868 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026868&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFV 9AS1,9AS2 6089 103936452 CHEMBL12420 DB01488 C08302 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 50130150 CN(C)CCc1c[nH]c2ccccc12 InChI=1S/C12H16N2/c1-14(2)8-7-10-9-13-12-6-4-3-5-11(10)12/h3-6,9,13H,7-8H2,1-2H3 DMULVCHRPCFFGV-UHFFFAOYSA-N 50026868 2-(1H-indol-3-yl)-N,N-dimethylethanamine::DMT::N,N-dimethyltryptamine::CHEMBL12420::N,N-dimethyl-1H-indole-3-ethylamine::3-[2-(dimethylamino)ethyl]indole::3-(2-dimethylaminoethyl)indole::2-(3-indolyl)ethyldimethylamine::WO2023019367, Compound DMT::US20240246911, Compound DMT::US20240166618, Compound DMT::US20240317683, Compound DMT::US20250034106, Compound DMT 5-hydroxytryptamine receptor 2A Homo sapiens 65 ChEMBL 10.1021/jm980692q 10.7270/Q2N29W45 10090793 Blair, JB; Marona-Lewicka, D; Kanthasamy, A; Lucaites, VL; Nelson, DL; Nichols, DE 4/13/1999 11/10/2009 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026868 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026868&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFV 9AS1,9AS2 6089 103936452 CHEMBL12420 DB01488 C08302 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 50411375 CN(C)CCc1c[nH]c2ccccc12 InChI=1S/C12H16N2/c1-14(2)8-7-10-9-13-12-6-4-3-5-11(10)12/h3-6,9,13H,7-8H2,1-2H3 DMULVCHRPCFFGV-UHFFFAOYSA-N 50026868 2-(1H-indol-3-yl)-N,N-dimethylethanamine::DMT::N,N-dimethyltryptamine::CHEMBL12420::N,N-dimethyl-1H-indole-3-ethylamine::3-[2-(dimethylamino)ethyl]indole::3-(2-dimethylaminoethyl)indole::2-(3-indolyl)ethyldimethylamine::WO2023019367, Compound DMT::US20240246911, Compound DMT::US20240166618, Compound DMT::US20240317683, Compound DMT::US20250034106, Compound DMT 5-hydroxytryptamine receptor 2A Rattus norvegicus 1636 ChEMBL 10.1016/j.bmc.2008.02.033 10.7270/Q25D8RNZ 18296055 Parker, MA; Kurrasch, DM; Nichols, DE 4/24/2008 1/11/2010 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026868 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026868&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFV 9AS1,9AS2 6089 103936452 CHEMBL12420 DB01488 C08302 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 51431966 CN(C)CCc1c[nH]c2ccccc12 InChI=1S/C12H16N2/c1-14(2)8-7-10-9-13-12-6-4-3-5-11(10)12/h3-6,9,13H,7-8H2,1-2H3 DMULVCHRPCFFGV-UHFFFAOYSA-N 50026868 2-(1H-indol-3-yl)-N,N-dimethylethanamine::DMT::N,N-dimethyltryptamine::CHEMBL12420::N,N-dimethyl-1H-indole-3-ethylamine::3-[2-(dimethylamino)ethyl]indole::3-(2-dimethylaminoethyl)indole::2-(3-indolyl)ethyldimethylamine::WO2023019367, Compound DMT::US20240246911, Compound DMT::US20240166618, Compound DMT::US20240317683, Compound DMT::US20250034106, Compound DMT 5-hydroxytryptamine receptor 2A Homo sapiens 22 ChEMBL 10.1021/acsmedchemlett.1c00577 10.7270/Q2Z89H7T 34917241 Kargbo, RB 12/9/2021 8/24/2022 Usona Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026868 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026868&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFV 9AS1,9AS2 6089 103936452 CHEMBL12420 DB01488 C08302 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51441330 CN(C)CCc1c[nH]c2ccccc12 InChI=1S/C12H16N2/c1-14(2)8-7-10-9-13-12-6-4-3-5-11(10)12/h3-6,9,13H,7-8H2,1-2H3 DMULVCHRPCFFGV-UHFFFAOYSA-N 50026868 2-(1H-indol-3-yl)-N,N-dimethylethanamine::DMT::N,N-dimethyltryptamine::CHEMBL12420::N,N-dimethyl-1H-indole-3-ethylamine::3-[2-(dimethylamino)ethyl]indole::3-(2-dimethylaminoethyl)indole::2-(3-indolyl)ethyldimethylamine::WO2023019367, Compound DMT::US20240246911, Compound DMT::US20240166618, Compound DMT::US20240317683, Compound DMT::US20250034106, Compound DMT 5-hydroxytryptamine receptor 2A Homo sapiens 22 ChEMBL 10.1021/acsmedchemlett.2c00129 10.7270/Q23T9N3F 35450349 Kargbo, RB 4/14/2022 3/5/2023 Usona Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026868 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026868&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFV 9AS1,9AS2 6089 103936452 CHEMBL12420 DB01488 C08302 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51566568 CN(C)CCc1c[nH]c2ccccc12 InChI=1S/C12H16N2/c1-14(2)8-7-10-9-13-12-6-4-3-5-11(10)12/h3-6,9,13H,7-8H2,1-2H3 DMULVCHRPCFFGV-UHFFFAOYSA-N 50026868 2-(1H-indol-3-yl)-N,N-dimethylethanamine::DMT::N,N-dimethyltryptamine::CHEMBL12420::N,N-dimethyl-1H-indole-3-ethylamine::3-[2-(dimethylamino)ethyl]indole::3-(2-dimethylaminoethyl)indole::2-(3-indolyl)ethyldimethylamine::WO2023019367, Compound DMT::US20240246911, Compound DMT::US20240166618, Compound DMT::US20240317683, Compound DMT::US20250034106, Compound DMT 5-hydroxytryptamine receptor 2A Homo sapiens 220 ChEMBL 10.7270/Q26Q22P8 37736183 Layzell, M; Rands, P; Good, M; Joel, Z; Cousins, R; Benway, T; James, E; Routledge, C 9/14/2023 12/20/2024 Small Pharma. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026868 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026868&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFV 9AS1,9AS2 6089 103936452 CHEMBL12420 DB01488 C08302 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51566569 CN(C)CCc1c[nH]c2ccccc12 InChI=1S/C12H16N2/c1-14(2)8-7-10-9-13-12-6-4-3-5-11(10)12/h3-6,9,13H,7-8H2,1-2H3 DMULVCHRPCFFGV-UHFFFAOYSA-N 50026868 2-(1H-indol-3-yl)-N,N-dimethylethanamine::DMT::N,N-dimethyltryptamine::CHEMBL12420::N,N-dimethyl-1H-indole-3-ethylamine::3-[2-(dimethylamino)ethyl]indole::3-(2-dimethylaminoethyl)indole::2-(3-indolyl)ethyldimethylamine::WO2023019367, Compound DMT::US20240246911, Compound DMT::US20240166618, Compound DMT::US20240317683, Compound DMT::US20250034106, Compound DMT 5-hydroxytryptamine receptor 2A Homo sapiens 150 ChEMBL 10.7270/Q26Q22P8 37736183 Layzell, M; Rands, P; Good, M; Joel, Z; Cousins, R; Benway, T; James, E; Routledge, C 9/14/2023 12/20/2024 Small Pharma. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026868 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026868&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFV 9AS1,9AS2 6089 103936452 CHEMBL12420 DB01488 C08302 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51566602 CN(C)CCc1c[nH]c2ccccc12 InChI=1S/C12H16N2/c1-14(2)8-7-10-9-13-12-6-4-3-5-11(10)12/h3-6,9,13H,7-8H2,1-2H3 DMULVCHRPCFFGV-UHFFFAOYSA-N 50026868 2-(1H-indol-3-yl)-N,N-dimethylethanamine::DMT::N,N-dimethyltryptamine::CHEMBL12420::N,N-dimethyl-1H-indole-3-ethylamine::3-[2-(dimethylamino)ethyl]indole::3-(2-dimethylaminoethyl)indole::2-(3-indolyl)ethyldimethylamine::WO2023019367, Compound DMT::US20240246911, Compound DMT::US20240166618, Compound DMT::US20240317683, Compound DMT::US20250034106, Compound DMT 5-hydroxytryptamine receptor 2A Homo sapiens 60 ChEMBL 10.7270/Q26Q22P8 37736183 Layzell, M; Rands, P; Good, M; Joel, Z; Cousins, R; Benway, T; James, E; Routledge, C 9/14/2023 12/20/2024 Small Pharma. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026868 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026868&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFV 9AS1,9AS2 6089 103936452 CHEMBL12420 DB01488 C08302 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51566603 CN(C)CCc1c[nH]c2ccccc12 InChI=1S/C12H16N2/c1-14(2)8-7-10-9-13-12-6-4-3-5-11(10)12/h3-6,9,13H,7-8H2,1-2H3 DMULVCHRPCFFGV-UHFFFAOYSA-N 50026868 2-(1H-indol-3-yl)-N,N-dimethylethanamine::DMT::N,N-dimethyltryptamine::CHEMBL12420::N,N-dimethyl-1H-indole-3-ethylamine::3-[2-(dimethylamino)ethyl]indole::3-(2-dimethylaminoethyl)indole::2-(3-indolyl)ethyldimethylamine::WO2023019367, Compound DMT::US20240246911, Compound DMT::US20240166618, Compound DMT::US20240317683, Compound DMT::US20250034106, Compound DMT 5-hydroxytryptamine receptor 2A Homo sapiens 40 ChEMBL 10.7270/Q26Q22P8 37736183 Layzell, M; Rands, P; Good, M; Joel, Z; Cousins, R; Benway, T; James, E; Routledge, C 9/14/2023 12/20/2024 Small Pharma. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026868 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026868&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFV 9AS1,9AS2 6089 103936452 CHEMBL12420 DB01488 C08302 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 157438 CN(C)CCc1c[nH]c2ccccc12 InChI=1S/C12H16N2/c1-14(2)8-7-10-9-13-12-6-4-3-5-11(10)12/h3-6,9,13H,7-8H2,1-2H3 DMULVCHRPCFFGV-UHFFFAOYSA-N 50026868 2-(1H-indol-3-yl)-N,N-dimethylethanamine::DMT::N,N-dimethyltryptamine::CHEMBL12420::N,N-dimethyl-1H-indole-3-ethylamine::3-[2-(dimethylamino)ethyl]indole::3-(2-dimethylaminoethyl)indole::2-(3-indolyl)ethyldimethylamine::WO2023019367, Compound DMT::US20240246911, Compound DMT::US20240166618, Compound DMT::US20240317683, Compound DMT::US20250034106, Compound DMT 5-hydroxytryptamine receptor 2A Rattus norvegicus 42 PDSP Ki 10.7270/Q2FX77Z2 2795135 McKenna, DJ; Peroutka, SJ 12/28/1989 11/22/2011 Stanford University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026868 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026868&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFV 9AS1,9AS2 6089 103936452 CHEMBL12420 DB01488 C08302 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 391590 CN(C)CCc1c[nH]c2ccccc12 InChI=1S/C12H16N2/c1-14(2)8-7-10-9-13-12-6-4-3-5-11(10)12/h3-6,9,13H,7-8H2,1-2H3 DMULVCHRPCFFGV-UHFFFAOYSA-N 50026868 2-(1H-indol-3-yl)-N,N-dimethylethanamine::DMT::N,N-dimethyltryptamine::CHEMBL12420::N,N-dimethyl-1H-indole-3-ethylamine::3-[2-(dimethylamino)ethyl]indole::3-(2-dimethylaminoethyl)indole::2-(3-indolyl)ethyldimethylamine::WO2023019367, Compound DMT::US20240246911, Compound DMT::US20240166618, Compound DMT::US20240317683, Compound DMT::US20250034106, Compound DMT 5-hydroxytryptamine receptor 2A Homo sapiens 181 Curated from the literature by BindingDB 10.7270/Q2ZG6XSW 20126400 aid2060762 Ray, TS 2/2/2010 4/24/2025 University of Oklahoma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026868 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026868&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFV 9AS1,9AS2 6089 103936452 CHEMBL12420 DB01488 C08302 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 391592 CN(C)CCc1c[nH]c2ccccc12 InChI=1S/C12H16N2/c1-14(2)8-7-10-9-13-12-6-4-3-5-11(10)12/h3-6,9,13H,7-8H2,1-2H3 DMULVCHRPCFFGV-UHFFFAOYSA-N 50026868 2-(1H-indol-3-yl)-N,N-dimethylethanamine::DMT::N,N-dimethyltryptamine::CHEMBL12420::N,N-dimethyl-1H-indole-3-ethylamine::3-[2-(dimethylamino)ethyl]indole::3-(2-dimethylaminoethyl)indole::2-(3-indolyl)ethyldimethylamine::WO2023019367, Compound DMT::US20240246911, Compound DMT::US20240166618, Compound DMT::US20240317683, Compound DMT::US20250034106, Compound DMT 5-hydroxytryptamine receptor 2A Homo sapiens 439.9 Curated from the literature by BindingDB 10.7270/Q2ZG6XSW 20126400 aid2060762 Ray, TS 2/2/2010 4/24/2025 University of Oklahoma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026868 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026868&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFV 9AS1,9AS2 6089 103936452 CHEMBL12420 DB01488 C08302 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1237700 CN(C)CCc1c[nH]c2ccccc12 InChI=1S/C12H16N2/c1-14(2)8-7-10-9-13-12-6-4-3-5-11(10)12/h3-6,9,13H,7-8H2,1-2H3 DMULVCHRPCFFGV-UHFFFAOYSA-N 50026868 2-(1H-indol-3-yl)-N,N-dimethylethanamine::DMT::N,N-dimethyltryptamine::CHEMBL12420::N,N-dimethyl-1H-indole-3-ethylamine::3-[2-(dimethylamino)ethyl]indole::3-(2-dimethylaminoethyl)indole::2-(3-indolyl)ethyldimethylamine::WO2023019367, Compound DMT::US20240246911, Compound DMT::US20240166618, Compound DMT::US20240317683, Compound DMT::US20250034106, Compound DMT 5-hydroxytryptamine receptor 2A Homo sapiens <10000 WIPO 10.7270/Q2QN6BNM aid1919199 WO2023019327 Abdelmalik, S; A., AJ; Guy, H 2/23/2023 3/5/2023 Mindset Pharma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026868 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026868&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFV 9AS1,9AS2 6089 103936452 CHEMBL12420 DB01488 C08302 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1415153 CN(C)CCc1c[nH]c2ccccc12 InChI=1S/C12H16N2/c1-14(2)8-7-10-9-13-12-6-4-3-5-11(10)12/h3-6,9,13H,7-8H2,1-2H3 DMULVCHRPCFFGV-UHFFFAOYSA-N 50026868 2-(1H-indol-3-yl)-N,N-dimethylethanamine::DMT::N,N-dimethyltryptamine::CHEMBL12420::N,N-dimethyl-1H-indole-3-ethylamine::3-[2-(dimethylamino)ethyl]indole::3-(2-dimethylaminoethyl)indole::2-(3-indolyl)ethyldimethylamine::WO2023019367, Compound DMT::US20240246911, Compound DMT::US20240166618, Compound DMT::US20240317683, Compound DMT::US20250034106, Compound DMT 5-hydroxytryptamine receptor 2A Homo sapiens 416 US Patent 10.7270/Q2R49W2W aid1963741 US20240166618 KRUEGEL, AC 5/23/2024 8/26/2024 Gilgamesh Pharmaceuticals http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026868 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026868&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFV 9AS1,9AS2 6089 103936452 CHEMBL12420 DB01488 C08302 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1430281 CN(C)CCc1c[nH]c2ccccc12 InChI=1S/C12H16N2/c1-14(2)8-7-10-9-13-12-6-4-3-5-11(10)12/h3-6,9,13H,7-8H2,1-2H3 DMULVCHRPCFFGV-UHFFFAOYSA-N 50026868 2-(1H-indol-3-yl)-N,N-dimethylethanamine::DMT::N,N-dimethyltryptamine::CHEMBL12420::N,N-dimethyl-1H-indole-3-ethylamine::3-[2-(dimethylamino)ethyl]indole::3-(2-dimethylaminoethyl)indole::2-(3-indolyl)ethyldimethylamine::WO2023019367, Compound DMT::US20240246911, Compound DMT::US20240166618, Compound DMT::US20240317683, Compound DMT::US20250034106, Compound DMT 5-hydroxytryptamine receptor 2A Homo sapiens 416 US Patent 10.7270/Q2794904 aid1964011 US20240246911 KRUEGEL, AC 7/25/2024 11/7/2024 Gilgamesh Pharmaceuticals http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026868 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026868&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFV 9AS1,9AS2 6089 103936452 CHEMBL12420 DB01488 C08302 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1459342 CN(C)CCc1c[nH]c2ccccc12 InChI=1S/C12H16N2/c1-14(2)8-7-10-9-13-12-6-4-3-5-11(10)12/h3-6,9,13H,7-8H2,1-2H3 DMULVCHRPCFFGV-UHFFFAOYSA-N 50026868 2-(1H-indol-3-yl)-N,N-dimethylethanamine::DMT::N,N-dimethyltryptamine::CHEMBL12420::N,N-dimethyl-1H-indole-3-ethylamine::3-[2-(dimethylamino)ethyl]indole::3-(2-dimethylaminoethyl)indole::2-(3-indolyl)ethyldimethylamine::WO2023019367, Compound DMT::US20240246911, Compound DMT::US20240166618, Compound DMT::US20240317683, Compound DMT::US20250034106, Compound DMT 5-hydroxytryptamine receptor 2A Homo sapiens <2000 US Patent 10.7270/Q2V129BP aid2060581 US20240376052 Slassi, A; Araujo, JA; Higgins, G 11/14/2024 3/20/2025 Mindset Pharma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026868 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026868&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFV 9AS1,9AS2 6089 103936452 CHEMBL12420 DB01488 C08302 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1466004 CN(C)CCc1c[nH]c2ccccc12 InChI=1S/C12H16N2/c1-14(2)8-7-10-9-13-12-6-4-3-5-11(10)12/h3-6,9,13H,7-8H2,1-2H3 DMULVCHRPCFFGV-UHFFFAOYSA-N 50026868 2-(1H-indol-3-yl)-N,N-dimethylethanamine::DMT::N,N-dimethyltryptamine::CHEMBL12420::N,N-dimethyl-1H-indole-3-ethylamine::3-[2-(dimethylamino)ethyl]indole::3-(2-dimethylaminoethyl)indole::2-(3-indolyl)ethyldimethylamine::WO2023019367, Compound DMT::US20240246911, Compound DMT::US20240166618, Compound DMT::US20240317683, Compound DMT::US20250034106, Compound DMT 5-hydroxytryptamine receptor 2A Homo sapiens 2323.000000 Curated from the literature by BindingDB 10.7270/Q2ZG6XSW 20126400 aid2060761 Ray, TS 2/2/2010 4/24/2025 University of Oklahoma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026868 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026868&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFV 9AS1,9AS2 6089 103936452 CHEMBL12420 DB01488 C08302 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1484103 CN(C)CCc1c[nH]c2ccccc12 InChI=1S/C12H16N2/c1-14(2)8-7-10-9-13-12-6-4-3-5-11(10)12/h3-6,9,13H,7-8H2,1-2H3 DMULVCHRPCFFGV-UHFFFAOYSA-N 50026868 2-(1H-indol-3-yl)-N,N-dimethylethanamine::DMT::N,N-dimethyltryptamine::CHEMBL12420::N,N-dimethyl-1H-indole-3-ethylamine::3-[2-(dimethylamino)ethyl]indole::3-(2-dimethylaminoethyl)indole::2-(3-indolyl)ethyldimethylamine::WO2023019367, Compound DMT::US20240246911, Compound DMT::US20240166618, Compound DMT::US20240317683, Compound DMT::US20250034106, Compound DMT 5-hydroxytryptamine receptor 2A Homo sapiens <500 US Patent 10.7270/Q26D5ZHT aid2060955 US20250034106 Slassi, A; Araujo, JA 1/30/2025 6/5/2025 Mindset Pharma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026868 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026868&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFV 9AS1,9AS2 6089 103936452 CHEMBL12420 DB01488 C08302 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 50130150 CN(C)CCc1c[nH]c2ccccc12 InChI=1S/C12H16N2/c1-14(2)8-7-10-9-13-12-6-4-3-5-11(10)12/h3-6,9,13H,7-8H2,1-2H3 DMULVCHRPCFFGV-UHFFFAOYSA-N 50026868 2-(1H-indol-3-yl)-N,N-dimethylethanamine::DMT::N,N-dimethyltryptamine::CHEMBL12420::N,N-dimethyl-1H-indole-3-ethylamine::3-[2-(dimethylamino)ethyl]indole::3-(2-dimethylaminoethyl)indole::2-(3-indolyl)ethyldimethylamine::WO2023019367, Compound DMT::US20240246911, Compound DMT::US20240166618, Compound DMT::US20240317683, Compound DMT::US20250034106, Compound DMT 5-hydroxytryptamine receptor 2A Homo sapiens 65 ChEMBL 10.1021/jm980692q 10.7270/Q2N29W45 10090793 Blair, JB; Marona-Lewicka, D; Kanthasamy, A; Lucaites, VL; Nelson, DL; Nichols, DE 4/13/1999 11/10/2009 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026868 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026868&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFV 9AS1,9AS2 6089 103936452 CHEMBL12420 DB01488 C08302 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 50411375 CN(C)CCc1c[nH]c2ccccc12 InChI=1S/C12H16N2/c1-14(2)8-7-10-9-13-12-6-4-3-5-11(10)12/h3-6,9,13H,7-8H2,1-2H3 DMULVCHRPCFFGV-UHFFFAOYSA-N 50026868 2-(1H-indol-3-yl)-N,N-dimethylethanamine::DMT::N,N-dimethyltryptamine::CHEMBL12420::N,N-dimethyl-1H-indole-3-ethylamine::3-[2-(dimethylamino)ethyl]indole::3-(2-dimethylaminoethyl)indole::2-(3-indolyl)ethyldimethylamine::WO2023019367, Compound DMT::US20240246911, Compound DMT::US20240166618, Compound DMT::US20240317683, Compound DMT::US20250034106, Compound DMT 5-hydroxytryptamine receptor 2A Rattus norvegicus 1636 ChEMBL 10.1016/j.bmc.2008.02.033 10.7270/Q25D8RNZ 18296055 Parker, MA; Kurrasch, DM; Nichols, DE 4/24/2008 1/11/2010 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026868 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026868&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFV 9AS1,9AS2 6089 103936452 CHEMBL12420 DB01488 C08302 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 51431966 CN(C)CCc1c[nH]c2ccccc12 InChI=1S/C12H16N2/c1-14(2)8-7-10-9-13-12-6-4-3-5-11(10)12/h3-6,9,13H,7-8H2,1-2H3 DMULVCHRPCFFGV-UHFFFAOYSA-N 50026868 2-(1H-indol-3-yl)-N,N-dimethylethanamine::DMT::N,N-dimethyltryptamine::CHEMBL12420::N,N-dimethyl-1H-indole-3-ethylamine::3-[2-(dimethylamino)ethyl]indole::3-(2-dimethylaminoethyl)indole::2-(3-indolyl)ethyldimethylamine::WO2023019367, Compound DMT::US20240246911, Compound DMT::US20240166618, Compound DMT::US20240317683, Compound DMT::US20250034106, Compound DMT 5-hydroxytryptamine receptor 2A Homo sapiens 22 ChEMBL 10.1021/acsmedchemlett.1c00577 10.7270/Q2Z89H7T 34917241 Kargbo, RB 12/9/2021 8/24/2022 Usona Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026868 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026868&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFV 9AS1,9AS2 6089 103936452 CHEMBL12420 DB01488 C08302 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51441330 CN(C)CCc1c[nH]c2ccccc12 InChI=1S/C12H16N2/c1-14(2)8-7-10-9-13-12-6-4-3-5-11(10)12/h3-6,9,13H,7-8H2,1-2H3 DMULVCHRPCFFGV-UHFFFAOYSA-N 50026868 2-(1H-indol-3-yl)-N,N-dimethylethanamine::DMT::N,N-dimethyltryptamine::CHEMBL12420::N,N-dimethyl-1H-indole-3-ethylamine::3-[2-(dimethylamino)ethyl]indole::3-(2-dimethylaminoethyl)indole::2-(3-indolyl)ethyldimethylamine::WO2023019367, Compound DMT::US20240246911, Compound DMT::US20240166618, Compound DMT::US20240317683, Compound DMT::US20250034106, Compound DMT 5-hydroxytryptamine receptor 2A Homo sapiens 22 ChEMBL 10.1021/acsmedchemlett.2c00129 10.7270/Q23T9N3F 35450349 Kargbo, RB 4/14/2022 3/5/2023 Usona Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026868 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026868&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFV 9AS1,9AS2 6089 103936452 CHEMBL12420 DB01488 C08302 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51566568 CN(C)CCc1c[nH]c2ccccc12 InChI=1S/C12H16N2/c1-14(2)8-7-10-9-13-12-6-4-3-5-11(10)12/h3-6,9,13H,7-8H2,1-2H3 DMULVCHRPCFFGV-UHFFFAOYSA-N 50026868 2-(1H-indol-3-yl)-N,N-dimethylethanamine::DMT::N,N-dimethyltryptamine::CHEMBL12420::N,N-dimethyl-1H-indole-3-ethylamine::3-[2-(dimethylamino)ethyl]indole::3-(2-dimethylaminoethyl)indole::2-(3-indolyl)ethyldimethylamine::WO2023019367, Compound DMT::US20240246911, Compound DMT::US20240166618, Compound DMT::US20240317683, Compound DMT::US20250034106, Compound DMT 5-hydroxytryptamine receptor 2A Homo sapiens 220 ChEMBL 10.7270/Q26Q22P8 37736183 Layzell, M; Rands, P; Good, M; Joel, Z; Cousins, R; Benway, T; James, E; Routledge, C 9/14/2023 12/20/2024 Small Pharma. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026868 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026868&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFV 9AS1,9AS2 6089 103936452 CHEMBL12420 DB01488 C08302 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51566569 CN(C)CCc1c[nH]c2ccccc12 InChI=1S/C12H16N2/c1-14(2)8-7-10-9-13-12-6-4-3-5-11(10)12/h3-6,9,13H,7-8H2,1-2H3 DMULVCHRPCFFGV-UHFFFAOYSA-N 50026868 2-(1H-indol-3-yl)-N,N-dimethylethanamine::DMT::N,N-dimethyltryptamine::CHEMBL12420::N,N-dimethyl-1H-indole-3-ethylamine::3-[2-(dimethylamino)ethyl]indole::3-(2-dimethylaminoethyl)indole::2-(3-indolyl)ethyldimethylamine::WO2023019367, Compound DMT::US20240246911, Compound DMT::US20240166618, Compound DMT::US20240317683, Compound DMT::US20250034106, Compound DMT 5-hydroxytryptamine receptor 2A Homo sapiens 150 ChEMBL 10.7270/Q26Q22P8 37736183 Layzell, M; Rands, P; Good, M; Joel, Z; Cousins, R; Benway, T; James, E; Routledge, C 9/14/2023 12/20/2024 Small Pharma. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026868 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026868&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFV 9AS1,9AS2 6089 103936452 CHEMBL12420 DB01488 C08302 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51566602 CN(C)CCc1c[nH]c2ccccc12 InChI=1S/C12H16N2/c1-14(2)8-7-10-9-13-12-6-4-3-5-11(10)12/h3-6,9,13H,7-8H2,1-2H3 DMULVCHRPCFFGV-UHFFFAOYSA-N 50026868 2-(1H-indol-3-yl)-N,N-dimethylethanamine::DMT::N,N-dimethyltryptamine::CHEMBL12420::N,N-dimethyl-1H-indole-3-ethylamine::3-[2-(dimethylamino)ethyl]indole::3-(2-dimethylaminoethyl)indole::2-(3-indolyl)ethyldimethylamine::WO2023019367, Compound DMT::US20240246911, Compound DMT::US20240166618, Compound DMT::US20240317683, Compound DMT::US20250034106, Compound DMT 5-hydroxytryptamine receptor 2A Homo sapiens 60 ChEMBL 10.7270/Q26Q22P8 37736183 Layzell, M; Rands, P; Good, M; Joel, Z; Cousins, R; Benway, T; James, E; Routledge, C 9/14/2023 12/20/2024 Small Pharma. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026868 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026868&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFV 9AS1,9AS2 6089 103936452 CHEMBL12420 DB01488 C08302 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51566603 CN(C)CCc1c[nH]c2ccccc12 InChI=1S/C12H16N2/c1-14(2)8-7-10-9-13-12-6-4-3-5-11(10)12/h3-6,9,13H,7-8H2,1-2H3 DMULVCHRPCFFGV-UHFFFAOYSA-N 50026868 2-(1H-indol-3-yl)-N,N-dimethylethanamine::DMT::N,N-dimethyltryptamine::CHEMBL12420::N,N-dimethyl-1H-indole-3-ethylamine::3-[2-(dimethylamino)ethyl]indole::3-(2-dimethylaminoethyl)indole::2-(3-indolyl)ethyldimethylamine::WO2023019367, Compound DMT::US20240246911, Compound DMT::US20240166618, Compound DMT::US20240317683, Compound DMT::US20250034106, Compound DMT 5-hydroxytryptamine receptor 2A Homo sapiens 40 ChEMBL 10.7270/Q26Q22P8 37736183 Layzell, M; Rands, P; Good, M; Joel, Z; Cousins, R; Benway, T; James, E; Routledge, C 9/14/2023 12/20/2024 Small Pharma. http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50026868 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50026868&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search A1AFV 9AS1,9AS2 6089 103936452 CHEMBL12420 DB01488 C08302 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 157448 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Rattus norvegicus 3.5 PDSP Ki 10.7270/Q2FX77Z2 2795135 McKenna, DJ; Peroutka, SJ 12/28/1989 11/22/2011 Stanford University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 159549 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Rattus norvegicus 5.47 PDSP Ki 10.1016/0024-3205(83)90740-3 10.7270/Q2DR2T0M 6645787 Battaglia, G; Shannon, M; Borgundvaag, B; Titeler, M 12/14/1983 12/20/2011 University of Toronto http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 159550 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Rattus norvegicus 3.16 PDSP Ki 10.1016/0024-3205(83)90740-3 10.7270/Q2DR2T0M 6645787 Battaglia, G; Shannon, M; Borgundvaag, B; Titeler, M 12/14/1983 12/20/2011 University of Toronto http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 159551 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Rattus norvegicus 3.23 PDSP Ki 10.1016/0024-3205(83)90740-3 10.7270/Q2DR2T0M 6645787 Battaglia, G; Shannon, M; Borgundvaag, B; Titeler, M 12/14/1983 12/20/2011 University of Toronto http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 162413 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Rattus norvegicus 7.07 PDSP Ki 10.1016/0028-3908(94)90059-0 10.7270/Q2M043X2 7984267 Boess, FG; Martin, IL 12/28/1994 12/30/2011 University of Alberta http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 162414 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Rattus norvegicus 12.02 PDSP Ki 10.1016/0028-3908(94)90059-0 10.7270/Q2M043X2 7984267 Boess, FG; Martin, IL 12/28/1994 12/30/2011 University of Alberta http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 179461 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Homo sapiens 21.38 PDSP Ki 10.1038/sj.bjp.0702751 10.7270/Q2GH9GH2 10498829 Porter, RH; Benwell, KR; Lamb, H; Malcolm, CS; Allen, NH; Revell, DF; Adams, DR; Sheardown, MJ 12/28/1999 4/13/2012 Cerebrus http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 180079 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Homo sapiens 2.7 PDSP Ki 10.1002/(SICI)1098-2396(200002)35:2<144::AID-SYN7>3.0.CO;2-K 10.7270/Q2ST7NDX 10611640 Egan, C; Grinde, E; Dupre, A; Roth, BL; Hake, M; Teitler, M; Herrick-Davis, K 12/28/2000 4/17/2012 Albany Medical College http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 180080 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Homo sapiens 5.2 PDSP Ki 10.1002/(SICI)1098-2396(200002)35:2<144::AID-SYN7>3.0.CO;2-K 10.7270/Q2ST7NDX 10611640 Egan, C; Grinde, E; Dupre, A; Roth, BL; Hake, M; Teitler, M; Herrick-Davis, K 12/28/2000 4/17/2012 Albany Medical College http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1415151 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Homo sapiens 0.890 US Patent 10.7270/Q2R49W2W aid1963741 US20240166618 KRUEGEL, AC 5/23/2024 8/26/2024 Gilgamesh Pharmaceuticals http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1457572 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Homo sapiens 0.890 US Patent 10.7270/Q2X06CJ0 aid2060558 US20240368151 KRUEGEL, AC 11/7/2024 3/14/2025 Gilgamesh Pharmaceuticals http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 50051670 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Rattus norvegicus 4.4 ChEMBL 10.1021/jm00006a015 10.7270/Q2NZ86N6 7699712 Monte, AP; Marona-Lewicka, D; Kanthasamy, A; Sanders-Bush, E; Nichols, DE 4/28/1995 11/10/2009 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 50086081 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Rattus norvegicus 4.4 ChEMBL 10.1021/jm960199j 10.7270/Q28914ZS 8709129 Monte, AP; Marona-Lewicka, D; Parker, MA; Wainscott, DB; Nelson, DL; Nichols, DE 9/6/1996 11/10/2009 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 50203190 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Rattus norvegicus 15 ChEMBL 10.1021/jm020153s 10.7270/Q2765G2F 12213075 Nichols, DE; Frescas, S; Marona-Lewicka, D; Kurrasch-Orbaugh, DM 9/5/2002 11/26/2012 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 50211403 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Homo sapiens 3.1 ChEMBL 10.1016/j.bmc.2008.04.050 10.7270/Q2G73FND 18468904 Nichols, DE; Frescas, SP; Chemel, BR; Rehder, KS; Zhong, D; Lewin, AH 6/5/2008 12/16/2012 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 50211405 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Homo sapiens 2.6 ChEMBL 10.1016/j.bmc.2008.04.050 10.7270/Q2G73FND 18468904 Nichols, DE; Frescas, SP; Chemel, BR; Rehder, KS; Zhong, D; Lewin, AH 6/5/2008 12/16/2012 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 50211411 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Homo sapiens 4 ChEMBL 10.1016/j.bmc.2008.04.050 10.7270/Q2G73FND 18468904 Nichols, DE; Frescas, SP; Chemel, BR; Rehder, KS; Zhong, D; Lewin, AH 6/5/2008 12/16/2012 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 50239812 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Rattus norvegicus 9.8 ChEMBL 10.1021/jm030064v 10.7270/Q20P0ZC1 12877591 Chambers, JJ; Parrish, JC; Jensen, NH; Kurrasch-Orbaugh, DM; Marona-Lewicka, D; Nichols, DE 7/24/2003 11/10/2009 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 50239825 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Rattus norvegicus 3.5 ChEMBL 10.1021/jm030064v 10.7270/Q20P0ZC1 12877591 Chambers, JJ; Parrish, JC; Jensen, NH; Kurrasch-Orbaugh, DM; Marona-Lewicka, D; Nichols, DE 7/24/2003 11/10/2009 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 50352648 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Rattus norvegicus 3.5 ChEMBL 10.1021/jm060272y 10.7270/Q2PC320K 16821786 McLean, TH; Chambers, JJ; Parrish, JC; Braden, MR; Marona-Lewicka, D; Kurrasch-Orbaugh, D; Nichols, DE 7/6/2006 11/10/2009 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 50352650 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Rattus norvegicus 9.8 ChEMBL 10.1021/jm060272y 10.7270/Q2PC320K 16821786 McLean, TH; Chambers, JJ; Parrish, JC; Braden, MR; Marona-Lewicka, D; Kurrasch-Orbaugh, D; Nichols, DE 7/6/2006 11/10/2009 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 50807350 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Rattus norvegicus 3.5 ChEMBL 10.1021/jm020153s 10.7270/Q2765G2F 12213075 Nichols, DE; Frescas, S; Marona-Lewicka, D; Kurrasch-Orbaugh, DM 9/5/2002 11/26/2012 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 50871494 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Homo sapiens 3.5 ChEMBL 10.1016/j.bmc.2008.04.050 10.7270/Q2G73FND 18468904 Nichols, DE; Frescas, SP; Chemel, BR; Rehder, KS; Zhong, D; Lewin, AH 6/5/2008 12/16/2012 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51157878 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Homo sapiens 3.2 ChEMBL 10.1021/jm0341204 10.7270/Q2Q242ZQ 14613313 Vázquez, MJ; Roa, AM; Reyes, F; Vega, A; Rivera-Sagredo, A; Thomas, DR; Díez, E; Hueso-Rodríguez, JA 11/20/2003 8/22/2020 Glaxosmithkline R&D http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51470283 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Homo sapiens 13 ChEMBL 10.7270/Q2WD44J5 36099411 Poulie, CBM; Pottie, E; Simon, IA; Harpsøe, K; D'Andrea, L; Komarov, IV; Gloriam, DE; Jensen, AA; Stove, CP; Kristensen, JL 9/22/2022 6/20/2023 University of Copenhagen http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51470295 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Homo sapiens 13 ChEMBL 10.7270/Q2WD44J5 36099411 Poulie, CBM; Pottie, E; Simon, IA; Harpsøe, K; D'Andrea, L; Komarov, IV; Gloriam, DE; Jensen, AA; Stove, CP; Kristensen, JL 9/22/2022 6/20/2023 University of Copenhagen http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51470307 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Homo sapiens 5.2 ChEMBL 10.7270/Q2WD44J5 36099411 Poulie, CBM; Pottie, E; Simon, IA; Harpsøe, K; D'Andrea, L; Komarov, IV; Gloriam, DE; Jensen, AA; Stove, CP; Kristensen, JL 9/22/2022 6/20/2023 University of Copenhagen http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51470315 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Homo sapiens 5.4 ChEMBL 10.7270/Q2WD44J5 36099411 Poulie, CBM; Pottie, E; Simon, IA; Harpsøe, K; D'Andrea, L; Komarov, IV; Gloriam, DE; Jensen, AA; Stove, CP; Kristensen, JL 9/22/2022 6/20/2023 University of Copenhagen http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1466950 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 50241702 [N-methyl-3H]LSD::CHEMBL463207::lsd 5-hydroxytryptamine receptor 2A Homo sapiens 11.300000 Curated from the literature by BindingDB 10.7270/Q2ZG6XSW 20126400 aid2060761 Ray, TS 2/2/2010 4/24/2025 University of Oklahoma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50241702 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50241702&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 104098839 CHEMBL463207 DB04829 C07542 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 50363788 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 50241702 [N-methyl-3H]LSD::CHEMBL463207::lsd 5-hydroxytryptamine receptor 2A Homo sapiens 21.17 ChEMBL 10.1021/np0601760 10.7270/Q2H9950V 17067154 Hedner, E; Sjogren, M; Frandberg, PA; Johansson, T; Goransson, U; Dahlstrom, M; Jonsson, P; Nyberg, F; Bohlin, L 10/27/2006 1/11/2010 Uppsala University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50241702 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50241702&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 104098839 CHEMBL463207 DB04829 C07542 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 50666230 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD Serotonin 2 (5-HT2) receptor Rattus norvegicus 2.5 ChEMBL 10.1021/jm00082a014 10.7270/Q29K4BV4 1542100 Glennon, RA; Raghupathi, R; Bartyzel, P; Teitler, M; Leonhardt, S 4/3/1992 10/24/2012 Virginia Commonwealth University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000484&target=Serotonin+2+%285-HT2%29+receptor&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=Serotonin+2+%285-HT2%29+receptor&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 3 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 MVNLGNAVRSLLMHLIGLLVWQFDISISPVAAIVTDTFNSSDGGRLFQFPDGVQNWPALSIVVIIIMTIGGNILVIMAVSMEKKLHNATNYFLMSLAIADMLVGLLVMPLSLLAILYDYVWPLPRYLCPVWISLDVLFSTASIMHLCAISLDRYVAIRNPIEHSRFNSRTKAIMKIAIVWAISIGVSVPIPVIGLRDESKVFVNNTTCVLNDPNFVLIGSFVAFFIPLTIMVITYFLTIYVLRRQTLMLLRGHTEEELANMSLNFLNCCCKKNGGEEENAPNPNPDQKPRRKKKEKRPRGTMQAINNEKKASKVLGIVFFVFLIMWCPFFITNILSVLCGKACNQKLMEKLLNVFVWIGYVCSGINPLVYTLFNKIYRRAFSKYLRCDYKPDKKPPVRQIPRVAATALSGRELNVNIYRHTNERVARKANDPEPGIEMQVENLELPVNPSNVVSERISSV 5-hydroxytryptamine receptor 2C 5HT2C_RAT P08909 MASSYKMSEQSTISEHILQKTCDHLILTDRSGLKAESAAEEMKQTAENQGNTVHWAALLIFAVIIPTIGGNILVILAVSLEKRLQYATNYFLMSLAVADLLVGLFVMPIALLTIMFEATWPLPLALCPAWLFLDVLFSTASIMHLCAISLDRYIAIKKPIQANQCNSRTTAFVKITVVWLISIGIAIPVPIKGIEADVVNAHNITCELTKDRFGSFMLFGSLAAFFAPLTIMIVTYFLTIHALRKKAYLVRNRPPQRLTRWTVSTVLQREDSSFSSPEKMVMLDGSHKDKILPNSTDETLMRRMSSAGKKPAQTISNEQRASKVLGIVFLFFLLMWCPFFITNVTLALCDSCNQTTLKTLLQIFVWVGYVSSGVNPLIYTLFNKTFREAFGRYITCNYQATKSVKVLRKCSSTLYFGNSMVENSKFFTKHGIRNGINPAMYQSPVRLRSSTIQSSSIILLNTFLTENDGDKVEDQVSYI 5-hydroxytryptamine receptor 2B 5HT2B_RAT P30994 Q9QW44 51148412 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD Serotonin 2 (5-HT2) receptor Rattus norvegicus 6.3 ChEMBL 10.1021/jm00018a019 10.7270/Q2PC3535 7658446 Oberlender, R; Ramachandran, PV; Johnson, MP; Huang, X; Nichols, DE 9/1/1995 8/21/2020 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000484&target=Serotonin+2+%285-HT2%29+receptor&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=Serotonin+2+%285-HT2%29+receptor&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 3 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 MVNLGNAVRSLLMHLIGLLVWQFDISISPVAAIVTDTFNSSDGGRLFQFPDGVQNWPALSIVVIIIMTIGGNILVIMAVSMEKKLHNATNYFLMSLAIADMLVGLLVMPLSLLAILYDYVWPLPRYLCPVWISLDVLFSTASIMHLCAISLDRYVAIRNPIEHSRFNSRTKAIMKIAIVWAISIGVSVPIPVIGLRDESKVFVNNTTCVLNDPNFVLIGSFVAFFIPLTIMVITYFLTIYVLRRQTLMLLRGHTEEELANMSLNFLNCCCKKNGGEEENAPNPNPDQKPRRKKKEKRPRGTMQAINNEKKASKVLGIVFFVFLIMWCPFFITNILSVLCGKACNQKLMEKLLNVFVWIGYVCSGINPLVYTLFNKIYRRAFSKYLRCDYKPDKKPPVRQIPRVAATALSGRELNVNIYRHTNERVARKANDPEPGIEMQVENLELPVNPSNVVSERISSV 5-hydroxytryptamine receptor 2C 5HT2C_RAT P08909 MASSYKMSEQSTISEHILQKTCDHLILTDRSGLKAESAAEEMKQTAENQGNTVHWAALLIFAVIIPTIGGNILVILAVSLEKRLQYATNYFLMSLAVADLLVGLFVMPIALLTIMFEATWPLPLALCPAWLFLDVLFSTASIMHLCAISLDRYIAIKKPIQANQCNSRTTAFVKITVVWLISIGIAIPVPIKGIEADVVNAHNITCELTKDRFGSFMLFGSLAAFFAPLTIMIVTYFLTIHALRKKAYLVRNRPPQRLTRWTVSTVLQREDSSFSSPEKMVMLDGSHKDKILPNSTDETLMRRMSSAGKKPAQTISNEQRASKVLGIVFLFFLLMWCPFFITNVTLALCDSCNQTTLKTLLQIFVWVGYVSSGVNPLIYTLFNKTFREAFGRYITCNYQATKSVKVLRKCSSTLYFGNSMVENSKFFTKHGIRNGINPAMYQSPVRLRSSTIQSSSIILLNTFLTENDGDKVEDQVSYI 5-hydroxytryptamine receptor 2B 5HT2B_RAT P30994 Q9QW44 157448 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Rattus norvegicus 3.5 PDSP Ki 10.7270/Q2FX77Z2 2795135 McKenna, DJ; Peroutka, SJ 12/28/1989 11/22/2011 Stanford University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 159549 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Rattus norvegicus 5.47 PDSP Ki 10.1016/0024-3205(83)90740-3 10.7270/Q2DR2T0M 6645787 Battaglia, G; Shannon, M; Borgundvaag, B; Titeler, M 12/14/1983 12/20/2011 University of Toronto http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 159550 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Rattus norvegicus 3.16 PDSP Ki 10.1016/0024-3205(83)90740-3 10.7270/Q2DR2T0M 6645787 Battaglia, G; Shannon, M; Borgundvaag, B; Titeler, M 12/14/1983 12/20/2011 University of Toronto http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 159551 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Rattus norvegicus 3.23 PDSP Ki 10.1016/0024-3205(83)90740-3 10.7270/Q2DR2T0M 6645787 Battaglia, G; Shannon, M; Borgundvaag, B; Titeler, M 12/14/1983 12/20/2011 University of Toronto http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 162413 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Rattus norvegicus 7.07 PDSP Ki 10.1016/0028-3908(94)90059-0 10.7270/Q2M043X2 7984267 Boess, FG; Martin, IL 12/28/1994 12/30/2011 University of Alberta http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 162414 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Rattus norvegicus 12.02 PDSP Ki 10.1016/0028-3908(94)90059-0 10.7270/Q2M043X2 7984267 Boess, FG; Martin, IL 12/28/1994 12/30/2011 University of Alberta http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 179461 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Homo sapiens 21.38 PDSP Ki 10.1038/sj.bjp.0702751 10.7270/Q2GH9GH2 10498829 Porter, RH; Benwell, KR; Lamb, H; Malcolm, CS; Allen, NH; Revell, DF; Adams, DR; Sheardown, MJ 12/28/1999 4/13/2012 Cerebrus http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 180079 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Homo sapiens 2.7 PDSP Ki 10.1002/(SICI)1098-2396(200002)35:2<144::AID-SYN7>3.0.CO;2-K 10.7270/Q2ST7NDX 10611640 Egan, C; Grinde, E; Dupre, A; Roth, BL; Hake, M; Teitler, M; Herrick-Davis, K 12/28/2000 4/17/2012 Albany Medical College http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 180080 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Homo sapiens 5.2 PDSP Ki 10.1002/(SICI)1098-2396(200002)35:2<144::AID-SYN7>3.0.CO;2-K 10.7270/Q2ST7NDX 10611640 Egan, C; Grinde, E; Dupre, A; Roth, BL; Hake, M; Teitler, M; Herrick-Davis, K 12/28/2000 4/17/2012 Albany Medical College http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1415151 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Homo sapiens 0.890 US Patent 10.7270/Q2R49W2W aid1963741 US20240166618 KRUEGEL, AC 5/23/2024 8/26/2024 Gilgamesh Pharmaceuticals http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1457572 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Homo sapiens 0.890 US Patent 10.7270/Q2X06CJ0 aid2060558 US20240368151 KRUEGEL, AC 11/7/2024 3/14/2025 Gilgamesh Pharmaceuticals http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 50051670 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Rattus norvegicus 4.4 ChEMBL 10.1021/jm00006a015 10.7270/Q2NZ86N6 7699712 Monte, AP; Marona-Lewicka, D; Kanthasamy, A; Sanders-Bush, E; Nichols, DE 4/28/1995 11/10/2009 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 50086081 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Rattus norvegicus 4.4 ChEMBL 10.1021/jm960199j 10.7270/Q28914ZS 8709129 Monte, AP; Marona-Lewicka, D; Parker, MA; Wainscott, DB; Nelson, DL; Nichols, DE 9/6/1996 11/10/2009 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 50203190 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Rattus norvegicus 15 ChEMBL 10.1021/jm020153s 10.7270/Q2765G2F 12213075 Nichols, DE; Frescas, S; Marona-Lewicka, D; Kurrasch-Orbaugh, DM 9/5/2002 11/26/2012 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 50211403 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Homo sapiens 3.1 ChEMBL 10.1016/j.bmc.2008.04.050 10.7270/Q2G73FND 18468904 Nichols, DE; Frescas, SP; Chemel, BR; Rehder, KS; Zhong, D; Lewin, AH 6/5/2008 12/16/2012 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 50211405 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Homo sapiens 2.6 ChEMBL 10.1016/j.bmc.2008.04.050 10.7270/Q2G73FND 18468904 Nichols, DE; Frescas, SP; Chemel, BR; Rehder, KS; Zhong, D; Lewin, AH 6/5/2008 12/16/2012 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 50211411 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Homo sapiens 4 ChEMBL 10.1016/j.bmc.2008.04.050 10.7270/Q2G73FND 18468904 Nichols, DE; Frescas, SP; Chemel, BR; Rehder, KS; Zhong, D; Lewin, AH 6/5/2008 12/16/2012 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 50239812 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Rattus norvegicus 9.8 ChEMBL 10.1021/jm030064v 10.7270/Q20P0ZC1 12877591 Chambers, JJ; Parrish, JC; Jensen, NH; Kurrasch-Orbaugh, DM; Marona-Lewicka, D; Nichols, DE 7/24/2003 11/10/2009 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 50239825 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Rattus norvegicus 3.5 ChEMBL 10.1021/jm030064v 10.7270/Q20P0ZC1 12877591 Chambers, JJ; Parrish, JC; Jensen, NH; Kurrasch-Orbaugh, DM; Marona-Lewicka, D; Nichols, DE 7/24/2003 11/10/2009 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 50352648 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Rattus norvegicus 3.5 ChEMBL 10.1021/jm060272y 10.7270/Q2PC320K 16821786 McLean, TH; Chambers, JJ; Parrish, JC; Braden, MR; Marona-Lewicka, D; Kurrasch-Orbaugh, D; Nichols, DE 7/6/2006 11/10/2009 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 50352650 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Rattus norvegicus 9.8 ChEMBL 10.1021/jm060272y 10.7270/Q2PC320K 16821786 McLean, TH; Chambers, JJ; Parrish, JC; Braden, MR; Marona-Lewicka, D; Kurrasch-Orbaugh, D; Nichols, DE 7/6/2006 11/10/2009 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 50807350 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Rattus norvegicus 3.5 ChEMBL 10.1021/jm020153s 10.7270/Q2765G2F 12213075 Nichols, DE; Frescas, S; Marona-Lewicka, D; Kurrasch-Orbaugh, DM 9/5/2002 11/26/2012 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2154&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 50871494 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Homo sapiens 3.5 ChEMBL 10.1016/j.bmc.2008.04.050 10.7270/Q2G73FND 18468904 Nichols, DE; Frescas, SP; Chemel, BR; Rehder, KS; Zhong, D; Lewin, AH 6/5/2008 12/16/2012 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51157878 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Homo sapiens 3.2 ChEMBL 10.1021/jm0341204 10.7270/Q2Q242ZQ 14613313 Vázquez, MJ; Roa, AM; Reyes, F; Vega, A; Rivera-Sagredo, A; Thomas, DR; Díez, E; Hueso-Rodríguez, JA 11/20/2003 8/22/2020 Glaxosmithkline R&D http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51470283 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Homo sapiens 13 ChEMBL 10.7270/Q2WD44J5 36099411 Poulie, CBM; Pottie, E; Simon, IA; Harpsøe, K; D'Andrea, L; Komarov, IV; Gloriam, DE; Jensen, AA; Stove, CP; Kristensen, JL 9/22/2022 6/20/2023 University of Copenhagen http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51470295 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Homo sapiens 13 ChEMBL 10.7270/Q2WD44J5 36099411 Poulie, CBM; Pottie, E; Simon, IA; Harpsøe, K; D'Andrea, L; Komarov, IV; Gloriam, DE; Jensen, AA; Stove, CP; Kristensen, JL 9/22/2022 6/20/2023 University of Copenhagen http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51470307 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Homo sapiens 5.2 ChEMBL 10.7270/Q2WD44J5 36099411 Poulie, CBM; Pottie, E; Simon, IA; Harpsøe, K; D'Andrea, L; Komarov, IV; Gloriam, DE; Jensen, AA; Stove, CP; Kristensen, JL 9/22/2022 6/20/2023 University of Copenhagen http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 51470315 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD 5-hydroxytryptamine receptor 2A Homo sapiens 5.4 ChEMBL 10.7270/Q2WD44J5 36099411 Poulie, CBM; Pottie, E; Simon, IA; Harpsøe, K; D'Andrea, L; Komarov, IV; Gloriam, DE; Jensen, AA; Stove, CP; Kristensen, JL 9/22/2022 6/20/2023 University of Copenhagen http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 1466950 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 50241702 [N-methyl-3H]LSD::CHEMBL463207::lsd 5-hydroxytryptamine receptor 2A Homo sapiens 11.300000 Curated from the literature by BindingDB 10.7270/Q2ZG6XSW 20126400 aid2060761 Ray, TS 2/2/2010 4/24/2025 University of Oklahoma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50241702 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50241702&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 104098839 CHEMBL463207 DB04829 C07542 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 50363788 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 50241702 [N-methyl-3H]LSD::CHEMBL463207::lsd 5-hydroxytryptamine receptor 2A Homo sapiens 21.17 ChEMBL 10.1021/np0601760 10.7270/Q2H9950V 17067154 Hedner, E; Sjogren, M; Frandberg, PA; Johansson, T; Goransson, U; Dahlstrom, M; Jonsson, P; Nyberg, F; Bohlin, L 10/27/2006 1/11/2010 Uppsala University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50241702 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=687&target=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50241702&enzyme=5-hydroxytryptamine+receptor+2A&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 104098839 CHEMBL463207 DB04829 C07542 1 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEATLCVSDLGTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYTGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENKKPLQLILVNTIPALAYKSSQLQMGQKKNSKQDAKTTDNDCSMVALGKQHSEEASKDNSDGVNEKVSCV 9LLB,9LLA,9LL9,9LL8,9LL7,9ASA,9AS9,9AS8,9AS7,9AS6,9AS5,9AS4,9AS3,9AS2,9AS1,9AS0,9ARZ,9ARY,9ARX,6WHA,8V6U,8UWL,7RAN 5-hydroxytryptamine receptor 2A 5HT2A_HUMAN P28223 B2RAC5 B4DZ79 F5GWE8 Q5T8C0 50666230 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD Serotonin 2 (5-HT2) receptor Rattus norvegicus 2.5 ChEMBL 10.1021/jm00082a014 10.7270/Q29K4BV4 1542100 Glennon, RA; Raghupathi, R; Bartyzel, P; Teitler, M; Leonhardt, S 4/3/1992 10/24/2012 Virginia Commonwealth University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000484&target=Serotonin+2+%285-HT2%29+receptor&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=Serotonin+2+%285-HT2%29+receptor&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 3 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 MVNLGNAVRSLLMHLIGLLVWQFDISISPVAAIVTDTFNSSDGGRLFQFPDGVQNWPALSIVVIIIMTIGGNILVIMAVSMEKKLHNATNYFLMSLAIADMLVGLLVMPLSLLAILYDYVWPLPRYLCPVWISLDVLFSTASIMHLCAISLDRYVAIRNPIEHSRFNSRTKAIMKIAIVWAISIGVSVPIPVIGLRDESKVFVNNTTCVLNDPNFVLIGSFVAFFIPLTIMVITYFLTIYVLRRQTLMLLRGHTEEELANMSLNFLNCCCKKNGGEEENAPNPNPDQKPRRKKKEKRPRGTMQAINNEKKASKVLGIVFFVFLIMWCPFFITNILSVLCGKACNQKLMEKLLNVFVWIGYVCSGINPLVYTLFNKIYRRAFSKYLRCDYKPDKKPPVRQIPRVAATALSGRELNVNIYRHTNERVARKANDPEPGIEMQVENLELPVNPSNVVSERISSV 5-hydroxytryptamine receptor 2C 5HT2C_RAT P08909 MASSYKMSEQSTISEHILQKTCDHLILTDRSGLKAESAAEEMKQTAENQGNTVHWAALLIFAVIIPTIGGNILVILAVSLEKRLQYATNYFLMSLAVADLLVGLFVMPIALLTIMFEATWPLPLALCPAWLFLDVLFSTASIMHLCAISLDRYIAIKKPIQANQCNSRTTAFVKITVVWLISIGIAIPVPIKGIEADVVNAHNITCELTKDRFGSFMLFGSLAAFFAPLTIMIVTYFLTIHALRKKAYLVRNRPPQRLTRWTVSTVLQREDSSFSSPEKMVMLDGSHKDKILPNSTDETLMRRMSSAGKKPAQTISNEQRASKVLGIVFLFFLLMWCPFFITNVTLALCDSCNQTTLKTLLQIFVWVGYVSSGVNPLIYTLFNKTFREAFGRYITCNYQATKSVKVLRKCSSTLYFGNSMVENSKFFTKHGIRNGINPAMYQSPVRLRSSTIQSSSIILLNTFLTENDGDKVEDQVSYI 5-hydroxytryptamine receptor 2B 5HT2B_RAT P30994 Q9QW44 51148412 CCN(CC)C(=O)[C@@H]1C=C2c3cccc4[nH]cc(c34)C[C@H]2N(C)C1 InChI=1S/C20H25N3O/c1-4-23(5-2)20(24)14-9-16-15-7-6-8-17-19(15)13(11-21-17)10-18(16)22(3)12-14/h6-9,11,14,18,21H,4-5,10,12H2,1-3H3 VAYOSLLFUXYJDT-UHFFFAOYSA-N 21342 (4R,7R)-N,N-diethyl-6-methyl-6,11-diazatetracyclo[7.6.1.0^{2,7}.0^{12,16}]hexadeca-1(16),2,9,12,14-pentaene-4-carboxamide::Lysergic Acid Diethylamide Tartrate::LSD::CHEMBL263881::LSD,(+)::LSD,l-::Lysergic Acid Diethylamide::d-Isolysergic acid amide::LSD 25::[3H]-LSD::US20240166618, Compound LSD::US20240368151, Compound LSD Serotonin 2 (5-HT2) receptor Rattus norvegicus 6.3 ChEMBL 10.1021/jm00018a019 10.7270/Q2PC3535 7658446 Oberlender, R; Ramachandran, PV; Johnson, MP; Huang, X; Nichols, DE 9/1/1995 8/21/2020 Purdue University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=21342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000484&target=Serotonin+2+%285-HT2%29+receptor&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=21342&enzyme=Serotonin+2+%285-HT2%29+receptor&column=ki&startPg=0&Increment=50&submit=Search 7LD 5TVN,6WGT,7SRQ,7SRR,7SRS,7WC6,8FYT,8JXR,8ZSP,9AS3,9AS4,9BS9,9BSB 5761 49689414 CHEMBL263881 DB04829 C07542 3 MEILCEDNISLSSIPNSLMQLGDGPRLYHNDFNSRDANTSEASNWTIDAENRTNLSCEGYLPPTCLSILHLQEKNWSALLTTVVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAIWIYLDVLFSTASIMHLCAISLDRYVAIQNPIHHSRFNSRTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIGSFVAFFIPLTIMVITYFLTIKSLQKEATLCVSDLSTRAKLASFSFLPQSSLSSEKLFQRSIHREPGSYAGRRTMQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVICKESCNENVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKENRKPLQLILVNTIPALAYKSSQLQVGQKKNSQEDAEQTVDDCSMVTLGKQQSEENCTDNIETVNEKVSCV 5-hydroxytryptamine receptor 2A 5HT2A_RAT P14842 MVNLGNAVRSLLMHLIGLLVWQFDISISPVAAIVTDTFNSSDGGRLFQFPDGVQNWPALSIVVIIIMTIGGNILVIMAVSMEKKLHNATNYFLMSLAIADMLVGLLVMPLSLLAILYDYVWPLPRYLCPVWISLDVLFSTASIMHLCAISLDRYVAIRNPIEHSRFNSRTKAIMKIAIVWAISIGVSVPIPVIGLRDESKVFVNNTTCVLNDPNFVLIGSFVAFFIPLTIMVITYFLTIYVLRRQTLMLLRGHTEEELANMSLNFLNCCCKKNGGEEENAPNPNPDQKPRRKKKEKRPRGTMQAINNEKKASKVLGIVFFVFLIMWCPFFITNILSVLCGKACNQKLMEKLLNVFVWIGYVCSGINPLVYTLFNKIYRRAFSKYLRCDYKPDKKPPVRQIPRVAATALSGRELNVNIYRHTNERVARKANDPEPGIEMQVENLELPVNPSNVVSERISSV 5-hydroxytryptamine receptor 2C 5HT2C_RAT P08909 MASSYKMSEQSTISEHILQKTCDHLILTDRSGLKAESAAEEMKQTAENQGNTVHWAALLIFAVIIPTIGGNILVILAVSLEKRLQYATNYFLMSLAVADLLVGLFVMPIALLTIMFEATWPLPLALCPAWLFLDVLFSTASIMHLCAISLDRYIAIKKPIQANQCNSRTTAFVKITVVWLISIGIAIPVPIKGIEADVVNAHNITCELTKDRFGSFMLFGSLAAFFAPLTIMIVTYFLTIHALRKKAYLVRNRPPQRLTRWTVSTVLQREDSSFSSPEKMVMLDGSHKDKILPNSTDETLMRRMSSAGKKPAQTISNEQRASKVLGIVFLFFLLMWCPFFITNVTLALCDSCNQTTLKTLLQIFVWVGYVSSGVNPLIYTLFNKTFREAFGRYITCNYQATKSVKVLRKCSSTLYFGNSMVENSKFFTKHGIRNGINPAMYQSPVRLRSSTIQSSSIILLNTFLTENDGDKVEDQVSYI 5-hydroxytryptamine receptor 2B 5HT2B_RAT P30994 Q9QW44 174420 Cc1cc2c(cc1Cl)N(CC2)C(=O)Nc3ccc(nc3)Oc4cccnc4C InChI=1S/C21H19ClN4O2/c1-13-10-15-7-9-26(18(15)11-17(13)22)21(27)25-16-5-6-20(24-12-16)28-19-4-3-8-23-14(19)2/h3-6,8,10-12H,7,9H2,1-2H3,(H,25,27) GIUZEIJUFOPTMR-UHFFFAOYSA-N 85097 CAS_181632-25-7::CHEMBL14563::SB 242084 5-hydroxytryptamine receptor 2C Homo sapiens 1 PDSP Ki 10.1016/s0028-3908(97)00038-5 10.7270/Q2SN07GG 9225286 Kennett, GA; Wood, MD; Bright, F; Trail, B; Riley, G; Holland, V; Avenell, KY; Stean, T; Upton, N; Bromidge, S; Forbes, IT; Brown, AM; Middlemiss, DN; Blackburn, TP 12/28/1997 2/26/2012 Smithkline Beecham Pharmaceuticals http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=85097 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3430&target=5-hydroxytryptamine+receptor+2C&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=85097&enzyme=5-hydroxytryptamine+receptor+2C&column=ki&startPg=0&Increment=50&submit=Search A1L83 9UGL 3644637 136351197 CHEMBL14563 1 MVNLRNAVHSFLVHLIGLLVWQSDISVSPVAAIVTDIFNTSDGGRFKFPDGVQNWPALSIVIIIIMTIGGNILVIMAVSMEKKLHNATNYFLMSLAIADMLVGLLVMPLSLLAILYDYVWPLPRYLCPVWISLDVLFSTASIMHLCAISLDRYVAIRNPIEHSRFNSRTKAIMKIAIVWAISIGVSVPIPVIGLRDEEKVFVNNTTCVLNDPNFVLIGSFVAFFIPLTIMVITYCLTIYVLRRQALMLLHGHTEEPPGLSLDFLKCCKRNTAEEENSANPNQDQNARRRKKKERRPRGTMQAINNERKASKVLGIVFFVFLIMWCPFFITNILSVLCEKSCNQKLMEKLLNVFVWIGYVCSGINPLVYTLFNKIYRRAFSNYLRCNYKVEKKPPVRQIPRVAATALSGRELNVNIYRHTNEPVIEKASDNEPGIEMQVENLELPVNPSSVVSERISSV 8DPI,8DPH,9UGL 5-hydroxytryptamine receptor 2C 5HT2C_HUMAN P28335 B1AMW4 Q5VUF8 Q9NP28 182896 Cc1cc2c(cc1Cl)N(CC2)C(=O)Nc3ccc(nc3)Oc4cccnc4C InChI=1S/C21H19ClN4O2/c1-13-10-15-7-9-26(18(15)11-17(13)22)21(27)25-16-5-6-20(24-12-16)28-19-4-3-8-23-14(19)2/h3-6,8,10-12H,7,9H2,1-2H3,(H,25,27) GIUZEIJUFOPTMR-UHFFFAOYSA-N 85097 CAS_181632-25-7::CHEMBL14563::SB 242084 5-hydroxytryptamine receptor 2C Homo sapiens 0.48 PDSP Ki 10.1007/s00210-001-0505-y 10.7270/Q2W37TWZ 11882920 Cussac, D; Newman-Tancredi, A; Quentric, Y; Carpentier, N; Poissonnet, G; Parmentier, JG; Goldstein, S; Millan, MJ 12/28/2002 5/3/2012 Institut De Recherches Servier http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=85097 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3430&target=5-hydroxytryptamine+receptor+2C&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=85097&enzyme=5-hydroxytryptamine+receptor+2C&column=ki&startPg=0&Increment=50&submit=Search A1L83 9UGL 3644637 136351197 CHEMBL14563 1 MVNLRNAVHSFLVHLIGLLVWQSDISVSPVAAIVTDIFNTSDGGRFKFPDGVQNWPALSIVIIIIMTIGGNILVIMAVSMEKKLHNATNYFLMSLAIADMLVGLLVMPLSLLAILYDYVWPLPRYLCPVWISLDVLFSTASIMHLCAISLDRYVAIRNPIEHSRFNSRTKAIMKIAIVWAISIGVSVPIPVIGLRDEEKVFVNNTTCVLNDPNFVLIGSFVAFFIPLTIMVITYCLTIYVLRRQALMLLHGHTEEPPGLSLDFLKCCKRNTAEEENSANPNQDQNARRRKKKERRPRGTMQAINNERKASKVLGIVFFVFLIMWCPFFITNILSVLCEKSCNQKLMEKLLNVFVWIGYVCSGINPLVYTLFNKIYRRAFSNYLRCNYKVEKKPPVRQIPRVAATALSGRELNVNIYRHTNEPVIEKASDNEPGIEMQVENLELPVNPSSVVSERISSV 8DPI,8DPH,9UGL 5-hydroxytryptamine receptor 2C 5HT2C_HUMAN P28335 B1AMW4 Q5VUF8 Q9NP28 188253 Cc1cc2c(cc1Cl)N(CC2)C(=O)Nc3ccc(nc3)Oc4cccnc4C InChI=1S/C21H19ClN4O2/c1-13-10-15-7-9-26(18(15)11-17(13)22)21(27)25-16-5-6-20(24-12-16)28-19-4-3-8-23-14(19)2/h3-6,8,10-12H,7,9H2,1-2H3,(H,25,27) GIUZEIJUFOPTMR-UHFFFAOYSA-N 85097 CAS_181632-25-7::CHEMBL14563::SB 242084 5-hydroxytryptamine receptor 2C Homo sapiens 7.08 PDSP Ki 10.1007/s00210-004-0951-4 10.7270/Q2M32TBD 15322733 Knight, AR; Misra, A; Quirk, K; Benwell, K; Revell, D; Kennett, G; Bickerdike, M 12/28/2004 5/31/2012 Vernalis Research http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=85097 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3430&target=5-hydroxytryptamine+receptor+2C&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=85097&enzyme=5-hydroxytryptamine+receptor+2C&column=ki&startPg=0&Increment=50&submit=Search A1L83 9UGL 3644637 136351197 CHEMBL14563 1 MVNLRNAVHSFLVHLIGLLVWQSDISVSPVAAIVTDIFNTSDGGRFKFPDGVQNWPALSIVIIIIMTIGGNILVIMAVSMEKKLHNATNYFLMSLAIADMLVGLLVMPLSLLAILYDYVWPLPRYLCPVWISLDVLFSTASIMHLCAISLDRYVAIRNPIEHSRFNSRTKAIMKIAIVWAISIGVSVPIPVIGLRDEEKVFVNNTTCVLNDPNFVLIGSFVAFFIPLTIMVITYCLTIYVLRRQALMLLHGHTEEPPGLSLDFLKCCKRNTAEEENSANPNQDQNARRRKKKERRPRGTMQAINNERKASKVLGIVFFVFLIMWCPFFITNILSVLCEKSCNQKLMEKLLNVFVWIGYVCSGINPLVYTLFNKIYRRAFSNYLRCNYKVEKKPPVRQIPRVAATALSGRELNVNIYRHTNEPVIEKASDNEPGIEMQVENLELPVNPSSVVSERISSV 8DPI,8DPH,9UGL 5-hydroxytryptamine receptor 2C 5HT2C_HUMAN P28335 B1AMW4 Q5VUF8 Q9NP28 50064296 Cc1cc2c(cc1Cl)N(CC2)C(=O)Nc3ccc(nc3)Oc4cccnc4C InChI=1S/C21H19ClN4O2/c1-13-10-15-7-9-26(18(15)11-17(13)22)21(27)25-16-5-6-20(24-12-16)28-19-4-3-8-23-14(19)2/h3-6,8,10-12H,7,9H2,1-2H3,(H,25,27) GIUZEIJUFOPTMR-UHFFFAOYSA-N 85097 CAS_181632-25-7::CHEMBL14563::SB 242084 5-hydroxytryptamine receptor 2C Homo sapiens 1 ChEMBL 10.1021/jm990388c 10.7270/Q23X85V5 10737744 Bromidge, SM; Dabbs, S; Davies, DT; Davies, S; Duckworth, DM; Forbes, IT; Gaster, LM; Ham, P; Jones, GE; King, FD; Mulholland, KR; Saunders, DV; Wyman, PA; Blaney, FE; Clarke, SE; Blackburn, TP; Holland, V; Kennett, GA; Lightowler, S; Middlemiss, DN; Trail, B; Riley, GJ; Wood, MD 4/13/2000 11/10/2009 Smithkline Beecham Pharmaceuticals http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=85097 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3430&target=5-hydroxytryptamine+receptor+2C&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=85097&enzyme=5-hydroxytryptamine+receptor+2C&column=ki&startPg=0&Increment=50&submit=Search A1L83 9UGL 3644637 136351197 CHEMBL14563 1 MVNLRNAVHSFLVHLIGLLVWQSDISVSPVAAIVTDIFNTSDGGRFKFPDGVQNWPALSIVIIIIMTIGGNILVIMAVSMEKKLHNATNYFLMSLAIADMLVGLLVMPLSLLAILYDYVWPLPRYLCPVWISLDVLFSTASIMHLCAISLDRYVAIRNPIEHSRFNSRTKAIMKIAIVWAISIGVSVPIPVIGLRDEEKVFVNNTTCVLNDPNFVLIGSFVAFFIPLTIMVITYCLTIYVLRRQALMLLHGHTEEPPGLSLDFLKCCKRNTAEEENSANPNQDQNARRRKKKERRPRGTMQAINNERKASKVLGIVFFVFLIMWCPFFITNILSVLCEKSCNQKLMEKLLNVFVWIGYVCSGINPLVYTLFNKIYRRAFSNYLRCNYKVEKKPPVRQIPRVAATALSGRELNVNIYRHTNEPVIEKASDNEPGIEMQVENLELPVNPSSVVSERISSV 8DPI,8DPH,9UGL 5-hydroxytryptamine receptor 2C 5HT2C_HUMAN P28335 B1AMW4 Q5VUF8 Q9NP28 50456874 Cc1cc2c(cc1Cl)N(CC2)C(=O)Nc3ccc(nc3)Oc4cccnc4C InChI=1S/C21H19ClN4O2/c1-13-10-15-7-9-26(18(15)11-17(13)22)21(27)25-16-5-6-20(24-12-16)28-19-4-3-8-23-14(19)2/h3-6,8,10-12H,7,9H2,1-2H3,(H,25,27) GIUZEIJUFOPTMR-UHFFFAOYSA-N 85097 CAS_181632-25-7::CHEMBL14563::SB 242084 5-hydroxytryptamine receptor 2C Rattus norvegicus 0.160000 ChEMBL 10.1016/j.bmcl.2015.12.071 10.7270/Q2VX0JC7 26748694 Éliás, O; Nógrádi, K; Domány, G; Szakács, Z; Kóti, J; Szántay, C; Tarcsay, Á; Keseru, GM; Gere, A; Kiss, B; Kurkó, D; Kolok, S; Némethy, Z; Kapui, Z; Hellinger, É; Vastag, M; Sághy, K; Kedves, R; Gyertyán, I 1/25/2016 6/3/2017 Gedeon Richter http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=85097 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=7150&target=5-hydroxytryptamine+receptor+2C&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=85097&enzyme=5-hydroxytryptamine+receptor+2C&column=ki&startPg=0&Increment=50&submit=Search A1L83 9UGL 3644637 136351197 CHEMBL14563 1 MVNLGNAVRSLLMHLIGLLVWQFDISISPVAAIVTDTFNSSDGGRLFQFPDGVQNWPALSIVVIIIMTIGGNILVIMAVSMEKKLHNATNYFLMSLAIADMLVGLLVMPLSLLAILYDYVWPLPRYLCPVWISLDVLFSTASIMHLCAISLDRYVAIRNPIEHSRFNSRTKAIMKIAIVWAISIGVSVPIPVIGLRDESKVFVNNTTCVLNDPNFVLIGSFVAFFIPLTIMVITYFLTIYVLRRQTLMLLRGHTEEELANMSLNFLNCCCKKNGGEEENAPNPNPDQKPRRKKKEKRPRGTMQAINNEKKASKVLGIVFFVFLIMWCPFFITNILSVLCGKACNQKLMEKLLNVFVWIGYVCSGINPLVYTLFNKIYRRAFSKYLRCDYKPDKKPPVRQIPRVAATALSGRELNVNIYRHTNERVARKANDPEPGIEMQVENLELPVNPSNVVSERISSV 5-hydroxytryptamine receptor 2C 5HT2C_RAT P08909 50580462 Cc1cc2c(cc1Cl)N(CC2)C(=O)Nc3ccc(nc3)Oc4cccnc4C InChI=1S/C21H19ClN4O2/c1-13-10-15-7-9-26(18(15)11-17(13)22)21(27)25-16-5-6-20(24-12-16)28-19-4-3-8-23-14(19)2/h3-6,8,10-12H,7,9H2,1-2H3,(H,25,27) GIUZEIJUFOPTMR-UHFFFAOYSA-N 85097 CAS_181632-25-7::CHEMBL14563::SB 242084 5-hydroxytryptamine receptor 2C Homo sapiens 1 ChEMBL 10.1016/s0960-894x(00)00364-4 10.7270/Q2X63Q4P 10969986 Bromidge, SM; Dabbs, S; Davies, S; Duckworth, DM; Forbes, IT; Jones, GE; Jones, J; King, FD; Saunders, DV; Blackburn, TP; Holland, V; Kennett, GA; Lightowler, S; Middlemiss, DN; Riley, GJ; Trail, B; Wood, MD 8/21/2000 10/22/2018 Smithkline Beecham Pharmaceuticals http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=85097 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3430&target=5-hydroxytryptamine+receptor+2C&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=85097&enzyme=5-hydroxytryptamine+receptor+2C&column=ki&startPg=0&Increment=50&submit=Search A1L83 9UGL 3644637 136351197 CHEMBL14563 1 MVNLRNAVHSFLVHLIGLLVWQSDISVSPVAAIVTDIFNTSDGGRFKFPDGVQNWPALSIVIIIIMTIGGNILVIMAVSMEKKLHNATNYFLMSLAIADMLVGLLVMPLSLLAILYDYVWPLPRYLCPVWISLDVLFSTASIMHLCAISLDRYVAIRNPIEHSRFNSRTKAIMKIAIVWAISIGVSVPIPVIGLRDEEKVFVNNTTCVLNDPNFVLIGSFVAFFIPLTIMVITYCLTIYVLRRQALMLLHGHTEEPPGLSLDFLKCCKRNTAEEENSANPNQDQNARRRKKKERRPRGTMQAINNERKASKVLGIVFFVFLIMWCPFFITNILSVLCEKSCNQKLMEKLLNVFVWIGYVCSGINPLVYTLFNKIYRRAFSNYLRCNYKVEKKPPVRQIPRVAATALSGRELNVNIYRHTNEPVIEKASDNEPGIEMQVENLELPVNPSSVVSERISSV 8DPI,8DPH,9UGL 5-hydroxytryptamine receptor 2C 5HT2C_HUMAN P28335 B1AMW4 Q5VUF8 Q9NP28 51001569 Cc1cc2c(cc1Cl)N(CC2)C(=O)Nc3ccc(nc3)Oc4cccnc4C InChI=1S/C21H19ClN4O2/c1-13-10-15-7-9-26(18(15)11-17(13)22)21(27)25-16-5-6-20(24-12-16)28-19-4-3-8-23-14(19)2/h3-6,8,10-12H,7,9H2,1-2H3,(H,25,27) GIUZEIJUFOPTMR-UHFFFAOYSA-N 85097 CAS_181632-25-7::CHEMBL14563::SB 242084 5-hydroxytryptamine receptor 2C Homo sapiens 1 ChEMBL 10.1016/j.bmcl.2005.08.004 10.7270/Q2Z89DNZ 16168649 Goodacre, CJ; Bromidge, SM; Clapham, D; King, FD; Lovell, PJ; Allen, M; Campbell, LP; Holland, V; Riley, GJ; Starr, KR; Trail, BK; Wood, MD 10/5/2005 5/20/2013 Glaxosmithkline http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=85097 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3430&target=5-hydroxytryptamine+receptor+2C&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=85097&enzyme=5-hydroxytryptamine+receptor+2C&column=ki&startPg=0&Increment=50&submit=Search A1L83 9UGL 3644637 136351197 CHEMBL14563 1 MVNLRNAVHSFLVHLIGLLVWQSDISVSPVAAIVTDIFNTSDGGRFKFPDGVQNWPALSIVIIIIMTIGGNILVIMAVSMEKKLHNATNYFLMSLAIADMLVGLLVMPLSLLAILYDYVWPLPRYLCPVWISLDVLFSTASIMHLCAISLDRYVAIRNPIEHSRFNSRTKAIMKIAIVWAISIGVSVPIPVIGLRDEEKVFVNNTTCVLNDPNFVLIGSFVAFFIPLTIMVITYCLTIYVLRRQALMLLHGHTEEPPGLSLDFLKCCKRNTAEEENSANPNQDQNARRRKKKERRPRGTMQAINNERKASKVLGIVFFVFLIMWCPFFITNILSVLCEKSCNQKLMEKLLNVFVWIGYVCSGINPLVYTLFNKIYRRAFSNYLRCNYKVEKKPPVRQIPRVAATALSGRELNVNIYRHTNEPVIEKASDNEPGIEMQVENLELPVNPSSVVSERISSV 8DPI,8DPH,9UGL 5-hydroxytryptamine receptor 2C 5HT2C_HUMAN P28335 B1AMW4 Q5VUF8 Q9NP28 51344352 Cc1cc2c(cc1Cl)N(CC2)C(=O)Nc3ccc(nc3)Oc4cccnc4C InChI=1S/C21H19ClN4O2/c1-13-10-15-7-9-26(18(15)11-17(13)22)21(27)25-16-5-6-20(24-12-16)28-19-4-3-8-23-14(19)2/h3-6,8,10-12H,7,9H2,1-2H3,(H,25,27) GIUZEIJUFOPTMR-UHFFFAOYSA-N 85097 CAS_181632-25-7::CHEMBL14563::SB 242084 5-hydroxytryptamine receptor 2C Homo sapiens 0.330000 ChEMBL 10.1016/j.bmcl.2020.127358 10.7270/Q26113XJ 32631554 Evans, CA; Zuluaga, A; Vasquez Matute, D; Baradaran-Noviri, S; Perez-Cervantes, N; Siegler, MA 8/15/2020 8/13/2021 Dominican College http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=85097 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3430&target=5-hydroxytryptamine+receptor+2C&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=85097&enzyme=5-hydroxytryptamine+receptor+2C&column=ki&startPg=0&Increment=50&submit=Search A1L83 9UGL 3644637 136351197 CHEMBL14563 1 MVNLRNAVHSFLVHLIGLLVWQSDISVSPVAAIVTDIFNTSDGGRFKFPDGVQNWPALSIVIIIIMTIGGNILVIMAVSMEKKLHNATNYFLMSLAIADMLVGLLVMPLSLLAILYDYVWPLPRYLCPVWISLDVLFSTASIMHLCAISLDRYVAIRNPIEHSRFNSRTKAIMKIAIVWAISIGVSVPIPVIGLRDEEKVFVNNTTCVLNDPNFVLIGSFVAFFIPLTIMVITYCLTIYVLRRQALMLLHGHTEEPPGLSLDFLKCCKRNTAEEENSANPNQDQNARRRKKKERRPRGTMQAINNERKASKVLGIVFFVFLIMWCPFFITNILSVLCEKSCNQKLMEKLLNVFVWIGYVCSGINPLVYTLFNKIYRRAFSNYLRCNYKVEKKPPVRQIPRVAATALSGRELNVNIYRHTNEPVIEKASDNEPGIEMQVENLELPVNPSSVVSERISSV 8DPI,8DPH,9UGL 5-hydroxytryptamine receptor 2C 5HT2C_HUMAN P28335 B1AMW4 Q5VUF8 Q9NP28 50221370 Cc1ccc(c(c1)C)Sc2ccccc2N3CCNCC3 InChI=1S/C18H22N2S/c1-14-7-8-17(15(2)13-14)21-18-6-4-3-5-16(18)20-11-9-19-10-12-20/h3-8,13,19H,9-12H2,1-2H3 YQNWZWMKLDQSAC-UHFFFAOYSA-N 50400902 CHEMBL2204360::vortioxetine hydrobromide::1-(2-(2,4-dimethylphenylsulfanyl)phenyl)piperazine::brintellix::Lu-AA21004::Trintellix 5-hydroxytryptamine receptor 3A Homo sapiens 23 ChEMBL 10.1021/jm101459g 10.7270/Q2W37XFC 21486038 Bang-Andersen, B; Ruhland, T; Jorgensen, M; Smith, G; Frederiksen, K; Jensen, KG; Zhong, H; Nielsen, SM; Hogg, S; Mork, A; Stensbol, TB 5/5/2011 5/17/2013 H. Lundbeck http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50400902 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5137&target=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50400902&enzyme=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search VTX 8AW2,8BLA,8BLB 9966051 163349926 CHEMBL2204360 1 MLLWVQQALLALLLPTLLAQGEARRSRNTTRPALLRLSDYLLTNYRKGVRPVRDWRKPTTVSIDVIVYAILNVDEKNQVLTTYIWYRQYWTDEFLQWNPEDFDNITKLSIPTDSIWVPDILINEFVDVGKSPNIPYVYIRHQGEVQNYKPLQVVTACSLDIYNFPFDVQNCSLTFTSWLHTIQDINISLWRLPEKVKSDRSVFMNQGEWELLGVLPYFREFSMESSNYYAEMKFYVVIRRRPLFYVVSLLLPSIFLMVMDIVGFYLPPNSGERVSFKITLLLGYSVFLIIVSDTLPATAIGTPLIGVYFVVCMALLVISLAETIFIVRLVHKQDLQQPVPAWLRHLVLERIAWLLCLREQSTSQRPPATSQATKTDDCSAMGNHCSHMGGPQDFEKSPRDRCSPPPPPREASLAVCGLLQELSSIRQFLEKRDEIREVARDWLRVGSVLDKLLFHIYLLAVLAYSITLVMLWSIWQYA 8BLB,4PIR,8C21,8C20,8C1Z,8C1W,6Y5B,6Y5A,6Y59,8BLA,8BL8 5-hydroxytryptamine receptor 3A 5HT3A_HUMAN P46098 B4DSY6 G5E986 O60854 Q7KZM7 Q99918 Q9BSZ9 50221372 Cc1ccc(c(c1)C)Sc2ccccc2N3CCNCC3 InChI=1S/C18H22N2S/c1-14-7-8-17(15(2)13-14)21-18-6-4-3-5-16(18)20-11-9-19-10-12-20/h3-8,13,19H,9-12H2,1-2H3 YQNWZWMKLDQSAC-UHFFFAOYSA-N 50400902 CHEMBL2204360::vortioxetine hydrobromide::1-(2-(2,4-dimethylphenylsulfanyl)phenyl)piperazine::brintellix::Lu-AA21004::Trintellix 5-hydroxytryptamine receptor 3A Rattus norvegicus 230 ChEMBL 10.1021/jm101459g 10.7270/Q2W37XFC 21486038 Bang-Andersen, B; Ruhland, T; Jorgensen, M; Smith, G; Frederiksen, K; Jensen, KG; Zhong, H; Nielsen, SM; Hogg, S; Mork, A; Stensbol, TB 5/5/2011 5/17/2013 H. Lundbeck http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50400902 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=49000077&target=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50400902&enzyme=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search VTX 8AW2,8BLA,8BLB 9966051 163349926 CHEMBL2204360 1 MPLCIPQVLLALFLSVLIAQGEGSRRRATQAHSTTQPALLRLSDHLLANYKKGVRPVRDWRKPTLVSIDVIMYAILNVDEKNQVLTTYIWYRQFWTDEFLQWTPEDFDNVTKLSIPTDSIWVPDILINEFVDVGKSPSIPYVYVHHQGEVQNYKPLQLVTACSLDIYNFPFDVQNCSLTFTSWLHTIQDINISLWRTPEEVRSDKSIFINQGEWELLGVFTKFQEFSIETSNSYAEMKFYVVIRRRPLFYAVSLLLPSIFLMVVDIVGFCLPPDSGERVSFKITLLLGYSVFLIIVSDTLPATAIGTPLIGVYFVVCMALLVISLAETIFIVQLVHKQDLQRPVPDWLRHLVLDRIAWLLCLGEQPMAHRPPATFQANKTDDCSAMGNHCSHVGSPQDLEKTSRSRDSPLPPPREASLAVRGLLQELSSIRHSLEKRDEMREVARDWLRVGYVLDRLLFRIYLLAVLAYSITLVTLWSIWHYS 8CC7,8CC6,6Y1Z 5-hydroxytryptamine receptor 3A 5HT3A_RAT P35563 50221382 Cc1ccc(c(c1)C)Sc2ccccc2N3CCNCC3 InChI=1S/C18H22N2S/c1-14-7-8-17(15(2)13-14)21-18-6-4-3-5-16(18)20-11-9-19-10-12-20/h3-8,13,19H,9-12H2,1-2H3 YQNWZWMKLDQSAC-UHFFFAOYSA-N 50400902 CHEMBL2204360::vortioxetine hydrobromide::1-(2-(2,4-dimethylphenylsulfanyl)phenyl)piperazine::brintellix::Lu-AA21004::Trintellix 5-hydroxytryptamine receptor 3A Homo sapiens 12 ChEMBL 10.1021/jm101459g 10.7270/Q2W37XFC 21486038 Bang-Andersen, B; Ruhland, T; Jorgensen, M; Smith, G; Frederiksen, K; Jensen, KG; Zhong, H; Nielsen, SM; Hogg, S; Mork, A; Stensbol, TB 5/5/2011 5/17/2013 H. Lundbeck http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50400902 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5137&target=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50400902&enzyme=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search VTX 8AW2,8BLA,8BLB 9966051 163349926 CHEMBL2204360 1 MLLWVQQALLALLLPTLLAQGEARRSRNTTRPALLRLSDYLLTNYRKGVRPVRDWRKPTTVSIDVIVYAILNVDEKNQVLTTYIWYRQYWTDEFLQWNPEDFDNITKLSIPTDSIWVPDILINEFVDVGKSPNIPYVYIRHQGEVQNYKPLQVVTACSLDIYNFPFDVQNCSLTFTSWLHTIQDINISLWRLPEKVKSDRSVFMNQGEWELLGVLPYFREFSMESSNYYAEMKFYVVIRRRPLFYVVSLLLPSIFLMVMDIVGFYLPPNSGERVSFKITLLLGYSVFLIIVSDTLPATAIGTPLIGVYFVVCMALLVISLAETIFIVRLVHKQDLQQPVPAWLRHLVLERIAWLLCLREQSTSQRPPATSQATKTDDCSAMGNHCSHMGGPQDFEKSPRDRCSPPPPPREASLAVCGLLQELSSIRQFLEKRDEIREVARDWLRVGSVLDKLLFHIYLLAVLAYSITLVMLWSIWQYA 8BLB,4PIR,8C21,8C20,8C1Z,8C1W,6Y5B,6Y5A,6Y59,8BLA,8BL8 5-hydroxytryptamine receptor 3A 5HT3A_HUMAN P46098 B4DSY6 G5E986 O60854 Q7KZM7 Q99918 Q9BSZ9 50221383 Cc1ccc(c(c1)C)Sc2ccccc2N3CCNCC3 InChI=1S/C18H22N2S/c1-14-7-8-17(15(2)13-14)21-18-6-4-3-5-16(18)20-11-9-19-10-12-20/h3-8,13,19H,9-12H2,1-2H3 YQNWZWMKLDQSAC-UHFFFAOYSA-N 50400902 CHEMBL2204360::vortioxetine hydrobromide::1-(2-(2,4-dimethylphenylsulfanyl)phenyl)piperazine::brintellix::Lu-AA21004::Trintellix 5-hydroxytryptamine receptor 3A Homo sapiens 2100 ChEMBL 10.1021/jm101459g 10.7270/Q2W37XFC 21486038 Bang-Andersen, B; Ruhland, T; Jorgensen, M; Smith, G; Frederiksen, K; Jensen, KG; Zhong, H; Nielsen, SM; Hogg, S; Mork, A; Stensbol, TB 5/5/2011 5/17/2013 H. Lundbeck http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50400902 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5137&target=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50400902&enzyme=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search VTX 8AW2,8BLA,8BLB 9966051 163349926 CHEMBL2204360 1 MLLWVQQALLALLLPTLLAQGEARRSRNTTRPALLRLSDYLLTNYRKGVRPVRDWRKPTTVSIDVIVYAILNVDEKNQVLTTYIWYRQYWTDEFLQWNPEDFDNITKLSIPTDSIWVPDILINEFVDVGKSPNIPYVYIRHQGEVQNYKPLQVVTACSLDIYNFPFDVQNCSLTFTSWLHTIQDINISLWRLPEKVKSDRSVFMNQGEWELLGVLPYFREFSMESSNYYAEMKFYVVIRRRPLFYVVSLLLPSIFLMVMDIVGFYLPPNSGERVSFKITLLLGYSVFLIIVSDTLPATAIGTPLIGVYFVVCMALLVISLAETIFIVRLVHKQDLQQPVPAWLRHLVLERIAWLLCLREQSTSQRPPATSQATKTDDCSAMGNHCSHMGGPQDFEKSPRDRCSPPPPPREASLAVCGLLQELSSIRQFLEKRDEIREVARDWLRVGSVLDKLLFHIYLLAVLAYSITLVMLWSIWQYA 8BLB,4PIR,8C21,8C20,8C1Z,8C1W,6Y5B,6Y5A,6Y59,8BLA,8BL8 5-hydroxytryptamine receptor 3A 5HT3A_HUMAN P46098 B4DSY6 G5E986 O60854 Q7KZM7 Q99918 Q9BSZ9 50977693 Cc1ccc(c(c1)C)Sc2ccccc2N3CCNCC3 InChI=1S/C18H22N2S/c1-14-7-8-17(15(2)13-14)21-18-6-4-3-5-16(18)20-11-9-19-10-12-20/h3-8,13,19H,9-12H2,1-2H3 YQNWZWMKLDQSAC-UHFFFAOYSA-N 50400902 CHEMBL2204360::vortioxetine hydrobromide::1-(2-(2,4-dimethylphenylsulfanyl)phenyl)piperazine::brintellix::Lu-AA21004::Trintellix 5-hydroxytryptamine receptor 3A Homo sapiens 3.7 ChEMBL 10.1021/jm101459g 10.7270/Q2W37XFC 21486038 Bang-Andersen, B; Ruhland, T; Jorgensen, M; Smith, G; Frederiksen, K; Jensen, KG; Zhong, H; Nielsen, SM; Hogg, S; Mork, A; Stensbol, TB 5/5/2011 5/17/2013 H. Lundbeck http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50400902 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5137&target=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50400902&enzyme=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search VTX 8AW2,8BLA,8BLB 9966051 163349926 CHEMBL2204360 1 MLLWVQQALLALLLPTLLAQGEARRSRNTTRPALLRLSDYLLTNYRKGVRPVRDWRKPTTVSIDVIVYAILNVDEKNQVLTTYIWYRQYWTDEFLQWNPEDFDNITKLSIPTDSIWVPDILINEFVDVGKSPNIPYVYIRHQGEVQNYKPLQVVTACSLDIYNFPFDVQNCSLTFTSWLHTIQDINISLWRLPEKVKSDRSVFMNQGEWELLGVLPYFREFSMESSNYYAEMKFYVVIRRRPLFYVVSLLLPSIFLMVMDIVGFYLPPNSGERVSFKITLLLGYSVFLIIVSDTLPATAIGTPLIGVYFVVCMALLVISLAETIFIVRLVHKQDLQQPVPAWLRHLVLERIAWLLCLREQSTSQRPPATSQATKTDDCSAMGNHCSHMGGPQDFEKSPRDRCSPPPPPREASLAVCGLLQELSSIRQFLEKRDEIREVARDWLRVGSVLDKLLFHIYLLAVLAYSITLVMLWSIWQYA 8BLB,4PIR,8C21,8C20,8C1Z,8C1W,6Y5B,6Y5A,6Y59,8BLA,8BL8 5-hydroxytryptamine receptor 3A 5HT3A_HUMAN P46098 B4DSY6 G5E986 O60854 Q7KZM7 Q99918 Q9BSZ9 50977706 Cc1ccc(c(c1)C)Sc2ccccc2N3CCNCC3 InChI=1S/C18H22N2S/c1-14-7-8-17(15(2)13-14)21-18-6-4-3-5-16(18)20-11-9-19-10-12-20/h3-8,13,19H,9-12H2,1-2H3 YQNWZWMKLDQSAC-UHFFFAOYSA-N 50400902 CHEMBL2204360::vortioxetine hydrobromide::1-(2-(2,4-dimethylphenylsulfanyl)phenyl)piperazine::brintellix::Lu-AA21004::Trintellix 5-hydroxytryptamine receptor 3A Rattus norvegicus 0.180000 ChEMBL 10.1021/jm101459g 10.7270/Q2W37XFC 21486038 Bang-Andersen, B; Ruhland, T; Jorgensen, M; Smith, G; Frederiksen, K; Jensen, KG; Zhong, H; Nielsen, SM; Hogg, S; Mork, A; Stensbol, TB 5/5/2011 5/17/2013 H. Lundbeck http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50400902 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=49000077&target=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50400902&enzyme=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search VTX 8AW2,8BLA,8BLB 9966051 163349926 CHEMBL2204360 1 MPLCIPQVLLALFLSVLIAQGEGSRRRATQAHSTTQPALLRLSDHLLANYKKGVRPVRDWRKPTLVSIDVIMYAILNVDEKNQVLTTYIWYRQFWTDEFLQWTPEDFDNVTKLSIPTDSIWVPDILINEFVDVGKSPSIPYVYVHHQGEVQNYKPLQLVTACSLDIYNFPFDVQNCSLTFTSWLHTIQDINISLWRTPEEVRSDKSIFINQGEWELLGVFTKFQEFSIETSNSYAEMKFYVVIRRRPLFYAVSLLLPSIFLMVVDIVGFCLPPDSGERVSFKITLLLGYSVFLIIVSDTLPATAIGTPLIGVYFVVCMALLVISLAETIFIVQLVHKQDLQRPVPDWLRHLVLDRIAWLLCLGEQPMAHRPPATFQANKTDDCSAMGNHCSHVGSPQDLEKTSRSRDSPLPPPREASLAVRGLLQELSSIRHSLEKRDEMREVARDWLRVGYVLDRLLFRIYLLAVLAYSITLVTLWSIWHYS 8CC7,8CC6,6Y1Z 5-hydroxytryptamine receptor 3A 5HT3A_RAT P35563 51505668 Cc1ccc(c(c1)C)Sc2ccccc2N3CCNCC3 InChI=1S/C18H22N2S/c1-14-7-8-17(15(2)13-14)21-18-6-4-3-5-16(18)20-11-9-19-10-12-20/h3-8,13,19H,9-12H2,1-2H3 YQNWZWMKLDQSAC-UHFFFAOYSA-N 50400902 CHEMBL2204360::vortioxetine hydrobromide::1-(2-(2,4-dimethylphenylsulfanyl)phenyl)piperazine::brintellix::Lu-AA21004::Trintellix 5-hydroxytryptamine receptor 3A Homo sapiens 3.7 ChEMBL 10.7270/Q2VQ36SJ 34311086 Kucwaj-Brysz, K; Baltrukevich, H; Czarnota, K; Handzlik, J 10/1/2021 6/26/2023 Jagiellonian University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50400902 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5137&target=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50400902&enzyme=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search VTX 8AW2,8BLA,8BLB 9966051 163349926 CHEMBL2204360 1 MLLWVQQALLALLLPTLLAQGEARRSRNTTRPALLRLSDYLLTNYRKGVRPVRDWRKPTTVSIDVIVYAILNVDEKNQVLTTYIWYRQYWTDEFLQWNPEDFDNITKLSIPTDSIWVPDILINEFVDVGKSPNIPYVYIRHQGEVQNYKPLQVVTACSLDIYNFPFDVQNCSLTFTSWLHTIQDINISLWRLPEKVKSDRSVFMNQGEWELLGVLPYFREFSMESSNYYAEMKFYVVIRRRPLFYVVSLLLPSIFLMVMDIVGFYLPPNSGERVSFKITLLLGYSVFLIIVSDTLPATAIGTPLIGVYFVVCMALLVISLAETIFIVRLVHKQDLQQPVPAWLRHLVLERIAWLLCLREQSTSQRPPATSQATKTDDCSAMGNHCSHMGGPQDFEKSPRDRCSPPPPPREASLAVCGLLQELSSIRQFLEKRDEIREVARDWLRVGSVLDKLLFHIYLLAVLAYSITLVMLWSIWQYA 8BLB,4PIR,8C21,8C20,8C1Z,8C1W,6Y5B,6Y5A,6Y59,8BLA,8BL8 5-hydroxytryptamine receptor 3A 5HT3A_HUMAN P46098 B4DSY6 G5E986 O60854 Q7KZM7 Q99918 Q9BSZ9 50221370 Cc1ccc(c(c1)C)Sc2ccccc2N3CCNCC3 InChI=1S/C18H22N2S/c1-14-7-8-17(15(2)13-14)21-18-6-4-3-5-16(18)20-11-9-19-10-12-20/h3-8,13,19H,9-12H2,1-2H3 YQNWZWMKLDQSAC-UHFFFAOYSA-N 50400902 CHEMBL2204360::vortioxetine hydrobromide::1-(2-(2,4-dimethylphenylsulfanyl)phenyl)piperazine::brintellix::Lu-AA21004::Trintellix 5-hydroxytryptamine receptor 3A Homo sapiens 23 ChEMBL 10.1021/jm101459g 10.7270/Q2W37XFC 21486038 Bang-Andersen, B; Ruhland, T; Jorgensen, M; Smith, G; Frederiksen, K; Jensen, KG; Zhong, H; Nielsen, SM; Hogg, S; Mork, A; Stensbol, TB 5/5/2011 5/17/2013 H. Lundbeck http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50400902 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5137&target=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50400902&enzyme=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search VTX 8AW2,8BLA,8BLB 9966051 163349926 CHEMBL2204360 1 MLLWVQQALLALLLPTLLAQGEARRSRNTTRPALLRLSDYLLTNYRKGVRPVRDWRKPTTVSIDVIVYAILNVDEKNQVLTTYIWYRQYWTDEFLQWNPEDFDNITKLSIPTDSIWVPDILINEFVDVGKSPNIPYVYIRHQGEVQNYKPLQVVTACSLDIYNFPFDVQNCSLTFTSWLHTIQDINISLWRLPEKVKSDRSVFMNQGEWELLGVLPYFREFSMESSNYYAEMKFYVVIRRRPLFYVVSLLLPSIFLMVMDIVGFYLPPNSGERVSFKITLLLGYSVFLIIVSDTLPATAIGTPLIGVYFVVCMALLVISLAETIFIVRLVHKQDLQQPVPAWLRHLVLERIAWLLCLREQSTSQRPPATSQATKTDDCSAMGNHCSHMGGPQDFEKSPRDRCSPPPPPREASLAVCGLLQELSSIRQFLEKRDEIREVARDWLRVGSVLDKLLFHIYLLAVLAYSITLVMLWSIWQYA 8BLB,4PIR,8C21,8C20,8C1Z,8C1W,6Y5B,6Y5A,6Y59,8BLA,8BL8 5-hydroxytryptamine receptor 3A 5HT3A_HUMAN P46098 B4DSY6 G5E986 O60854 Q7KZM7 Q99918 Q9BSZ9 50221382 Cc1ccc(c(c1)C)Sc2ccccc2N3CCNCC3 InChI=1S/C18H22N2S/c1-14-7-8-17(15(2)13-14)21-18-6-4-3-5-16(18)20-11-9-19-10-12-20/h3-8,13,19H,9-12H2,1-2H3 YQNWZWMKLDQSAC-UHFFFAOYSA-N 50400902 CHEMBL2204360::vortioxetine hydrobromide::1-(2-(2,4-dimethylphenylsulfanyl)phenyl)piperazine::brintellix::Lu-AA21004::Trintellix 5-hydroxytryptamine receptor 3A Homo sapiens 12 ChEMBL 10.1021/jm101459g 10.7270/Q2W37XFC 21486038 Bang-Andersen, B; Ruhland, T; Jorgensen, M; Smith, G; Frederiksen, K; Jensen, KG; Zhong, H; Nielsen, SM; Hogg, S; Mork, A; Stensbol, TB 5/5/2011 5/17/2013 H. Lundbeck http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50400902 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5137&target=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50400902&enzyme=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search VTX 8AW2,8BLA,8BLB 9966051 163349926 CHEMBL2204360 1 MLLWVQQALLALLLPTLLAQGEARRSRNTTRPALLRLSDYLLTNYRKGVRPVRDWRKPTTVSIDVIVYAILNVDEKNQVLTTYIWYRQYWTDEFLQWNPEDFDNITKLSIPTDSIWVPDILINEFVDVGKSPNIPYVYIRHQGEVQNYKPLQVVTACSLDIYNFPFDVQNCSLTFTSWLHTIQDINISLWRLPEKVKSDRSVFMNQGEWELLGVLPYFREFSMESSNYYAEMKFYVVIRRRPLFYVVSLLLPSIFLMVMDIVGFYLPPNSGERVSFKITLLLGYSVFLIIVSDTLPATAIGTPLIGVYFVVCMALLVISLAETIFIVRLVHKQDLQQPVPAWLRHLVLERIAWLLCLREQSTSQRPPATSQATKTDDCSAMGNHCSHMGGPQDFEKSPRDRCSPPPPPREASLAVCGLLQELSSIRQFLEKRDEIREVARDWLRVGSVLDKLLFHIYLLAVLAYSITLVMLWSIWQYA 8BLB,4PIR,8C21,8C20,8C1Z,8C1W,6Y5B,6Y5A,6Y59,8BLA,8BL8 5-hydroxytryptamine receptor 3A 5HT3A_HUMAN P46098 B4DSY6 G5E986 O60854 Q7KZM7 Q99918 Q9BSZ9 50221383 Cc1ccc(c(c1)C)Sc2ccccc2N3CCNCC3 InChI=1S/C18H22N2S/c1-14-7-8-17(15(2)13-14)21-18-6-4-3-5-16(18)20-11-9-19-10-12-20/h3-8,13,19H,9-12H2,1-2H3 YQNWZWMKLDQSAC-UHFFFAOYSA-N 50400902 CHEMBL2204360::vortioxetine hydrobromide::1-(2-(2,4-dimethylphenylsulfanyl)phenyl)piperazine::brintellix::Lu-AA21004::Trintellix 5-hydroxytryptamine receptor 3A Homo sapiens 2100 ChEMBL 10.1021/jm101459g 10.7270/Q2W37XFC 21486038 Bang-Andersen, B; Ruhland, T; Jorgensen, M; Smith, G; Frederiksen, K; Jensen, KG; Zhong, H; Nielsen, SM; Hogg, S; Mork, A; Stensbol, TB 5/5/2011 5/17/2013 H. Lundbeck http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50400902 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5137&target=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50400902&enzyme=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search VTX 8AW2,8BLA,8BLB 9966051 163349926 CHEMBL2204360 1 MLLWVQQALLALLLPTLLAQGEARRSRNTTRPALLRLSDYLLTNYRKGVRPVRDWRKPTTVSIDVIVYAILNVDEKNQVLTTYIWYRQYWTDEFLQWNPEDFDNITKLSIPTDSIWVPDILINEFVDVGKSPNIPYVYIRHQGEVQNYKPLQVVTACSLDIYNFPFDVQNCSLTFTSWLHTIQDINISLWRLPEKVKSDRSVFMNQGEWELLGVLPYFREFSMESSNYYAEMKFYVVIRRRPLFYVVSLLLPSIFLMVMDIVGFYLPPNSGERVSFKITLLLGYSVFLIIVSDTLPATAIGTPLIGVYFVVCMALLVISLAETIFIVRLVHKQDLQQPVPAWLRHLVLERIAWLLCLREQSTSQRPPATSQATKTDDCSAMGNHCSHMGGPQDFEKSPRDRCSPPPPPREASLAVCGLLQELSSIRQFLEKRDEIREVARDWLRVGSVLDKLLFHIYLLAVLAYSITLVMLWSIWQYA 8BLB,4PIR,8C21,8C20,8C1Z,8C1W,6Y5B,6Y5A,6Y59,8BLA,8BL8 5-hydroxytryptamine receptor 3A 5HT3A_HUMAN P46098 B4DSY6 G5E986 O60854 Q7KZM7 Q99918 Q9BSZ9 50977693 Cc1ccc(c(c1)C)Sc2ccccc2N3CCNCC3 InChI=1S/C18H22N2S/c1-14-7-8-17(15(2)13-14)21-18-6-4-3-5-16(18)20-11-9-19-10-12-20/h3-8,13,19H,9-12H2,1-2H3 YQNWZWMKLDQSAC-UHFFFAOYSA-N 50400902 CHEMBL2204360::vortioxetine hydrobromide::1-(2-(2,4-dimethylphenylsulfanyl)phenyl)piperazine::brintellix::Lu-AA21004::Trintellix 5-hydroxytryptamine receptor 3A Homo sapiens 3.7 ChEMBL 10.1021/jm101459g 10.7270/Q2W37XFC 21486038 Bang-Andersen, B; Ruhland, T; Jorgensen, M; Smith, G; Frederiksen, K; Jensen, KG; Zhong, H; Nielsen, SM; Hogg, S; Mork, A; Stensbol, TB 5/5/2011 5/17/2013 H. Lundbeck http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50400902 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5137&target=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50400902&enzyme=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search VTX 8AW2,8BLA,8BLB 9966051 163349926 CHEMBL2204360 1 MLLWVQQALLALLLPTLLAQGEARRSRNTTRPALLRLSDYLLTNYRKGVRPVRDWRKPTTVSIDVIVYAILNVDEKNQVLTTYIWYRQYWTDEFLQWNPEDFDNITKLSIPTDSIWVPDILINEFVDVGKSPNIPYVYIRHQGEVQNYKPLQVVTACSLDIYNFPFDVQNCSLTFTSWLHTIQDINISLWRLPEKVKSDRSVFMNQGEWELLGVLPYFREFSMESSNYYAEMKFYVVIRRRPLFYVVSLLLPSIFLMVMDIVGFYLPPNSGERVSFKITLLLGYSVFLIIVSDTLPATAIGTPLIGVYFVVCMALLVISLAETIFIVRLVHKQDLQQPVPAWLRHLVLERIAWLLCLREQSTSQRPPATSQATKTDDCSAMGNHCSHMGGPQDFEKSPRDRCSPPPPPREASLAVCGLLQELSSIRQFLEKRDEIREVARDWLRVGSVLDKLLFHIYLLAVLAYSITLVMLWSIWQYA 8BLB,4PIR,8C21,8C20,8C1Z,8C1W,6Y5B,6Y5A,6Y59,8BLA,8BL8 5-hydroxytryptamine receptor 3A 5HT3A_HUMAN P46098 B4DSY6 G5E986 O60854 Q7KZM7 Q99918 Q9BSZ9 51505668 Cc1ccc(c(c1)C)Sc2ccccc2N3CCNCC3 InChI=1S/C18H22N2S/c1-14-7-8-17(15(2)13-14)21-18-6-4-3-5-16(18)20-11-9-19-10-12-20/h3-8,13,19H,9-12H2,1-2H3 YQNWZWMKLDQSAC-UHFFFAOYSA-N 50400902 CHEMBL2204360::vortioxetine hydrobromide::1-(2-(2,4-dimethylphenylsulfanyl)phenyl)piperazine::brintellix::Lu-AA21004::Trintellix 5-hydroxytryptamine receptor 3A Homo sapiens 3.7 ChEMBL 10.7270/Q2VQ36SJ 34311086 Kucwaj-Brysz, K; Baltrukevich, H; Czarnota, K; Handzlik, J 10/1/2021 6/26/2023 Jagiellonian University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50400902 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5137&target=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50400902&enzyme=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search VTX 8AW2,8BLA,8BLB 9966051 163349926 CHEMBL2204360 1 MLLWVQQALLALLLPTLLAQGEARRSRNTTRPALLRLSDYLLTNYRKGVRPVRDWRKPTTVSIDVIVYAILNVDEKNQVLTTYIWYRQYWTDEFLQWNPEDFDNITKLSIPTDSIWVPDILINEFVDVGKSPNIPYVYIRHQGEVQNYKPLQVVTACSLDIYNFPFDVQNCSLTFTSWLHTIQDINISLWRLPEKVKSDRSVFMNQGEWELLGVLPYFREFSMESSNYYAEMKFYVVIRRRPLFYVVSLLLPSIFLMVMDIVGFYLPPNSGERVSFKITLLLGYSVFLIIVSDTLPATAIGTPLIGVYFVVCMALLVISLAETIFIVRLVHKQDLQQPVPAWLRHLVLERIAWLLCLREQSTSQRPPATSQATKTDDCSAMGNHCSHMGGPQDFEKSPRDRCSPPPPPREASLAVCGLLQELSSIRQFLEKRDEIREVARDWLRVGSVLDKLLFHIYLLAVLAYSITLVMLWSIWQYA 8BLB,4PIR,8C21,8C20,8C1Z,8C1W,6Y5B,6Y5A,6Y59,8BLA,8BL8 5-hydroxytryptamine receptor 3A 5HT3A_HUMAN P46098 B4DSY6 G5E986 O60854 Q7KZM7 Q99918 Q9BSZ9 50606210 Cc1nc[nH]c1CN1CCc2c(c3ccccc3n2C)C1=O InChI=1S/C17H18N4O/c1-11-13(19-10-18-11)9-21-8-7-15-16(17(21)22)12-5-3-4-6-14(12)20(15)2/h3-6,10H,7-9H2,1-2H3,(H,18,19) JSWZEAMFRNKZNL-UHFFFAOYSA-N 93624 SMR000469211::ALOSETRON::MLS001401464::5-methyl-2-[(5-methyl-1H-imidazol-4-yl)methyl]-3,4-dihydropyrido[4,3-b]indol-1-one;hydrochloride::cid_60758::ALOSETRON HCl::5-methyl-2-[(5-methyl-1H-imidazol-4-yl)methyl]-3,4-dihydropyrid[4,3-b]indol-1-one;hydrochloride 5-hydroxytryptamine receptor 3A Homo sapiens 0.5 ChEMBL 10.1016/j.bmcl.2010.09.038 10.7270/Q2Z31ZVH 20889341 Yang, Z; Fairfax, DJ; Maeng, JH; Masih, L; Usyatinsky, A; Hassler, C; Isaacson, S; Fitzpatrick, K; DeOrazio, RJ; Chen, J; Harding, JP; Isherwood, M; Dobritsa, S; Christensen, KL; Wierschke, JD; Bliss, BI; Peterson, LH; Beer, CM; Cioffi, C; Lynch, M; Rennells, WM; Richards, JJ; Rust, T; Khmelnitsky, YL; Cohen, ML; Manning, DD 10/19/2010 6/13/2011 AMRI http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=93624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5137&target=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=93624&enzyme=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search S7Y 6W1J 2099 164034868 1 MLLWVQQALLALLLPTLLAQGEARRSRNTTRPALLRLSDYLLTNYRKGVRPVRDWRKPTTVSIDVIVYAILNVDEKNQVLTTYIWYRQYWTDEFLQWNPEDFDNITKLSIPTDSIWVPDILINEFVDVGKSPNIPYVYIRHQGEVQNYKPLQVVTACSLDIYNFPFDVQNCSLTFTSWLHTIQDINISLWRLPEKVKSDRSVFMNQGEWELLGVLPYFREFSMESSNYYAEMKFYVVIRRRPLFYVVSLLLPSIFLMVMDIVGFYLPPNSGERVSFKITLLLGYSVFLIIVSDTLPATAIGTPLIGVYFVVCMALLVISLAETIFIVRLVHKQDLQQPVPAWLRHLVLERIAWLLCLREQSTSQRPPATSQATKTDDCSAMGNHCSHMGGPQDFEKSPRDRCSPPPPPREASLAVCGLLQELSSIRQFLEKRDEIREVARDWLRVGSVLDKLLFHIYLLAVLAYSITLVMLWSIWQYA 8BLB,4PIR,8C21,8C20,8C1Z,8C1W,6Y5B,6Y5A,6Y59,8BLA,8BL8 5-hydroxytryptamine receptor 3A 5HT3A_HUMAN P46098 B4DSY6 G5E986 O60854 Q7KZM7 Q99918 Q9BSZ9 50617203 Cc1nc[nH]c1CN1CCc2c(c3ccccc3n2C)C1=O InChI=1S/C17H18N4O/c1-11-13(19-10-18-11)9-21-8-7-15-16(17(21)22)12-5-3-4-6-14(12)20(15)2/h3-6,10H,7-9H2,1-2H3,(H,18,19) JSWZEAMFRNKZNL-UHFFFAOYSA-N 93624 SMR000469211::ALOSETRON::MLS001401464::5-methyl-2-[(5-methyl-1H-imidazol-4-yl)methyl]-3,4-dihydropyrido[4,3-b]indol-1-one;hydrochloride::cid_60758::ALOSETRON HCl::5-methyl-2-[(5-methyl-1H-imidazol-4-yl)methyl]-3,4-dihydropyrid[4,3-b]indol-1-one;hydrochloride 5-hydroxytryptamine receptor 3A Homo sapiens 0.5 ChEMBL 10.1016/j.bmcl.2010.11.080 10.7270/Q2474B4Q 21146988 Manning, DD; Cioffi, CL; Usyatinsky, A; Fitzpatrick, K; Masih, L; Guo, C; Zhang, Z; Choo, SH; Sikkander, MI; Ryan, KN; Naginskaya, J; Hassler, C; Dobritsa, S; Wierschke, JD; Earley, WG; Butler, AS; Brady, CA; Barnes, NM; Cohen, ML; Guzzo, PR 12/24/2010 8/22/2011 AMRI http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=93624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5137&target=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=93624&enzyme=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search S7Y 6W1J 2099 164034868 1 MLLWVQQALLALLLPTLLAQGEARRSRNTTRPALLRLSDYLLTNYRKGVRPVRDWRKPTTVSIDVIVYAILNVDEKNQVLTTYIWYRQYWTDEFLQWNPEDFDNITKLSIPTDSIWVPDILINEFVDVGKSPNIPYVYIRHQGEVQNYKPLQVVTACSLDIYNFPFDVQNCSLTFTSWLHTIQDINISLWRLPEKVKSDRSVFMNQGEWELLGVLPYFREFSMESSNYYAEMKFYVVIRRRPLFYVVSLLLPSIFLMVMDIVGFYLPPNSGERVSFKITLLLGYSVFLIIVSDTLPATAIGTPLIGVYFVVCMALLVISLAETIFIVRLVHKQDLQQPVPAWLRHLVLERIAWLLCLREQSTSQRPPATSQATKTDDCSAMGNHCSHMGGPQDFEKSPRDRCSPPPPPREASLAVCGLLQELSSIRQFLEKRDEIREVARDWLRVGSVLDKLLFHIYLLAVLAYSITLVMLWSIWQYA 8BLB,4PIR,8C21,8C20,8C1Z,8C1W,6Y5B,6Y5A,6Y59,8BLA,8BL8 5-hydroxytryptamine receptor 3A 5HT3A_HUMAN P46098 B4DSY6 G5E986 O60854 Q7KZM7 Q99918 Q9BSZ9 51018807 c1cc2c3c(c1)C(=O)N(C[C@H]3CCC2)[C@@H]4CN5CCC4CC5 InChI=1S/C19H24N2O/c22-19-16-6-2-4-14-3-1-5-15(18(14)16)11-21(19)17-12-20-9-7-13(17)8-10-20/h2,4,6,13,15,17H,1,3,5,7-12H2 CPZBLNMUGSZIPR-UHFFFAOYSA-N 50417287 Aloxi::Aurothioglucose::PALONOSETRON::PALONOSETRON HYDROCHLORIDE 5-hydroxytryptamine receptor 3A Homo sapiens 0.0316 ChEMBL 10.1016/j.ejmech.2010.07.039 10.7270/Q2CV4K06 20724042 Moura Barbosa, AJ; De Rienzo, F; Ramos, MJ; Menziani, MC 10/11/2010 5/22/2013 University of Modena and Reggio Emilia http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50417287 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5137&target=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50417287&enzyme=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search O7B 6W1Y,6Y1Z 6337614 163366311 1 MLLWVQQALLALLLPTLLAQGEARRSRNTTRPALLRLSDYLLTNYRKGVRPVRDWRKPTTVSIDVIVYAILNVDEKNQVLTTYIWYRQYWTDEFLQWNPEDFDNITKLSIPTDSIWVPDILINEFVDVGKSPNIPYVYIRHQGEVQNYKPLQVVTACSLDIYNFPFDVQNCSLTFTSWLHTIQDINISLWRLPEKVKSDRSVFMNQGEWELLGVLPYFREFSMESSNYYAEMKFYVVIRRRPLFYVVSLLLPSIFLMVMDIVGFYLPPNSGERVSFKITLLLGYSVFLIIVSDTLPATAIGTPLIGVYFVVCMALLVISLAETIFIVRLVHKQDLQQPVPAWLRHLVLERIAWLLCLREQSTSQRPPATSQATKTDDCSAMGNHCSHMGGPQDFEKSPRDRCSPPPPPREASLAVCGLLQELSSIRQFLEKRDEIREVARDWLRVGSVLDKLLFHIYLLAVLAYSITLVMLWSIWQYA 8BLB,4PIR,8C21,8C20,8C1Z,8C1W,6Y5B,6Y5A,6Y59,8BLA,8BL8 5-hydroxytryptamine receptor 3A 5HT3A_HUMAN P46098 B4DSY6 G5E986 O60854 Q7KZM7 Q99918 Q9BSZ9 51084359 c1cc2c3c(c1)C(=O)N(C[C@H]3CCC2)[C@@H]4CN5CCC4CC5 InChI=1S/C19H24N2O/c22-19-16-6-2-4-14-3-1-5-15(18(14)16)11-21(19)17-12-20-9-7-13(17)8-10-20/h2,4,6,13,15,17H,1,3,5,7-12H2 CPZBLNMUGSZIPR-UHFFFAOYSA-N 50417287 Aloxi::Aurothioglucose::PALONOSETRON::PALONOSETRON HYDROCHLORIDE 5-hydroxytryptamine receptor 3A Homo sapiens 0.830000 ChEMBL 10.1016/j.bmc.2013.09.028 10.7270/Q2JM2C3F 24128813 Del Cadia, M; De Rienzo, F; Weston, DA; Thompson, AJ; Menziani, MC; Lummis, SC 11/1/2013 7/25/2014 University of Modena and Reggio Emilia http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50417287 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5137&target=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50417287&enzyme=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search O7B 6W1Y,6Y1Z 6337614 163366311 1 MLLWVQQALLALLLPTLLAQGEARRSRNTTRPALLRLSDYLLTNYRKGVRPVRDWRKPTTVSIDVIVYAILNVDEKNQVLTTYIWYRQYWTDEFLQWNPEDFDNITKLSIPTDSIWVPDILINEFVDVGKSPNIPYVYIRHQGEVQNYKPLQVVTACSLDIYNFPFDVQNCSLTFTSWLHTIQDINISLWRLPEKVKSDRSVFMNQGEWELLGVLPYFREFSMESSNYYAEMKFYVVIRRRPLFYVVSLLLPSIFLMVMDIVGFYLPPNSGERVSFKITLLLGYSVFLIIVSDTLPATAIGTPLIGVYFVVCMALLVISLAETIFIVRLVHKQDLQQPVPAWLRHLVLERIAWLLCLREQSTSQRPPATSQATKTDDCSAMGNHCSHMGGPQDFEKSPRDRCSPPPPPREASLAVCGLLQELSSIRQFLEKRDEIREVARDWLRVGSVLDKLLFHIYLLAVLAYSITLVMLWSIWQYA 8BLB,4PIR,8C21,8C20,8C1Z,8C1W,6Y5B,6Y5A,6Y59,8BLA,8BL8 5-hydroxytryptamine receptor 3A 5HT3A_HUMAN P46098 B4DSY6 G5E986 O60854 Q7KZM7 Q99918 Q9BSZ9 51084361 c1cc2c3c(c1)C(=O)N(C[C@H]3CCC2)[C@@H]4CN5CCC4CC5 InChI=1S/C19H24N2O/c22-19-16-6-2-4-14-3-1-5-15(18(14)16)11-21(19)17-12-20-9-7-13(17)8-10-20/h2,4,6,13,15,17H,1,3,5,7-12H2 CPZBLNMUGSZIPR-UHFFFAOYSA-N 50417287 Aloxi::Aurothioglucose::PALONOSETRON::PALONOSETRON HYDROCHLORIDE 5-hydroxytryptamine receptor 3A Homo sapiens 0.320000 ChEMBL 10.1016/j.bmc.2013.09.028 10.7270/Q2JM2C3F 24128813 Del Cadia, M; De Rienzo, F; Weston, DA; Thompson, AJ; Menziani, MC; Lummis, SC 11/1/2013 7/25/2014 University of Modena and Reggio Emilia http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50417287 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5137&target=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50417287&enzyme=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search O7B 6W1Y,6Y1Z 6337614 163366311 1 MLLWVQQALLALLLPTLLAQGEARRSRNTTRPALLRLSDYLLTNYRKGVRPVRDWRKPTTVSIDVIVYAILNVDEKNQVLTTYIWYRQYWTDEFLQWNPEDFDNITKLSIPTDSIWVPDILINEFVDVGKSPNIPYVYIRHQGEVQNYKPLQVVTACSLDIYNFPFDVQNCSLTFTSWLHTIQDINISLWRLPEKVKSDRSVFMNQGEWELLGVLPYFREFSMESSNYYAEMKFYVVIRRRPLFYVVSLLLPSIFLMVMDIVGFYLPPNSGERVSFKITLLLGYSVFLIIVSDTLPATAIGTPLIGVYFVVCMALLVISLAETIFIVRLVHKQDLQQPVPAWLRHLVLERIAWLLCLREQSTSQRPPATSQATKTDDCSAMGNHCSHMGGPQDFEKSPRDRCSPPPPPREASLAVCGLLQELSSIRQFLEKRDEIREVARDWLRVGSVLDKLLFHIYLLAVLAYSITLVMLWSIWQYA 8BLB,4PIR,8C21,8C20,8C1Z,8C1W,6Y5B,6Y5A,6Y59,8BLA,8BL8 5-hydroxytryptamine receptor 3A 5HT3A_HUMAN P46098 B4DSY6 G5E986 O60854 Q7KZM7 Q99918 Q9BSZ9 51434026 c1cc2c3c(c1)C(=O)N(C[C@H]3CCC2)[C@@H]4CN5CCC4CC5 InChI=1S/C19H24N2O/c22-19-16-6-2-4-14-3-1-5-15(18(14)16)11-21(19)17-12-20-9-7-13(17)8-10-20/h2,4,6,13,15,17H,1,3,5,7-12H2 CPZBLNMUGSZIPR-UHFFFAOYSA-N 50417287 Aloxi::Aurothioglucose::PALONOSETRON::PALONOSETRON HYDROCHLORIDE 5-hydroxytryptamine receptor 3A Homo sapiens 1.7 ChEMBL 10.1021/acs.jmedchem.1c00224 10.7270/Q2X3528B 34467765 Zajdel, P; Grychowska, K; Mogilski, S; Kurczab, R; Satała, G; Bugno, R; Kos, T; Gołębiowska, J; Malikowska-Racia, N; Nikiforuk, A; Chaumont-Dubel, S; Bantreil, X; Pawłowski, M; Martinez, J; Subra, G; Lamaty, F; Marin, P; Bojarski, AJ; Popik, P 9/23/2021 8/24/2022 Jagiellonian University Medical College http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50417287 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5137&target=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50417287&enzyme=5-hydroxytryptamine+receptor+3A&column=ki&startPg=0&Increment=50&submit=Search O7B 6W1Y,6Y1Z 6337614 163366311 1 MLLWVQQALLALLLPTLLAQGEARRSRNTTRPALLRLSDYLLTNYRKGVRPVRDWRKPTTVSIDVIVYAILNVDEKNQVLTTYIWYRQYWTDEFLQWNPEDFDNITKLSIPTDSIWVPDILINEFVDVGKSPNIPYVYIRHQGEVQNYKPLQVVTACSLDIYNFPFDVQNCSLTFTSWLHTIQDINISLWRLPEKVKSDRSVFMNQGEWELLGVLPYFREFSMESSNYYAEMKFYVVIRRRPLFYVVSLLLPSIFLMVMDIVGFYLPPNSGERVSFKITLLLGYSVFLIIVSDTLPATAIGTPLIGVYFVVCMALLVISLAETIFIVRLVHKQDLQQPVPAWLRHLVLERIAWLLCLREQSTSQRPPATSQATKTDDCSAMGNHCSHMGGPQDFEKSPRDRCSPPPPPREASLAVCGLLQELSSIRQFLEKRDEIREVARDWLRVGSVLDKLLFHIYLLAVLAYSITLVMLWSIWQYA 8BLB,4PIR,8C21,8C20,8C1Z,8C1W,6Y5B,6Y5A,6Y59,8BLA,8BL8 5-hydroxytryptamine receptor 3A 5HT3A_HUMAN P46098 B4DSY6 G5E986 O60854 Q7KZM7 Q99918 Q9BSZ9 50063535 c1cc2c3c(c1)C(=O)N(C[C@H]3CCC2)[C@@H]4CN5CCC4CC5 InChI=1S/C19H24N2O/c22-19-16-6-2-4-14-3-1-5-15(18(14)16)11-21(19)17-12-20-9-7-13(17)8-10-20/h2,4,6,13,15,17H,1,3,5,7-12H2 CPZBLNMUGSZIPR-UHFFFAOYSA-N 50417287 Aloxi::Aurothioglucose::PALONOSETRON::PALONOSETRON HYDROCHLORIDE 5-hydroxytryptamine receptor 3A/3B Rattus norvegicus 0.04 ChEMBL 10.1021/jm00070a008 10.7270/Q2GM88T8 8410977 Clark, RD; Miller, AB; Berger, J; Repke, DB; Weinhardt, KK; Kowalczyk, BA; Eglen, RM; Bonhaus, DW; Lee, CH; Michel, AD 10/29/1993 12/24/2014 Syntex Research http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50417287 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000003&target=5-hydroxytryptamine+receptor+3A%2F3B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50417287&enzyme=5-hydroxytryptamine+receptor+3A%2F3B&column=ki&startPg=0&Increment=50&submit=Search O7B 6337614 163366311 2 MPLCIPQVLLALFLSVLIAQGEGSRRRATQAHSTTQPALLRLSDHLLANYKKGVRPVRDWRKPTLVSIDVIMYAILNVDEKNQVLTTYIWYRQFWTDEFLQWTPEDFDNVTKLSIPTDSIWVPDILINEFVDVGKSPSIPYVYVHHQGEVQNYKPLQLVTACSLDIYNFPFDVQNCSLTFTSWLHTIQDINISLWRTPEEVRSDKSIFINQGEWELLGVFTKFQEFSIETSNSYAEMKFYVVIRRRPLFYAVSLLLPSIFLMVVDIVGFCLPPDSGERVSFKITLLLGYSVFLIIVSDTLPATAIGTPLIGVYFVVCMALLVISLAETIFIVQLVHKQDLQRPVPDWLRHLVLDRIAWLLCLGEQPMAHRPPATFQANKTDDCSAMGNHCSHVGSPQDLEKTSRSRDSPLPPPREASLAVRGLLQELSSIRHSLEKRDEMREVARDWLRVGYVLDRLLFRIYLLAVLAYSITLVTLWSIWHYS 8CC7,8CC6,6Y1Z 5-hydroxytryptamine receptor 3A 5HT3A_RAT P35563 MILLWSCLLVAVVGILGTATPQPGNSSLHRLTRQLLQQYHKEVRPVYNWAEATTVYLDLCVHAVLDVDVQNQKLKTSMWYREVWNDEFLSWNSSLFDDIQEISLPLSAIWAPDIIINEFVDVERSPDLPYVYVNSSGTIRNHKPIQVVSACSLQTYAFPFDIQNCSLTFNSILHTVEDIDLGFLRNQEDIENDKRSFLNDSEWQLLSVTSTYHIRQSSAGDFAQIRFNVVIRRCPLAYVVSLLIPSIFLMLVDLGSFYLPPNCRARIVFKTNVLVGYTVFRVNMSDEVPRSAGCTSLIGVFFTVCMALLVLSLSKSILLIKFLYEERHSEQERPLMCLRGDSDANESRLYLRAPCAEDTESPVRQEHQVPSDTLKDFWFQLQSINNSLRTRDQVYQKEVEWLAILCHFDQLLFRIYLAVLGLYTVTLCSLWALWSRM 5-hydroxytryptamine receptor 3B 5HT3B_RAT Q9JJ16 Q9ERJ5 51084358 c1cc2c3c(c1)C(=O)N(C[C@H]3CCC2)[C@@H]4CN5CCC4CC5 InChI=1S/C19H24N2O/c22-19-16-6-2-4-14-3-1-5-15(18(14)16)11-21(19)17-12-20-9-7-13(17)8-10-20/h2,4,6,13,15,17H,1,3,5,7-12H2 CPZBLNMUGSZIPR-UHFFFAOYSA-N 50417287 Aloxi::Aurothioglucose::PALONOSETRON::PALONOSETRON HYDROCHLORIDE 5-hydroxytryptamine receptor 3A/3B Homo sapiens 0.880000 ChEMBL 10.1016/j.bmc.2013.09.028 10.7270/Q2JM2C3F 24128813 Del Cadia, M; De Rienzo, F; Weston, DA; Thompson, AJ; Menziani, MC; Lummis, SC 11/1/2013 7/25/2014 University of Modena and Reggio Emilia http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50417287 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000004&target=5-hydroxytryptamine+receptor+3A%2F3B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50417287&enzyme=5-hydroxytryptamine+receptor+3A%2F3B&column=ki&startPg=0&Increment=50&submit=Search O7B 6W1Y,6Y1Z 6337614 163366311 2 MLLWVQQALLALLLPTLLAQGEARRSRNTTRPALLRLSDYLLTNYRKGVRPVRDWRKPTTVSIDVIVYAILNVDEKNQVLTTYIWYRQYWTDEFLQWNPEDFDNITKLSIPTDSIWVPDILINEFVDVGKSPNIPYVYIRHQGEVQNYKPLQVVTACSLDIYNFPFDVQNCSLTFTSWLHTIQDINISLWRLPEKVKSDRSVFMNQGEWELLGVLPYFREFSMESSNYYAEMKFYVVIRRRPLFYVVSLLLPSIFLMVMDIVGFYLPPNSGERVSFKITLLLGYSVFLIIVSDTLPATAIGTPLIGVYFVVCMALLVISLAETIFIVRLVHKQDLQQPVPAWLRHLVLERIAWLLCLREQSTSQRPPATSQATKTDDCSAMGNHCSHMGGPQDFEKSPRDRCSPPPPPREASLAVCGLLQELSSIRQFLEKRDEIREVARDWLRVGSVLDKLLFHIYLLAVLAYSITLVMLWSIWQYA 8BLB,4PIR,8C21,8C20,8C1Z,8C1W,6Y5B,6Y5A,6Y59,8BLA,8BL8 5-hydroxytryptamine receptor 3A 5HT3A_HUMAN P46098 B4DSY6 G5E986 O60854 Q7KZM7 Q99918 Q9BSZ9 MLSSVMAPLWACILVAAGILATDTHHPQDSALYHLSKQLLQKYHKEVRPVYNWTKATTVYLDLFVHAILDVDAENQILKTSVWYQEVWNDEFLSWNSSMFDEIREISLPLSAIWAPDIIINEFVDIERYPDLPYVYVNSSGTIENYKPIQVVSACSLETYAFPFDVQNCSLTFKSILHTVEDVDLAFLRSPEDIQHDKKAFLNDSEWELLSVSSTYSILQSSAGGFAQIQFNVVMRRHPLVYVVSLLIPSIFLMLVDLGSFYLPPNCRARIVFKTSVLVGYTVFRVNMSNQVPRSVGSTPLIGHFFTICMAFLVLSLAKSIVLVKFLHDEQRGGQEQPFLCLRGDTDADRPRVEPRAQRAVVTESSLYGEHLAQPGTLKEVWSQLQSISNYLQTQDQTDQQEAEWLVLLSRFDRLLFQSYLFMLGIYTITLCSLWALWGGV 5-hydroxytryptamine receptor 3B 5HT3B_HUMAN O95264 B0YJ23 Q0VJC3 51084360 c1cc2c3c(c1)C(=O)N(C[C@H]3CCC2)[C@@H]4CN5CCC4CC5 InChI=1S/C19H24N2O/c22-19-16-6-2-4-14-3-1-5-15(18(14)16)11-21(19)17-12-20-9-7-13(17)8-10-20/h2,4,6,13,15,17H,1,3,5,7-12H2 CPZBLNMUGSZIPR-UHFFFAOYSA-N 50417287 Aloxi::Aurothioglucose::PALONOSETRON::PALONOSETRON HYDROCHLORIDE 5-hydroxytryptamine receptor 3A/3B Homo sapiens 0.180000 ChEMBL 10.1016/j.bmc.2013.09.028 10.7270/Q2JM2C3F 24128813 Del Cadia, M; De Rienzo, F; Weston, DA; Thompson, AJ; Menziani, MC; Lummis, SC 11/1/2013 7/25/2014 University of Modena and Reggio Emilia http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50417287 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000004&target=5-hydroxytryptamine+receptor+3A%2F3B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50417287&enzyme=5-hydroxytryptamine+receptor+3A%2F3B&column=ki&startPg=0&Increment=50&submit=Search O7B 6W1Y,6Y1Z 6337614 163366311 2 MLLWVQQALLALLLPTLLAQGEARRSRNTTRPALLRLSDYLLTNYRKGVRPVRDWRKPTTVSIDVIVYAILNVDEKNQVLTTYIWYRQYWTDEFLQWNPEDFDNITKLSIPTDSIWVPDILINEFVDVGKSPNIPYVYIRHQGEVQNYKPLQVVTACSLDIYNFPFDVQNCSLTFTSWLHTIQDINISLWRLPEKVKSDRSVFMNQGEWELLGVLPYFREFSMESSNYYAEMKFYVVIRRRPLFYVVSLLLPSIFLMVMDIVGFYLPPNSGERVSFKITLLLGYSVFLIIVSDTLPATAIGTPLIGVYFVVCMALLVISLAETIFIVRLVHKQDLQQPVPAWLRHLVLERIAWLLCLREQSTSQRPPATSQATKTDDCSAMGNHCSHMGGPQDFEKSPRDRCSPPPPPREASLAVCGLLQELSSIRQFLEKRDEIREVARDWLRVGSVLDKLLFHIYLLAVLAYSITLVMLWSIWQYA 8BLB,4PIR,8C21,8C20,8C1Z,8C1W,6Y5B,6Y5A,6Y59,8BLA,8BL8 5-hydroxytryptamine receptor 3A 5HT3A_HUMAN P46098 B4DSY6 G5E986 O60854 Q7KZM7 Q99918 Q9BSZ9 MLSSVMAPLWACILVAAGILATDTHHPQDSALYHLSKQLLQKYHKEVRPVYNWTKATTVYLDLFVHAILDVDAENQILKTSVWYQEVWNDEFLSWNSSMFDEIREISLPLSAIWAPDIIINEFVDIERYPDLPYVYVNSSGTIENYKPIQVVSACSLETYAFPFDVQNCSLTFKSILHTVEDVDLAFLRSPEDIQHDKKAFLNDSEWELLSVSSTYSILQSSAGGFAQIQFNVVMRRHPLVYVVSLLIPSIFLMLVDLGSFYLPPNCRARIVFKTSVLVGYTVFRVNMSNQVPRSVGSTPLIGHFFTICMAFLVLSLAKSIVLVKFLHDEQRGGQEQPFLCLRGDTDADRPRVEPRAQRAVVTESSLYGEHLAQPGTLKEVWSQLQSISNYLQTQDQTDQQEAEWLVLLSRFDRLLFQSYLFMLGIYTITLCSLWALWGGV 5-hydroxytryptamine receptor 3B 5HT3B_HUMAN O95264 B0YJ23 Q0VJC3 50087833 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 29 ChEMBL 10.1021/jm401879z 10.7270/Q2Q81FMQ 24611893 Winter, E; Devantier Neuenfeldt, P; Chiaradia-Delatorre, LD; Gauthier, C; Yunes, RA; Nunes, RJ; Creczynski-Pasa, TB; Di Pietro, A 6/6/2014 2/8/2015 Bmssi Umr 5086 Cnrs/Universit£ http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 50087862 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 12 ChEMBL 10.1021/jm401879z 10.7270/Q2Q81FMQ 24611893 Winter, E; Devantier Neuenfeldt, P; Chiaradia-Delatorre, LD; Gauthier, C; Yunes, RA; Nunes, RJ; Creczynski-Pasa, TB; Di Pietro, A 6/6/2014 2/8/2015 Bmssi Umr 5086 Cnrs/Universit£ http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 50157993 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 230 ChEMBL 10.1016/j.bmcl.2009.11.004 10.7270/Q2G73DT7 19932960 Pick, A; Muller, H; Wiese, M 2/3/2010 8/31/2010 University of Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 50171796 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 390 ChEMBL 10.1016/j.bmc.2010.12.043 10.7270/Q2PZ593F 21354800 Pick, A; Muller, H; Mayer, R; Haenisch, B; Pajeva, IK; Weigt, M; Bonisch, H; Muller, CE; Wiese, M 3/14/2011 8/24/2011 University of Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 50242066 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 90 ChEMBL 10.1021/jm500943z 10.7270/Q2V40WST 25272055 Jabor Gozzi, G; Bouaziz, Z; Winter, E; Daflon-Yunes, N; Aichele, D; Nacereddine, A; Marminon, C; Valdameri, G; Zeinyeh, W; Bollacke, A; Guillon, J; Lacoudre, A; Pinaud, N; Cadena, SM; Jose, J; Le Borgne, M; Di Pietro, A 1/9/2015 3/10/2016 Bmssi Umr 5086 Cnrs/Universit£ http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 50337471 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 128 ChEMBL 10.1021/acs.jmedchem.5b00188 10.7270/Q2WD4296 25855895 Köhler, SC; Wiese, M 5/14/2015 5/6/2016 University of Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 50347255 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 24 ChEMBL 10.1021/acs.jmedchem.5b00085 10.7270/Q2N29ZP5 25985195 Wong, IL; Wang, BC; Yuan, J; Duan, LX; Liu, Z; Liu, T; Li, XM; Hu, X; Zhang, XY; Jiang, T; Wan, SB; Chow, LM 6/11/2015 10/10/2016 The Hong Kong Polytechnic University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 50498917 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 240 ChEMBL 10.1016/j.ejmech.2016.03.067 10.7270/Q23J3FW7 27100033 Kraege, S; Stefan, K; Juvale, K; Ross, T; Willmes, T; Wiese, M 5/16/2016 9/12/2017 University of Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 50528095 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 74 ChEMBL 10.1016/j.ejmech.2016.05.053 10.7270/Q28K7C22 27376492 Pires, ADRA; Lecerf-Schmidt, F; Guragossian, N; Pazinato, J; Gozzi, GJ; Winter, E; Valdameri, G; Veale, A; Boumendjel, A; Di Pietro, A; Pérès, B 10/21/2016 8/3/2018 University of Lyon 1 http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 50545011 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 221 ChEMBL 10.1016/j.ejmech.2016.09.010 10.7270/Q28P62HT 27676469 Köhler, SC; Silbermann, K; Wiese, M 11/29/2016 9/2/2018 Rheinische Friedrich-Wilhelms-Universit£T Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 50545035 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 276 ChEMBL 10.1016/j.ejmech.2016.09.010 10.7270/Q28P62HT 27676469 Köhler, SC; Silbermann, K; Wiese, M 11/29/2016 9/2/2018 Rheinische Friedrich-Wilhelms-Universit£T Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 50546493 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 74 ChEMBL 10.1016/j.bmcl.2009.11.004 10.7270/Q2G73DT7 19932960 Pick, A; Muller, H; Wiese, M 2/3/2010 8/31/2010 University of Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 50627937 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 210 ChEMBL 10.1016/j.bmc.2010.12.043 10.7270/Q2PZ593F 21354800 Pick, A; Muller, H; Mayer, R; Haenisch, B; Pajeva, IK; Weigt, M; Bonisch, H; Muller, CE; Wiese, M 3/14/2011 8/24/2011 University of Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 50709259 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 330 ChEMBL 10.1016/j.bmc.2011.10.074 10.7270/Q24X587H 22112540 Juvale, K; Pape, VF; Wiese, M 12/30/2011 7/22/2012 University of Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 50709294 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 260 ChEMBL 10.1016/j.bmc.2011.10.074 10.7270/Q24X587H 22112540 Juvale, K; Pape, VF; Wiese, M 12/30/2011 7/22/2012 University of Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 50750058 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 227 ChEMBL 10.1021/acs.jmedchem.7b00441 10.7270/Q2GT5Q9V 28471656 Krapf, MK; Gallus, J; Wiese, M 5/25/2017 9/20/2019 University of Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 50866045 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 233 ChEMBL 10.1021/acs.jmedchem.7b01012 10.7270/Q2HM5BXM 29547272 Krapf, MK; Gallus, J; Vahdati, S; Wiese, M 4/26/2018 1/29/2020 University of Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 50866054 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 227 ChEMBL 10.1021/acs.jmedchem.7b01012 10.7270/Q2HM5BXM 29547272 Krapf, MK; Gallus, J; Vahdati, S; Wiese, M 4/26/2018 1/29/2020 University of Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 50878248 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 225 ChEMBL 10.1021/jm8013822 10.7270/Q2VH5PQ4 19170519 Kuhnle, M; Egger, M; Muller, C; Mahringer, A; Bernhardt, G; Fricker, G; Konig, B; Buschauer, A 6/17/2009 12/19/2012 University of Regensburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 50924834 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 50 ChEMBL 10.1021/jm201404w 10.7270/Q2KH0PBT 22165858 Valdameri, G; Genoux-Bastide, E; Peres, B; Gauthier, C; Guitton, J; Terreux, R; Winnischofer, SM; Rocha, ME; Boumendjel, A; Di Pietro, A 1/26/2012 2/7/2013 Cnrs/Universit£ http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 50960595 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 250 ChEMBL 10.1016/j.bmcl.2012.08.024 10.7270/Q2QJ7JD9 23017888 Juvale, K; Wiese, M 10/15/2012 5/17/2013 University of Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 50982371 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 84 ChEMBL 10.1016/j.ejmech.2017.08.020 10.7270/Q2R49T8R 28841513 Krapf, MK; Gallus, J; Wiese, M 10/20/2017 6/2/2020 University of Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 50983215 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 227 ChEMBL 10.1016/j.ejmech.2017.08.020 10.7270/Q2R49T8R 28841513 Krapf, MK; Gallus, J; Wiese, M 10/20/2017 6/2/2020 University of Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 51007129 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 309.03 ChEMBL 10.1016/j.bmc.2008.07.034 10.7270/Q2765GK5 18678495 Pick, A; Muller, H; Wiese, M 9/4/2008 5/21/2013 University of Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 51026417 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 5 ChEMBL 10.1124/mol.65.6.1485 10.7270/Q20V8F2J 15155841 Ozvegy-Laczka, C; Hegedus, T; Varady, G; Ujhelly, O; Schuetz, JD; Varadi, A; Keri, G; Orfi, L; Nemet, K; Sarkadi, B 5/24/2004 5/22/2013 Membrane Research Group of The Hungarian Academy of Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 51038200 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 221 ChEMBL 10.1016/j.ejmech.2018.01.012 10.7270/Q2J67KJH 29407974 Köhler, SC; Vahdati, S; Scholz, MS; Wiese, M 2/25/2018 8/16/2020 Rheinische Friedrich-Wilhelms-Universit£T Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 51049470 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 117 ChEMBL 10.1021/ml4000832 10.7270/Q2T72JRQ 24900683 Ochoa-Puentes, C; Bauer, S; Kühnle, M; Bernhardt, G; Buschauer, A; König, B 4/11/2013 9/24/2013 University of Regensburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 51075437 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 354 ChEMBL 10.1016/j.ejmech.2013.06.035 10.7270/Q2W66N6K 23851114 Juvale, K; Stefan, K; Wiese, M 9/9/2013 4/13/2014 University of Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 51075438 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 215 ChEMBL 10.1016/j.ejmech.2013.06.035 10.7270/Q2W66N6K 23851114 Juvale, K; Stefan, K; Wiese, M 9/9/2013 4/13/2014 University of Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 51085049 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 330 ChEMBL 10.1016/j.bmc.2013.10.007 10.7270/Q2TX3GT2 24184213 Juvale, K; Gallus, J; Wiese, M 12/3/2013 7/25/2014 University of Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 51085059 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 250 ChEMBL 10.1016/j.bmc.2013.10.007 10.7270/Q2TX3GT2 24184213 Juvale, K; Gallus, J; Wiese, M 12/3/2013 7/25/2014 University of Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 51098909 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 227 ChEMBL 10.1021/acs.jmedchem.8b01011 10.7270/Q28C9ZTN 30075623 Krapf, MK; Gallus, J; Namasivayam, V; Wiese, M 9/13/2018 8/14/2020 University of Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 51205119 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 70 ChEMBL 10.1021/jm401649j 10.7270/Q2RJ4NF5 24304387 Winter, E; Lecerf-Schmidt, F; Gozzi, G; Peres, B; Lightbody, M; Gauthier, C; Ozvegy-Laczka, C; Szakacs, G; Sarkadi, B; Creczynski-Pasa, TB; Boumendjel, A; Di Pietro, A 12/27/2013 9/2/2020 Bmssi Umr 5086 Cnrs/Universit£ http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 51205136 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 90 ChEMBL 10.1021/jm401649j 10.7270/Q2RJ4NF5 24304387 Winter, E; Lecerf-Schmidt, F; Gozzi, G; Peres, B; Lightbody, M; Gauthier, C; Ozvegy-Laczka, C; Szakacs, G; Sarkadi, B; Creczynski-Pasa, TB; Boumendjel, A; Di Pietro, A 12/27/2013 9/2/2020 Bmssi Umr 5086 Cnrs/Universit£ http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 51205147 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 170 ChEMBL 10.1021/jm401649j 10.7270/Q2RJ4NF5 24304387 Winter, E; Lecerf-Schmidt, F; Gozzi, G; Peres, B; Lightbody, M; Gauthier, C; Ozvegy-Laczka, C; Szakacs, G; Sarkadi, B; Creczynski-Pasa, TB; Boumendjel, A; Di Pietro, A 12/27/2013 9/2/2020 Bmssi Umr 5086 Cnrs/Universit£ http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 51234022 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 24 ChEMBL 10.1021/acs.jmedchem.9b00963 10.7270/Q28S4T5Q 31465686 Zhu, X; Wong, ILK; Chan, KF; Cui, J; Law, MC; Chong, TC; Hu, X; Chow, LMC; Chan, TH 9/26/2019 2/18/2021 Hong Kong Polytechnic University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 51234029 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 10.0 ChEMBL 10.1021/acs.jmedchem.9b00963 10.7270/Q28S4T5Q 31465686 Zhu, X; Wong, ILK; Chan, KF; Cui, J; Law, MC; Chong, TC; Hu, X; Chow, LMC; Chan, TH 9/26/2019 2/18/2021 Hong Kong Polytechnic University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 51234097 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 8.7 ChEMBL 10.1021/acs.jmedchem.9b00963 10.7270/Q28S4T5Q 31465686 Zhu, X; Wong, ILK; Chan, KF; Cui, J; Law, MC; Chong, TC; Hu, X; Chow, LMC; Chan, TH 9/26/2019 2/18/2021 Hong Kong Polytechnic University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 51234117 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 9.0 ChEMBL 10.1021/acs.jmedchem.9b00963 10.7270/Q28S4T5Q 31465686 Zhu, X; Wong, ILK; Chan, KF; Cui, J; Law, MC; Chong, TC; Hu, X; Chow, LMC; Chan, TH 9/26/2019 2/18/2021 Hong Kong Polytechnic University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 51234324 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 5.4 ChEMBL 10.1021/acs.jmedchem.9b00963 10.7270/Q28S4T5Q 31465686 Zhu, X; Wong, ILK; Chan, KF; Cui, J; Law, MC; Chong, TC; Hu, X; Chow, LMC; Chan, TH 9/26/2019 2/18/2021 Hong Kong Polytechnic University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 51239166 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 227 ChEMBL 10.1016/j.ejmech.2018.10.026 10.7270/Q23N26P9 30390439 Krapf, MK; Gallus, J; Spindler, A; Wiese, M 1/1/2019 2/19/2021 University of Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 51254312 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 202 ChEMBL 10.1021/acs.jmedchem.8b01821 10.7270/Q2X06BDS 30925062 Silbermann, K; Stefan, SM; Elshawadfy, R; Namasivayam, V; Wiese, M 5/9/2019 2/20/2021 Rheinische Friedrich-Wilhelms-University of Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 51311888 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 221 ChEMBL 10.1021/acs.jmedchem.6b00330 10.7270/Q2HH6PJ5 27148793 Krapf, MK; Wiese, M 6/9/2016 2/27/2021 University of Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 51311913 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 221 ChEMBL 10.1021/acs.jmedchem.6b00330 10.7270/Q2HH6PJ5 27148793 Krapf, MK; Wiese, M 6/9/2016 2/27/2021 University of Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 51324564 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 4.0 ChEMBL 10.1021/acs.jmedchem.6b00035 10.7270/Q28K7DK6 27280693 Spindler, A; Stefan, K; Wiese, M 7/14/2016 2/28/2021 University of Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 51324570 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 28 ChEMBL 10.1021/acs.jmedchem.6b00035 10.7270/Q28K7DK6 27280693 Spindler, A; Stefan, K; Wiese, M 7/14/2016 2/28/2021 University of Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 51324574 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 221 ChEMBL 10.1021/acs.jmedchem.6b00035 10.7270/Q28K7DK6 27280693 Spindler, A; Stefan, K; Wiese, M 7/14/2016 2/28/2021 University of Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 51364230 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 92 ChEMBL 10.1016/j.ejmech.2020.112133 10.7270/Q2MP56XK 32105979 Antoni, F; Bause, M; Scholler, M; Bauer, S; Stark, SA; Jackson, SM; Manolaridis, I; Locher, KP; König, B; Buschauer, A; Bernhardt, G 4/1/2020 3/24/2022 University of Regensburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 51374041 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 90 ChEMBL 10.1016/j.ejmech.2020.112503 10.7270/Q29027FW 32653696 Roussel, E; Moréno, A; Altounian, N; Philouze, C; Pérès, B; Thomas, A; Renaudet, O; Falson, P; Boumendjel, A 9/15/2020 3/26/2022 Cnrs http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 51387814 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 220 ChEMBL 10.1021/acs.jmedchem.0c00961 10.7270/Q2ZS317X 32787102 Silbermann, K; Li, J; Namasivayam, V; Baltes, F; Bendas, G; Stefan, SM; Wiese, M 9/24/2020 3/28/2022 Rheinische Friedrich-Wilhelms-University Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 51387838 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 274 ChEMBL 10.1021/acs.jmedchem.0c00961 10.7270/Q2ZS317X 32787102 Silbermann, K; Li, J; Namasivayam, V; Baltes, F; Bendas, G; Stefan, SM; Wiese, M 9/24/2020 3/28/2022 Rheinische Friedrich-Wilhelms-University Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 51476090 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 10.0 ChEMBL 10.7270/Q2PZ5DT3 35483322 Zattoni, IF; Delabio, LC; Dutra, JP; Kita, DH; Scheiffer, G; Hembecker, M; Pereira, GDS; Moure, VR; Valdameri, G 7/5/2022 6/21/2023 Federal University of Parana http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 51546469 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 652 ChEMBL 10.7270/Q25M6B34 37154765 Zechner, M; Castro Jaramillo, CA; Zubler, NS; Taddio, MF; Mu, L; Altmann, KH; Krämer, SD 5/25/2023 12/16/2024 Eth Zurich http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 51562375 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 50 ChEMBL 10.7270/Q22R3X3G 36628850 Goracci, L; Nurisso, A; Roussel, E; Pérès, B; Chaptal, V; Falson, P; Marminon, C; Jose, J; Le Borgne, M; Boumendjel, A 2/15/2023 12/19/2024 University of Perugia http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 51575854 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 7.1 ChEMBL 10.7270/Q279494X 37847948 Yu, S; Zheng, J; Zhang, Y; Meng, D; Wang, Y; Xu, X; Liang, N; Shabiti, S; Zhang, X; Wang, Z; Yang, Z; Mi, P; Zheng, X; Li, W; Chen, H 11/15/2023 12/22/2024 University of South China http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 51613762 COc1ccc2c3c([nH]c2c1)[C@H](CC(C)C)N1C(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@@H]1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50305083 Ko143::Ko-143::3-((3S,6S)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::3-((3S,6S,12aS)-6-Isobutyl-9-methoxy-1,4-dioxo-1,2,3,4,6,7,12,12a-octahydro-pyrazino[1',2':1,6]pyrido[3,4-b]indol-3-yl)-propionic acid tert-butyl ester::CHEMBL488910::US9695174, Ko143 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 160 ChEMBL 10.7270/Q2KD23M3 37482017 Zhu, J; Lei, S; Lu, J; Hao, Y; Qian, Q; Devanathan, AS; Feng, Z; Xie, XQ; Wipf, P; Ma, X //0 10/13/2025 University of Pittsburgh http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50305083 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50305083&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 10322450 104159444 CHEMBL488910 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 51529637 COc1ccc2c3c([nH]c2c1)C(CC(C)C)N1C(=O)C(CCC(=O)OC(C)(C)C)NC(=O)C1C3 InChI=1S/C26H35N3O5/c1-14(2)11-20-23-17(16-8-7-15(33-6)12-19(16)27-23)13-21-24(31)28-18(25(32)29(20)21)9-10-22(30)34-26(3,4)5/h7-8,12,14,18,20-21,27H,9-11,13H2,1-6H3,(H,28,31) NXNRAECHCJZNRF-UHFFFAOYSA-N 50615469 CHEMBL5285476 Broad substrate specificity ATP-binding cassette transporter ABCG2 Homo sapiens 1250 ChEMBL 10.7270/Q2D50S7Q 29016119 Stefan, K; Schmitt, SM; Wiese, M 11/9/2017 4/23/2024 University of Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50615469 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4026&target=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50615469&enzyme=Broad+substrate+specificity+ATP-binding+cassette+transporter+ABCG2&column=ki&startPg=0&Increment=50&submit=Search I3O 8PY4 69534441 494505217 1 MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS 8U2C,8Q7B,8P8J,8P8A,8P7W,7NFD,7NEZ,7NEQ,6VXJ,6VXI,6VXH,6VXF,6HIJ,6FEQ,6ETI,8QCM,8PY4,8PXO,8BI0,8BHT,7OJI,7OJH,7OJ8,6FFC,5NJG,5NJ3 Broad substrate specificity ATP-binding cassette transporter ABCG2 ABCG2_HUMAN Q9UNQ0 A0A1W3 A8K1T5 O95374 Q4W5I3 Q53ZQ1 Q569L4 Q5YLG4 Q86V64 Q8IX16 Q96LD6 Q96TA8 Q9BY73 Q9NUS0 51509083 CCCCCCCn1c(O)c(-c2ccccc2)n(-c2ccccc2)c1=O InChI=1S/C22H26N2O2/c1-2-3-4-5-12-17-23-21(25)20(18-13-8-6-9-14-18)24(22(23)26)19-15-10-7-11-16-19/h6-11,13-16,25H,2-5,12,17H2,1H3 SHOHKCFHDLUFSW-UHFFFAOYSA-N 50422780 CHEMBL5286061 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 Human 13490 ChEMBL 10.7270/Q26H4NNJ 32679452 n/a 10/1/2020 4/19/2024 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50422780 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=8473&target=6-phosphofructo-2-kinase%2Ffructose-2%2C6-bisphosphatase+3&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50422780&enzyme=6-phosphofructo-2-kinase%2Ffructose-2%2C6-bisphosphatase+3&column=ki&startPg=0&Increment=50&submit=Search 91900212 164151655 CHEMBL425928 ZINC44220812 1 MPLELTQSRVQKIWVPVDHRPSLPRSCGPKLTNSPTVIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMKVRKQCALAALRDVKSYLAKEGGQIAVFDATNTTRERRHMILHFAKENDFKAFFIESVCDDPTVVASNIMEVKISSPDYKDCNSAEAMDDFMKRISCYEASYQPLDPDKCDRDLSLIKVIDVGRRFLVNRVQDHIQSRIVYYLMNIHVQPRTIYLCRHGENEHNLQGRIGGDSGLSSRGKKFASALSKFVEEQNLKDLRVWTSQLKSTIQTAEALRLPYEQWKALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQRLEPVIMELERQENVLVICHQAVLRCLLAYFLDKSAEEMPYLKCPLHTVLKLTPVAYGCRVESIYLNVESVCTHRERSEDAKKGPNPLMRRNSVTPLASPEPTKKPRINSFEEHVASTSAALPSCLPPEVPTQLPGQNMKGSRSSADSSRKH 2AXN,2DWO,2DWP,2I1V,3QPU,3QPV,3QPW,4D4J,4D4K,4D4L,4D4M,4MA4,5AJV,5AJW,5AJX,5AJY,5AJZ,5AK0,6ETJ,6HVH,6HVI,6HVJ 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 F263_HUMAN Q16875 B7Z955 O43622 O75902 Q5VX15 Q5VX18 Q5VX19 51509085 CCCCCCCn1c(O)c(-c2ccccc2)n(-c2ccccc2)c1=O InChI=1S/C22H26N2O2/c1-2-3-4-5-12-17-23-21(25)20(18-13-8-6-9-14-18)24(22(23)26)19-15-10-7-11-16-19/h6-11,13-16,25H,2-5,12,17H2,1H3 SHOHKCFHDLUFSW-UHFFFAOYSA-N 50422780 CHEMBL5286061 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 Human 47 ChEMBL 10.7270/Q26H4NNJ 32679452 n/a 10/1/2020 4/19/2024 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50422780 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=8473&target=6-phosphofructo-2-kinase%2Ffructose-2%2C6-bisphosphatase+3&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50422780&enzyme=6-phosphofructo-2-kinase%2Ffructose-2%2C6-bisphosphatase+3&column=ki&startPg=0&Increment=50&submit=Search 91900212 164151655 CHEMBL425928 ZINC44220812 1 MPLELTQSRVQKIWVPVDHRPSLPRSCGPKLTNSPTVIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMKVRKQCALAALRDVKSYLAKEGGQIAVFDATNTTRERRHMILHFAKENDFKAFFIESVCDDPTVVASNIMEVKISSPDYKDCNSAEAMDDFMKRISCYEASYQPLDPDKCDRDLSLIKVIDVGRRFLVNRVQDHIQSRIVYYLMNIHVQPRTIYLCRHGENEHNLQGRIGGDSGLSSRGKKFASALSKFVEEQNLKDLRVWTSQLKSTIQTAEALRLPYEQWKALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQRLEPVIMELERQENVLVICHQAVLRCLLAYFLDKSAEEMPYLKCPLHTVLKLTPVAYGCRVESIYLNVESVCTHRERSEDAKKGPNPLMRRNSVTPLASPEPTKKPRINSFEEHVASTSAALPSCLPPEVPTQLPGQNMKGSRSSADSSRKH 2AXN,2DWO,2DWP,2I1V,3QPU,3QPV,3QPW,4D4J,4D4K,4D4L,4D4M,4MA4,5AJV,5AJW,5AJX,5AJY,5AJZ,5AK0,6ETJ,6HVH,6HVI,6HVJ 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 F263_HUMAN Q16875 B7Z955 O43622 O75902 Q5VX15 Q5VX18 Q5VX19 50330860 c1ccc(cc1)Cn2c3ccc(cc3c(c2N)C#N)Oc4ccc(cc4)NC(=O)CN InChI=1S/C24H21N5O2/c25-13-21-20-12-19(31-18-8-6-17(7-9-18)28-23(30)14-26)10-11-22(20)29(24(21)27)15-16-4-2-1-3-5-16/h1-12H,14-15,26-27H2,(H,28,30) RVTAACJVJXEMFR-UHFFFAOYSA-N 50082135 CHEMBL3422658 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 Homo sapiens 104 ChEMBL 10.1021/acs.jmedchem.5b00352 10.7270/Q2571DQB 25849762 Boyd, S; Brookfield, JL; Critchlow, SE; Cumming, IA; Curtis, NJ; Debreczeni, J; Degorce, SL; Donald, C; Evans, NJ; Groombridge, S; Hopcroft, P; Jones, NP; Kettle, JG; Lamont, S; Lewis, HJ; MacFaull, P; McLoughlin, SB; Rigoreau, LJ; Smith, JM; St-Gallay, S; Stock, JK; Turnbull, AP; Wheatley, ER; Winter, J; Wingfield, J 4/23/2015 5/1/2016 Astrazeneca http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50082135 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=8473&target=6-phosphofructo-2-kinase%2Ffructose-2%2C6-bisphosphatase+3&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50082135&enzyme=6-phosphofructo-2-kinase%2Ffructose-2%2C6-bisphosphatase+3&column=ki&startPg=0&Increment=50&submit=Search S6L 5AJW 91668553 313074487 CHEMBL3422658 1 MPLELTQSRVQKIWVPVDHRPSLPRSCGPKLTNSPTVIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMKVRKQCALAALRDVKSYLAKEGGQIAVFDATNTTRERRHMILHFAKENDFKAFFIESVCDDPTVVASNIMEVKISSPDYKDCNSAEAMDDFMKRISCYEASYQPLDPDKCDRDLSLIKVIDVGRRFLVNRVQDHIQSRIVYYLMNIHVQPRTIYLCRHGENEHNLQGRIGGDSGLSSRGKKFASALSKFVEEQNLKDLRVWTSQLKSTIQTAEALRLPYEQWKALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQRLEPVIMELERQENVLVICHQAVLRCLLAYFLDKSAEEMPYLKCPLHTVLKLTPVAYGCRVESIYLNVESVCTHRERSEDAKKGPNPLMRRNSVTPLASPEPTKKPRINSFEEHVASTSAALPSCLPPEVPTQLPGQNMKGSRSSADSSRKH 6HVJ,6HVI,6HVH,6ETJ,5AK0,5AJZ,5AJY,5AJX,5AJW,5AJV,4MA4,3QPW,3QPV,3QPU,2I1V,2DWP,2DWO,2AXN,4D4M,4D4L,4D4K,4D4J,6IBZ,6IBX,6IBY,6IC0 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 F263_HUMAN Q16875 B7Z955 O43622 O75902 Q5VX15 Q5VX18 Q5VX19 50331091 c1ccc(cc1)Cn2c3ccc(cc3c(c2N)C#N)Oc4ccc(cc4)NC(=O)CN InChI=1S/C24H21N5O2/c25-13-21-20-12-19(31-18-8-6-17(7-9-18)28-23(30)14-26)10-11-22(20)29(24(21)27)15-16-4-2-1-3-5-16/h1-12H,14-15,26-27H2,(H,28,30) RVTAACJVJXEMFR-UHFFFAOYSA-N 50082135 CHEMBL3422658 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 Homo sapiens >30000 ChEMBL 10.1021/acs.jmedchem.5b00352 10.7270/Q2571DQB 25849762 Boyd, S; Brookfield, JL; Critchlow, SE; Cumming, IA; Curtis, NJ; Debreczeni, J; Degorce, SL; Donald, C; Evans, NJ; Groombridge, S; Hopcroft, P; Jones, NP; Kettle, JG; Lamont, S; Lewis, HJ; MacFaull, P; McLoughlin, SB; Rigoreau, LJ; Smith, JM; St-Gallay, S; Stock, JK; Turnbull, AP; Wheatley, ER; Winter, J; Wingfield, J 4/23/2015 5/1/2016 Astrazeneca http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50082135 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=8473&target=6-phosphofructo-2-kinase%2Ffructose-2%2C6-bisphosphatase+3&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50082135&enzyme=6-phosphofructo-2-kinase%2Ffructose-2%2C6-bisphosphatase+3&column=ki&startPg=0&Increment=50&submit=Search S6L 5AJW 91668553 313074487 CHEMBL3422658 1 MPLELTQSRVQKIWVPVDHRPSLPRSCGPKLTNSPTVIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMKVRKQCALAALRDVKSYLAKEGGQIAVFDATNTTRERRHMILHFAKENDFKAFFIESVCDDPTVVASNIMEVKISSPDYKDCNSAEAMDDFMKRISCYEASYQPLDPDKCDRDLSLIKVIDVGRRFLVNRVQDHIQSRIVYYLMNIHVQPRTIYLCRHGENEHNLQGRIGGDSGLSSRGKKFASALSKFVEEQNLKDLRVWTSQLKSTIQTAEALRLPYEQWKALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQRLEPVIMELERQENVLVICHQAVLRCLLAYFLDKSAEEMPYLKCPLHTVLKLTPVAYGCRVESIYLNVESVCTHRERSEDAKKGPNPLMRRNSVTPLASPEPTKKPRINSFEEHVASTSAALPSCLPPEVPTQLPGQNMKGSRSSADSSRKH 6HVJ,6HVI,6HVH,6ETJ,5AK0,5AJZ,5AJY,5AJX,5AJW,5AJV,4MA4,3QPW,3QPV,3QPU,2I1V,2DWP,2DWO,2AXN,4D4M,4D4L,4D4K,4D4J,6IBZ,6IBX,6IBY,6IC0 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 F263_HUMAN Q16875 B7Z955 O43622 O75902 Q5VX15 Q5VX18 Q5VX19 50331112 c1ccc(cc1)Cn2c3ccc(cc3c(c2N)C#N)Oc4ccc(cc4)NC(=O)CN InChI=1S/C24H21N5O2/c25-13-21-20-12-19(31-18-8-6-17(7-9-18)28-23(30)14-26)10-11-22(20)29(24(21)27)15-16-4-2-1-3-5-16/h1-12H,14-15,26-27H2,(H,28,30) RVTAACJVJXEMFR-UHFFFAOYSA-N 50082135 CHEMBL3422658 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 Homo sapiens 12600 ChEMBL 10.1021/acs.jmedchem.5b00352 10.7270/Q2571DQB 25849762 Boyd, S; Brookfield, JL; Critchlow, SE; Cumming, IA; Curtis, NJ; Debreczeni, J; Degorce, SL; Donald, C; Evans, NJ; Groombridge, S; Hopcroft, P; Jones, NP; Kettle, JG; Lamont, S; Lewis, HJ; MacFaull, P; McLoughlin, SB; Rigoreau, LJ; Smith, JM; St-Gallay, S; Stock, JK; Turnbull, AP; Wheatley, ER; Winter, J; Wingfield, J 4/23/2015 5/1/2016 Astrazeneca http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50082135 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=8473&target=6-phosphofructo-2-kinase%2Ffructose-2%2C6-bisphosphatase+3&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50082135&enzyme=6-phosphofructo-2-kinase%2Ffructose-2%2C6-bisphosphatase+3&column=ki&startPg=0&Increment=50&submit=Search S6L 5AJW 91668553 313074487 CHEMBL3422658 1 MPLELTQSRVQKIWVPVDHRPSLPRSCGPKLTNSPTVIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMKVRKQCALAALRDVKSYLAKEGGQIAVFDATNTTRERRHMILHFAKENDFKAFFIESVCDDPTVVASNIMEVKISSPDYKDCNSAEAMDDFMKRISCYEASYQPLDPDKCDRDLSLIKVIDVGRRFLVNRVQDHIQSRIVYYLMNIHVQPRTIYLCRHGENEHNLQGRIGGDSGLSSRGKKFASALSKFVEEQNLKDLRVWTSQLKSTIQTAEALRLPYEQWKALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQRLEPVIMELERQENVLVICHQAVLRCLLAYFLDKSAEEMPYLKCPLHTVLKLTPVAYGCRVESIYLNVESVCTHRERSEDAKKGPNPLMRRNSVTPLASPEPTKKPRINSFEEHVASTSAALPSCLPPEVPTQLPGQNMKGSRSSADSSRKH 6HVJ,6HVI,6HVH,6ETJ,5AK0,5AJZ,5AJY,5AJX,5AJW,5AJV,4MA4,3QPW,3QPV,3QPU,2I1V,2DWP,2DWO,2AXN,4D4M,4D4L,4D4K,4D4J,6IBZ,6IBX,6IBY,6IC0 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 F263_HUMAN Q16875 B7Z955 O43622 O75902 Q5VX15 Q5VX18 Q5VX19 50330930 Cc1c(c(on1)C)Cn2cc(c3c2ccc(c3)Oc4ccc(cc4)NC(=O)[C@@H]5CCCN5)C#N InChI=1S/C26H25N5O3/c1-16-23(17(2)34-30-16)15-31-14-18(13-27)22-12-21(9-10-25(22)31)33-20-7-5-19(6-8-20)29-26(32)24-4-3-11-28-24/h5-10,12,14,24,28H,3-4,11,15H2,1-2H3,(H,29,32) NDIKFKQBWGMLCA-UHFFFAOYSA-N 50082116 CHEMBL3422676 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 Homo sapiens 11 ChEMBL 10.1021/acs.jmedchem.5b00352 10.7270/Q2571DQB 25849762 Boyd, S; Brookfield, JL; Critchlow, SE; Cumming, IA; Curtis, NJ; Debreczeni, J; Degorce, SL; Donald, C; Evans, NJ; Groombridge, S; Hopcroft, P; Jones, NP; Kettle, JG; Lamont, S; Lewis, HJ; MacFaull, P; McLoughlin, SB; Rigoreau, LJ; Smith, JM; St-Gallay, S; Stock, JK; Turnbull, AP; Wheatley, ER; Winter, J; Wingfield, J 4/23/2015 5/1/2016 Astrazeneca http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50082116 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=8473&target=6-phosphofructo-2-kinase%2Ffructose-2%2C6-bisphosphatase+3&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50082116&enzyme=6-phosphofructo-2-kinase%2Ffructose-2%2C6-bisphosphatase+3&column=ki&startPg=0&Increment=50&submit=Search FD9 5AJX 91668554 313074470 CHEMBL3422676 1 MPLELTQSRVQKIWVPVDHRPSLPRSCGPKLTNSPTVIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMKVRKQCALAALRDVKSYLAKEGGQIAVFDATNTTRERRHMILHFAKENDFKAFFIESVCDDPTVVASNIMEVKISSPDYKDCNSAEAMDDFMKRISCYEASYQPLDPDKCDRDLSLIKVIDVGRRFLVNRVQDHIQSRIVYYLMNIHVQPRTIYLCRHGENEHNLQGRIGGDSGLSSRGKKFASALSKFVEEQNLKDLRVWTSQLKSTIQTAEALRLPYEQWKALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQRLEPVIMELERQENVLVICHQAVLRCLLAYFLDKSAEEMPYLKCPLHTVLKLTPVAYGCRVESIYLNVESVCTHRERSEDAKKGPNPLMRRNSVTPLASPEPTKKPRINSFEEHVASTSAALPSCLPPEVPTQLPGQNMKGSRSSADSSRKH 6HVJ,6HVI,6HVH,6ETJ,5AK0,5AJZ,5AJY,5AJX,5AJW,5AJV,4MA4,3QPW,3QPV,3QPU,2I1V,2DWP,2DWO,2AXN,4D4M,4D4L,4D4K,4D4J,6IBZ,6IBX,6IBY,6IC0 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 F263_HUMAN Q16875 B7Z955 O43622 O75902 Q5VX15 Q5VX18 Q5VX19 50331099 Cc1c(c(on1)C)Cn2cc(c3c2ccc(c3)Oc4ccc(cc4)NC(=O)[C@@H]5CCCN5)C#N InChI=1S/C26H25N5O3/c1-16-23(17(2)34-30-16)15-31-14-18(13-27)22-12-21(9-10-25(22)31)33-20-7-5-19(6-8-20)29-26(32)24-4-3-11-28-24/h5-10,12,14,24,28H,3-4,11,15H2,1-2H3,(H,29,32) NDIKFKQBWGMLCA-UHFFFAOYSA-N 50082116 CHEMBL3422676 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 Homo sapiens 281 ChEMBL 10.1021/acs.jmedchem.5b00352 10.7270/Q2571DQB 25849762 Boyd, S; Brookfield, JL; Critchlow, SE; Cumming, IA; Curtis, NJ; Debreczeni, J; Degorce, SL; Donald, C; Evans, NJ; Groombridge, S; Hopcroft, P; Jones, NP; Kettle, JG; Lamont, S; Lewis, HJ; MacFaull, P; McLoughlin, SB; Rigoreau, LJ; Smith, JM; St-Gallay, S; Stock, JK; Turnbull, AP; Wheatley, ER; Winter, J; Wingfield, J 4/23/2015 5/1/2016 Astrazeneca http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50082116 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=8473&target=6-phosphofructo-2-kinase%2Ffructose-2%2C6-bisphosphatase+3&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50082116&enzyme=6-phosphofructo-2-kinase%2Ffructose-2%2C6-bisphosphatase+3&column=ki&startPg=0&Increment=50&submit=Search FD9 5AJX 91668554 313074470 CHEMBL3422676 1 MPLELTQSRVQKIWVPVDHRPSLPRSCGPKLTNSPTVIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMKVRKQCALAALRDVKSYLAKEGGQIAVFDATNTTRERRHMILHFAKENDFKAFFIESVCDDPTVVASNIMEVKISSPDYKDCNSAEAMDDFMKRISCYEASYQPLDPDKCDRDLSLIKVIDVGRRFLVNRVQDHIQSRIVYYLMNIHVQPRTIYLCRHGENEHNLQGRIGGDSGLSSRGKKFASALSKFVEEQNLKDLRVWTSQLKSTIQTAEALRLPYEQWKALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQRLEPVIMELERQENVLVICHQAVLRCLLAYFLDKSAEEMPYLKCPLHTVLKLTPVAYGCRVESIYLNVESVCTHRERSEDAKKGPNPLMRRNSVTPLASPEPTKKPRINSFEEHVASTSAALPSCLPPEVPTQLPGQNMKGSRSSADSSRKH 6HVJ,6HVI,6HVH,6ETJ,5AK0,5AJZ,5AJY,5AJX,5AJW,5AJV,4MA4,3QPW,3QPV,3QPU,2I1V,2DWP,2DWO,2AXN,4D4M,4D4L,4D4K,4D4J,6IBZ,6IBX,6IBY,6IC0 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 F263_HUMAN Q16875 B7Z955 O43622 O75902 Q5VX15 Q5VX18 Q5VX19 50331551 Cc1c(c(on1)C)Cn2cc(c3c2ccc(c3)Oc4ccc(cc4)NC(=O)[C@@H]5CCCN5)C#N InChI=1S/C26H25N5O3/c1-16-23(17(2)34-30-16)15-31-14-18(13-27)22-12-21(9-10-25(22)31)33-20-7-5-19(6-8-20)29-26(32)24-4-3-11-28-24/h5-10,12,14,24,28H,3-4,11,15H2,1-2H3,(H,29,32) NDIKFKQBWGMLCA-UHFFFAOYSA-N 50082116 CHEMBL3422676 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 Homo sapiens >30000 ChEMBL 10.1021/acs.jmedchem.5b00352 10.7270/Q2571DQB 25849762 Boyd, S; Brookfield, JL; Critchlow, SE; Cumming, IA; Curtis, NJ; Debreczeni, J; Degorce, SL; Donald, C; Evans, NJ; Groombridge, S; Hopcroft, P; Jones, NP; Kettle, JG; Lamont, S; Lewis, HJ; MacFaull, P; McLoughlin, SB; Rigoreau, LJ; Smith, JM; St-Gallay, S; Stock, JK; Turnbull, AP; Wheatley, ER; Winter, J; Wingfield, J 4/23/2015 5/1/2016 Astrazeneca http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50082116 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=8473&target=6-phosphofructo-2-kinase%2Ffructose-2%2C6-bisphosphatase+3&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50082116&enzyme=6-phosphofructo-2-kinase%2Ffructose-2%2C6-bisphosphatase+3&column=ki&startPg=0&Increment=50&submit=Search FD9 5AJX 91668554 313074470 CHEMBL3422676 1 MPLELTQSRVQKIWVPVDHRPSLPRSCGPKLTNSPTVIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMKVRKQCALAALRDVKSYLAKEGGQIAVFDATNTTRERRHMILHFAKENDFKAFFIESVCDDPTVVASNIMEVKISSPDYKDCNSAEAMDDFMKRISCYEASYQPLDPDKCDRDLSLIKVIDVGRRFLVNRVQDHIQSRIVYYLMNIHVQPRTIYLCRHGENEHNLQGRIGGDSGLSSRGKKFASALSKFVEEQNLKDLRVWTSQLKSTIQTAEALRLPYEQWKALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQRLEPVIMELERQENVLVICHQAVLRCLLAYFLDKSAEEMPYLKCPLHTVLKLTPVAYGCRVESIYLNVESVCTHRERSEDAKKGPNPLMRRNSVTPLASPEPTKKPRINSFEEHVASTSAALPSCLPPEVPTQLPGQNMKGSRSSADSSRKH 6HVJ,6HVI,6HVH,6ETJ,5AK0,5AJZ,5AJY,5AJX,5AJW,5AJV,4MA4,3QPW,3QPV,3QPU,2I1V,2DWP,2DWO,2AXN,4D4M,4D4L,4D4K,4D4J,6IBZ,6IBX,6IBY,6IC0 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 F263_HUMAN Q16875 B7Z955 O43622 O75902 Q5VX15 Q5VX18 Q5VX19 50330862 N#Cc1c[nH]c2ccc(Oc3ccc(NC(=O)CN)cc3)cc12 InChI=1S/C17H14N4O2/c18-8-11-10-20-16-6-5-14(7-15(11)16)23-13-3-1-12(2-4-13)21-17(22)9-19/h1-7,10,20H,9,19H2,(H,21,22) FTYQKBVNGALNLT-UHFFFAOYSA-N 50082137 CHEMBL3422660 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 Homo sapiens 2010 ChEMBL 10.1021/acs.jmedchem.5b00352 10.7270/Q2571DQB 25849762 Boyd, S; Brookfield, JL; Critchlow, SE; Cumming, IA; Curtis, NJ; Debreczeni, J; Degorce, SL; Donald, C; Evans, NJ; Groombridge, S; Hopcroft, P; Jones, NP; Kettle, JG; Lamont, S; Lewis, HJ; MacFaull, P; McLoughlin, SB; Rigoreau, LJ; Smith, JM; St-Gallay, S; Stock, JK; Turnbull, AP; Wheatley, ER; Winter, J; Wingfield, J 4/23/2015 5/1/2016 AstraZeneca http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50082137 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=8473&target=6-phosphofructo-2-kinase%2Ffructose-2%2C6-bisphosphatase+3&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50082137&enzyme=6-phosphofructo-2-kinase%2Ffructose-2%2C6-bisphosphatase+3&column=ki&startPg=0&Increment=50&submit=Search MJP 5AJZ 91668556 313074489 CHEMBL3422660 1 MPLELTQSRVQKIWVPVDHRPSLPRSCGPKLTNSPTVIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMKVRKQCALAALRDVKSYLAKEGGQIAVFDATNTTRERRHMILHFAKENDFKAFFIESVCDDPTVVASNIMEVKISSPDYKDCNSAEAMDDFMKRISCYEASYQPLDPDKCDRDLSLIKVIDVGRRFLVNRVQDHIQSRIVYYLMNIHVQPRTIYLCRHGENEHNLQGRIGGDSGLSSRGKKFASALSKFVEEQNLKDLRVWTSQLKSTIQTAEALRLPYEQWKALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQRLEPVIMELERQENVLVICHQAVLRCLLAYFLDKSAEEMPYLKCPLHTVLKLTPVAYGCRVESIYLNVESVCTHRERSEDAKKGPNPLMRRNSVTPLASPEPTKKPRINSFEEHVASTSAALPSCLPPEVPTQLPGQNMKGSRSSADSSRKH 6HVJ,6HVI,6HVH,6ETJ,5AK0,5AJZ,5AJY,5AJX,5AJW,5AJV,4MA4,3QPW,3QPV,3QPU,2I1V,2DWP,2DWO,2AXN,4D4M,4D4L,4D4K,4D4J,6IBZ,6IBX,6IBY,6IC0 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 F263_HUMAN Q16875 B7Z955 O43622 O75902 Q5VX15 Q5VX18 Q5VX19 50590204 CC1(O[C@@H]([C@@H](O1)C(=O)NO)COP(=O)(O)O)C InChI=1S/C7H14NO8P/c1-7(2)15-4(3-14-17(11,12)13)5(16-7)6(9)8-10/h4-5,10H,3H2,1-2H3,(H,8,9)(H2,11,12,13) DVFAQEVWJBLFDS-UHFFFAOYSA-N 50148780 (5-(hydroxycarbamoyl)-2,2-dimethyl-1,3-dioxolan-4-yl)methyl dihydrogen phosphate::Phosphoric acid mono-((R)-(R)-5-hydroxycarbamoyl-2,2-dimethyl-[1,3]dioxolan-4-ylmethyl) ester::((4R,5R)-5-(hydroxycarbamoyl)-2,2-dimethyl-1,3-dioxolan-4-yl)methyl dihydrogen phosphate::CHEMBL324609 6-phosphogluconate dehydrogenase, decarboxylating Ovis aries 1100 ChEMBL 10.1021/jm1004754 10.7270/Q2Q81D8T 20666371 Ruda, GF; Wong, PE; Alibu, VP; Norval, S; Read, KD; Barrett, MP; Gilbert, IH 8/19/2010 3/19/2011 University of Dundee http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50148780 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50004528&target=6-phosphogluconate+dehydrogenase%2C+decarboxylating&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50148780&enzyme=6-phosphogluconate+dehydrogenase%2C+decarboxylating&column=ki&startPg=0&Increment=50&submit=Search 8HS 5UQ9 11242708 104037016 CHEMBL324609 1 MAQADIALIGLAVMGQNLILNMNDHGFVVCAFNRTVSKVDDFLANEAKGTKVLGAHSLEEMVSKLKKPRRIILLVKAGQAVDNFIEKLVPLLDIGDIIIDGGNSEYRDTMRRCRDLKDKGILFVGSGVSGGEDGARYGPSLMPGGNKEAWPHIKAIFQGIAAKVGTGEPCCDWVGDDGAGHFVKMVHNGIEYGDMQLICEAYHLMKDVLGLGHKEMAKAFEEWNKTELDSFLIEITASILKFQDADGKHLLPKIRDSAGQKGTGKWTAISALEYGVPVTLIGEAVFARCLSSLKDERIQASKKLKGPQNIPFEGDKKSFLEDIRKALYASKIISYAQGFMLLRQAATEFGWTLNYGGIALMWRGGCIIRSVFLGKIKDAFDRNPGLQNLLLDDFFKSAVENCQDSWRRAISTGVQAGIPMPCFTTALSFYDGYRHAMLPANLIQAQRDYFGAHTYELLAKPGQFIHTNWTGHGGSVSSSSYNA 2PGD,1PGQ,1PGP,1PGO,1PGN 6-phosphogluconate dehydrogenase, decarboxylating 6PGD_SHEEP P00349 50819153 CC1(O[C@@H]([C@@H](O1)C(=O)NO)COP(=O)(O)O)C InChI=1S/C7H14NO8P/c1-7(2)15-4(3-14-17(11,12)13)5(16-7)6(9)8-10/h4-5,10H,3H2,1-2H3,(H,8,9)(H2,11,12,13) DVFAQEVWJBLFDS-UHFFFAOYSA-N 50148780 (5-(hydroxycarbamoyl)-2,2-dimethyl-1,3-dioxolan-4-yl)methyl dihydrogen phosphate::Phosphoric acid mono-((R)-(R)-5-hydroxycarbamoyl-2,2-dimethyl-[1,3]dioxolan-4-ylmethyl) ester::((4R,5R)-5-(hydroxycarbamoyl)-2,2-dimethyl-1,3-dioxolan-4-yl)methyl dihydrogen phosphate::CHEMBL324609 6-phosphogluconate dehydrogenase, decarboxylating Homo sapiens 1100 ChEMBL 10.1021/jm031066i 10.7270/Q2S1837H 15189039 Dardonville, C; Rinaldi, E; Barrett, MP; Brun, R; Gilbert, IH; Hanau, S 6/10/2004 11/30/2012 Cardiff University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50148780 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5076&target=6-phosphogluconate+dehydrogenase%2C+decarboxylating&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50148780&enzyme=6-phosphogluconate+dehydrogenase%2C+decarboxylating&column=ki&startPg=0&Increment=50&submit=Search 8HS 5UQ9 11242708 104037016 CHEMBL324609 1 MAQADIALIGLAVMGQNLILNMNDHGFVVCAFNRTVSKVDDFLANEAKGTKVVGAQSLKEMVSKLKKPRRIILLVKAGQAVDDFIEKLVPLLDTGDIIIDGGNSEYRDTTRRCRDLKAKGILFVGSGVSGGEEGARYGPSLMPGGNKEAWPHIKTIFQGIAAKVGTGEPCCDWVGDEGAGHFVKMVHNGIEYGDMQLICEAYHLMKDVLGMAQDEMAQAFEDWNKTELDSFLIEITANILKFQDTDGKHLLPKIRDSAGQKGTGKWTAISALEYGVPVTLIGEAVFARCLSSLKDERIQASKKLKGPQKFQFDGDKKSFLEDIRKALYASKIISYAQGFMLLRQAATEFGWTLNYGGIALMWRGGCIIRSVFLGKIKDAFDRNPELQNLLLDDFFKSAVENCQDSWRRAVSTGVQAGIPMPCFTTALSFYDGYRHEMLPASLIQAQRDYFGAHTYELLAKPGQFIHTNWTGHGGTVSSSSYNA 5UQ9,2JKV,4GWK,4GWG 6-phosphogluconate dehydrogenase, decarboxylating 6PGD_HUMAN P52209 A8K2Y9 B4DQJ8 Q9BWD8 50819156 CC1(O[C@@H]([C@@H](O1)C(=O)NO)COP(=O)(O)O)C InChI=1S/C7H14NO8P/c1-7(2)15-4(3-14-17(11,12)13)5(16-7)6(9)8-10/h4-5,10H,3H2,1-2H3,(H,8,9)(H2,11,12,13) DVFAQEVWJBLFDS-UHFFFAOYSA-N 50148780 (5-(hydroxycarbamoyl)-2,2-dimethyl-1,3-dioxolan-4-yl)methyl dihydrogen phosphate::Phosphoric acid mono-((R)-(R)-5-hydroxycarbamoyl-2,2-dimethyl-[1,3]dioxolan-4-ylmethyl) ester::((4R,5R)-5-(hydroxycarbamoyl)-2,2-dimethyl-1,3-dioxolan-4-yl)methyl dihydrogen phosphate::CHEMBL324609 6-phosphogluconate dehydrogenase, decarboxylating Homo sapiens 35 ChEMBL 10.1021/jm031066i 10.7270/Q2S1837H 15189039 Dardonville, C; Rinaldi, E; Barrett, MP; Brun, R; Gilbert, IH; Hanau, S 6/10/2004 11/30/2012 Cardiff University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50148780 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5076&target=6-phosphogluconate+dehydrogenase%2C+decarboxylating&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50148780&enzyme=6-phosphogluconate+dehydrogenase%2C+decarboxylating&column=ki&startPg=0&Increment=50&submit=Search 8HS 5UQ9 11242708 104037016 CHEMBL324609 1 MAQADIALIGLAVMGQNLILNMNDHGFVVCAFNRTVSKVDDFLANEAKGTKVVGAQSLKEMVSKLKKPRRIILLVKAGQAVDDFIEKLVPLLDTGDIIIDGGNSEYRDTTRRCRDLKAKGILFVGSGVSGGEEGARYGPSLMPGGNKEAWPHIKTIFQGIAAKVGTGEPCCDWVGDEGAGHFVKMVHNGIEYGDMQLICEAYHLMKDVLGMAQDEMAQAFEDWNKTELDSFLIEITANILKFQDTDGKHLLPKIRDSAGQKGTGKWTAISALEYGVPVTLIGEAVFARCLSSLKDERIQASKKLKGPQKFQFDGDKKSFLEDIRKALYASKIISYAQGFMLLRQAATEFGWTLNYGGIALMWRGGCIIRSVFLGKIKDAFDRNPELQNLLLDDFFKSAVENCQDSWRRAVSTGVQAGIPMPCFTTALSFYDGYRHEMLPASLIQAQRDYFGAHTYELLAKPGQFIHTNWTGHGGTVSSSSYNA 5UQ9,2JKV,4GWK,4GWG 6-phosphogluconate dehydrogenase, decarboxylating 6PGD_HUMAN P52209 A8K2Y9 B4DQJ8 Q9BWD8 50915782 CC1(O[C@@H]([C@@H](O1)C(=O)NO)COP(=O)(O)O)C InChI=1S/C7H14NO8P/c1-7(2)15-4(3-14-17(11,12)13)5(16-7)6(9)8-10/h4-5,10H,3H2,1-2H3,(H,8,9)(H2,11,12,13) DVFAQEVWJBLFDS-UHFFFAOYSA-N 50148780 (5-(hydroxycarbamoyl)-2,2-dimethyl-1,3-dioxolan-4-yl)methyl dihydrogen phosphate::Phosphoric acid mono-((R)-(R)-5-hydroxycarbamoyl-2,2-dimethyl-[1,3]dioxolan-4-ylmethyl) ester::((4R,5R)-5-(hydroxycarbamoyl)-2,2-dimethyl-1,3-dioxolan-4-yl)methyl dihydrogen phosphate::CHEMBL324609 6-phosphogluconate dehydrogenase, decarboxylating Ovis aries 1100 ChEMBL 10.1016/j.bmc.2010.05.077 10.7270/Q2X34ZDH 20598892 Ruda, GF; Campbell, G; Alibu, VP; Barrett, MP; Brenk, R; Gilbert, IH 7/13/2010 12/31/2012 University of Dundee http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50148780 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50004528&target=6-phosphogluconate+dehydrogenase%2C+decarboxylating&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50148780&enzyme=6-phosphogluconate+dehydrogenase%2C+decarboxylating&column=ki&startPg=0&Increment=50&submit=Search 8HS 5UQ9 11242708 104037016 CHEMBL324609 1 MAQADIALIGLAVMGQNLILNMNDHGFVVCAFNRTVSKVDDFLANEAKGTKVLGAHSLEEMVSKLKKPRRIILLVKAGQAVDNFIEKLVPLLDIGDIIIDGGNSEYRDTMRRCRDLKDKGILFVGSGVSGGEDGARYGPSLMPGGNKEAWPHIKAIFQGIAAKVGTGEPCCDWVGDDGAGHFVKMVHNGIEYGDMQLICEAYHLMKDVLGLGHKEMAKAFEEWNKTELDSFLIEITASILKFQDADGKHLLPKIRDSAGQKGTGKWTAISALEYGVPVTLIGEAVFARCLSSLKDERIQASKKLKGPQNIPFEGDKKSFLEDIRKALYASKIISYAQGFMLLRQAATEFGWTLNYGGIALMWRGGCIIRSVFLGKIKDAFDRNPGLQNLLLDDFFKSAVENCQDSWRRAISTGVQAGIPMPCFTTALSFYDGYRHAMLPANLIQAQRDYFGAHTYELLAKPGQFIHTNWTGHGGSVSSSSYNA 2PGD,1PGQ,1PGP,1PGO,1PGN 6-phosphogluconate dehydrogenase, decarboxylating 6PGD_SHEEP P00349 122677 C[C@H]1C[C@@H](C(=O)[C@@H](C1)[C@@H](CC2CC(=O)NC(=O)C2)O)C InChI=1S/C15H23NO4/c1-8-3-9(2)15(20)11(4-8)12(17)5-10-6-13(18)16-14(19)7-10/h8-12,17H,3-7H2,1-2H3,(H,16,18,19) YPHMISFOHDHNIV-UHFFFAOYSA-N 50080528 Cycloheximid::3-((R)-2-((1S,3S,5S)-3,5-dimethyl-2-oxocyclohexyl)-2-hydroxyethyl)glutarimide::CHEMBL123292::cycloheximide::Zykloheximid::cid_6197::4-{(2R)-2-[(1S,3S,5S)-3,5-dimethyl-2-oxocyclohexyl]-2-hydroxyethyl}piperidine-2,6-dione::med.21724, Compound Cycloheximide 60S ribosomal protein L19-A Saccharomyces cerevisiae (strain ATCC 204508 / S288c) 644 PubChem 10.7270/Q2JQ0ZGP aid2740 PubChem, PC 4/1/2010 7/11/2011 Nmmlsc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50080528 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4787&target=60S+ribosomal+protein+L19-A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50080528&enzyme=60S+ribosomal+protein+L19-A&column=ki&startPg=0&Increment=50&submit=Search 3HE 4U3U,5GAK,5LKS,6HD7,6TNU,6Y0G,6Y2L,7N8B,7Q08,7R81,8BN3,8G6J,8IPA,8IPB,8T2X,8T2Y,8T2Z,8T30,8UT0,8UTI,9BH5,9CAI,9FQZ,9P7F,9P7G,9P7H,9P7I,9P7J,9P8I 6197 103980685 CHEMBL123292 C06685 1 MANLRTQKRLAASVVGVGKRKVWLDPNETSEIAQANSRNAIRKLVKNGTIVKKAVTVHSKSRTRAHAQSKREGRHSGYGKRKGTREARLPSQVVWIRRLRVLRRLLAKYRDAGKIDKHLYHVLYKESKGNAFKHKRALVEHIIQAKADAQREKALNEEAEARRLKNRAARDRRAQRVAEKRDALLKEDA 9R9P,9R9O,9PN5,9F9S,9DP7,9DOV,8Y0U,8V87,8T3F,8T3E,8T3D,8T3C,8T3B,8T3A,8T30,8T2Z,8T2Y,8T2X,8PNN,8PFR,8P9A,8P8U,8P8N,8P8M,8P85,8P4V,8K82,8K2D,8HFR,8EWC,8EWB,8EVT,8EVS,8EVR,8EVQ,8EVP,8EUB,8CMJ,8CKU,8CIV,8CGN,8CG8,8CF5,8CEH,8CDR,8CDL,8CCS,8AGZ,8AGX,8AGW,8AGV,8AGU,8AGT,8AAF,7ZW0,7Z34,7V08,7UQZ,7UQB,7UOO,7UG6,7U0H,7TOP,7TOO,7RR5,7R7A,7R72,7OHV,7OHR,7OHQ,7OH3,7OF1,7NAD,7NAC,7BTB,7BT6,7AZY,6Z6K,6Z6J,6YLY,6YLX,6YLH,6YLG,6XIR,6XIQ,6T83,6T7I,6SV4,6S05,6RZZ,6RI5,6QTZ,6QT0,6QIK,6N8L,6N8K,6N8J,6M62,6HHQ,6HD7,6FT6,6EM5,6ELZ,5MC6,5JUU,5JUT,5JUS,5JUP,5JUO,5JCS,5H4P,5GAK,5APO,5APN,4V91,4V8T,4V88,4V7R,4V7F,4V6I,3JCT,2WWB,2WWA,2WW9,8ZHC,8ZHB,8ZH3,8ZGY,8ZGR,8Z71,8Z70,8YLR,8YLD,8XU8,8UTI,8UT0,8BQX,8BQD,8BN3,8BJQ,8BIP,7ZUX,7ZUW,7ZRS,7ZPQ,7NRD,7NRC,7N8B,7MPJ,7MPI,7B7D,6WOO,6TNU,6TB3,6T7T,6T4Q,6S47,6Q8Y,6OIG,6I7O,6GQV,6GQB,6GQ1,5TGM,5TGA,5TBW,5ON6,5OBM,5NDW,5NDV,5NDG,5MEI,5M1J,5LYB,5I4L,5FCJ,5FCI,5DGV,5DGF,5DGE,5DC3,5DAT,4V8Z,4V8Y,4U6F,4U56,4U55,4U53,4U52,4U51,4U50,4U4Z,4U4Y,4U4U,4U4R,4U4Q,4U4O,4U4N,4U3U,4U3N,4U3M,7ZS5,6R87,6R86,6R84,4V4B,4V7H Large ribosomal subunit protein eL19A RL19A_YEAST P0CX82 D6VPX3 P05735 122677 C[C@H]1C[C@@H](C(=O)[C@@H](C1)[C@@H](CC2CC(=O)NC(=O)C2)O)C InChI=1S/C15H23NO4/c1-8-3-9(2)15(20)11(4-8)12(17)5-10-6-13(18)16-14(19)7-10/h8-12,17H,3-7H2,1-2H3,(H,16,18,19) YPHMISFOHDHNIV-UHFFFAOYSA-N 50080528 Cycloheximid::3-((R)-2-((1S,3S,5S)-3,5-dimethyl-2-oxocyclohexyl)-2-hydroxyethyl)glutarimide::CHEMBL123292::cycloheximide::Zykloheximid::cid_6197::4-{(2R)-2-[(1S,3S,5S)-3,5-dimethyl-2-oxocyclohexyl]-2-hydroxyethyl}piperidine-2,6-dione::med.21724, Compound Cycloheximide 60S ribosomal protein L19-A Saccharomyces cerevisiae (strain ATCC 204508 / S288c) 644 PubChem 10.7270/Q2JQ0ZGP aid2740 PubChem, PC 4/1/2010 7/11/2011 Nmmlsc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50080528 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4787&target=60S+ribosomal+protein+L19-A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50080528&enzyme=60S+ribosomal+protein+L19-A&column=ki&startPg=0&Increment=50&submit=Search 3HE 4U3U,5GAK,5LKS,6HD7,6TNU,6Y0G,6Y2L,7N8B,7Q08,7R81,8BN3,8G6J,8IPA,8IPB,8T2X,8T2Y,8T2Z,8T30,8UT0,8UTI,9BH5,9CAI,9FQZ,9P7F,9P7G,9P7H,9P7I,9P7J,9P8I 6197 103980685 CHEMBL123292 C06685 1 MANLRTQKRLAASVVGVGKRKVWLDPNETSEIAQANSRNAIRKLVKNGTIVKKAVTVHSKSRTRAHAQSKREGRHSGYGKRKGTREARLPSQVVWIRRLRVLRRLLAKYRDAGKIDKHLYHVLYKESKGNAFKHKRALVEHIIQAKADAQREKALNEEAEARRLKNRAARDRRAQRVAEKRDALLKEDA 9R9P,9R9O,9PN5,9F9S,9DP7,9DOV,8Y0U,8V87,8T3F,8T3E,8T3D,8T3C,8T3B,8T3A,8T30,8T2Z,8T2Y,8T2X,8PNN,8PFR,8P9A,8P8U,8P8N,8P8M,8P85,8P4V,8K82,8K2D,8HFR,8EWC,8EWB,8EVT,8EVS,8EVR,8EVQ,8EVP,8EUB,8CMJ,8CKU,8CIV,8CGN,8CG8,8CF5,8CEH,8CDR,8CDL,8CCS,8AGZ,8AGX,8AGW,8AGV,8AGU,8AGT,8AAF,7ZW0,7Z34,7V08,7UQZ,7UQB,7UOO,7UG6,7U0H,7TOP,7TOO,7RR5,7R7A,7R72,7OHV,7OHR,7OHQ,7OH3,7OF1,7NAD,7NAC,7BTB,7BT6,7AZY,6Z6K,6Z6J,6YLY,6YLX,6YLH,6YLG,6XIR,6XIQ,6T83,6T7I,6SV4,6S05,6RZZ,6RI5,6QTZ,6QT0,6QIK,6N8L,6N8K,6N8J,6M62,6HHQ,6HD7,6FT6,6EM5,6ELZ,5MC6,5JUU,5JUT,5JUS,5JUP,5JUO,5JCS,5H4P,5GAK,5APO,5APN,4V91,4V8T,4V88,4V7R,4V7F,4V6I,3JCT,2WWB,2WWA,2WW9,8ZHC,8ZHB,8ZH3,8ZGY,8ZGR,8Z71,8Z70,8YLR,8YLD,8XU8,8UTI,8UT0,8BQX,8BQD,8BN3,8BJQ,8BIP,7ZUX,7ZUW,7ZRS,7ZPQ,7NRD,7NRC,7N8B,7MPJ,7MPI,7B7D,6WOO,6TNU,6TB3,6T7T,6T4Q,6S47,6Q8Y,6OIG,6I7O,6GQV,6GQB,6GQ1,5TGM,5TGA,5TBW,5ON6,5OBM,5NDW,5NDV,5NDG,5MEI,5M1J,5LYB,5I4L,5FCJ,5FCI,5DGV,5DGF,5DGE,5DC3,5DAT,4V8Z,4V8Y,4U6F,4U56,4U55,4U53,4U52,4U51,4U50,4U4Z,4U4Y,4U4U,4U4R,4U4Q,4U4O,4U4N,4U3U,4U3N,4U3M,7ZS5,6R87,6R86,6R84,4V4B,4V7H Large ribosomal subunit protein eL19A RL19A_YEAST P0CX82 D6VPX3 P05735 122677 C[C@H]1C[C@@H](C(=O)[C@@H](C1)[C@@H](CC2CC(=O)NC(=O)C2)O)C InChI=1S/C15H23NO4/c1-8-3-9(2)15(20)11(4-8)12(17)5-10-6-13(18)16-14(19)7-10/h8-12,17H,3-7H2,1-2H3,(H,16,18,19) YPHMISFOHDHNIV-UHFFFAOYSA-N 50080528 Cycloheximid::3-((R)-2-((1S,3S,5S)-3,5-dimethyl-2-oxocyclohexyl)-2-hydroxyethyl)glutarimide::CHEMBL123292::cycloheximide::Zykloheximid::cid_6197::4-{(2R)-2-[(1S,3S,5S)-3,5-dimethyl-2-oxocyclohexyl]-2-hydroxyethyl}piperidine-2,6-dione::med.21724, Compound Cycloheximide 60S ribosomal protein L19-A Saccharomyces cerevisiae (strain ATCC 204508 / S288c) 644 PubChem 10.7270/Q2JQ0ZGP aid2740 PubChem, PC 4/1/2010 7/11/2011 Nmmlsc http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50080528 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4787&target=60S+ribosomal+protein+L19-A&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50080528&enzyme=60S+ribosomal+protein+L19-A&column=ki&startPg=0&Increment=50&submit=Search 3HE 4U3U,5GAK,5LKS,6HD7,6TNU,6Y0G,6Y2L,7N8B,7Q08,7R81,8BN3,8G6J,8IPA,8IPB,8T2X,8T2Y,8T2Z,8T30,8UT0,8UTI,9BH5,9CAI,9FQZ,9P7F,9P7G,9P7H,9P7I,9P7J,9P8I 6197 103980685 CHEMBL123292 C06685 1 MANLRTQKRLAASVVGVGKRKVWLDPNETSEIAQANSRNAIRKLVKNGTIVKKAVTVHSKSRTRAHAQSKREGRHSGYGKRKGTREARLPSQVVWIRRLRVLRRLLAKYRDAGKIDKHLYHVLYKESKGNAFKHKRALVEHIIQAKADAQREKALNEEAEARRLKNRAARDRRAQRVAEKRDALLKEDA 9R9P,9R9O,9PN5,9F9S,9DP7,9DOV,8Y0U,8V87,8T3F,8T3E,8T3D,8T3C,8T3B,8T3A,8T30,8T2Z,8T2Y,8T2X,8PNN,8PFR,8P9A,8P8U,8P8N,8P8M,8P85,8P4V,8K82,8K2D,8HFR,8EWC,8EWB,8EVT,8EVS,8EVR,8EVQ,8EVP,8EUB,8CMJ,8CKU,8CIV,8CGN,8CG8,8CF5,8CEH,8CDR,8CDL,8CCS,8AGZ,8AGX,8AGW,8AGV,8AGU,8AGT,8AAF,7ZW0,7Z34,7V08,7UQZ,7UQB,7UOO,7UG6,7U0H,7TOP,7TOO,7RR5,7R7A,7R72,7OHV,7OHR,7OHQ,7OH3,7OF1,7NAD,7NAC,7BTB,7BT6,7AZY,6Z6K,6Z6J,6YLY,6YLX,6YLH,6YLG,6XIR,6XIQ,6T83,6T7I,6SV4,6S05,6RZZ,6RI5,6QTZ,6QT0,6QIK,6N8L,6N8K,6N8J,6M62,6HHQ,6HD7,6FT6,6EM5,6ELZ,5MC6,5JUU,5JUT,5JUS,5JUP,5JUO,5JCS,5H4P,5GAK,5APO,5APN,4V91,4V8T,4V88,4V7R,4V7F,4V6I,3JCT,2WWB,2WWA,2WW9,8ZHC,8ZHB,8ZH3,8ZGY,8ZGR,8Z71,8Z70,8YLR,8YLD,8XU8,8UTI,8UT0,8BQX,8BQD,8BN3,8BJQ,8BIP,7ZUX,7ZUW,7ZRS,7ZPQ,7NRD,7NRC,7N8B,7MPJ,7MPI,7B7D,6WOO,6TNU,6TB3,6T7T,6T4Q,6S47,6Q8Y,6OIG,6I7O,6GQV,6GQB,6GQ1,5TGM,5TGA,5TBW,5ON6,5OBM,5NDW,5NDV,5NDG,5MEI,5M1J,5LYB,5I4L,5FCJ,5FCI,5DGV,5DGF,5DGE,5DC3,5DAT,4V8Z,4V8Y,4U6F,4U56,4U55,4U53,4U52,4U51,4U50,4U4Z,4U4Y,4U4U,4U4R,4U4Q,4U4O,4U4N,4U3U,4U3N,4U3M,7ZS5,6R87,6R86,6R84,4V4B,4V7H Large ribosomal subunit protein eL19A RL19A_YEAST P0CX82 D6VPX3 P05735 51250464 CNc1cc(nc(n1)N)N2CCCCC2 InChI=1S/C10H17N5/c1-12-8-7-9(14-10(11)13-8)15-5-3-2-4-6-15/h7H,2-6H2,1H3,(H3,11,12,13,14) WOSMHMANFDUDQJ-UHFFFAOYSA-N 50511439 CHEMBL4565830 Oxidized purine nucleoside triphosphate hydrolase Homo sapiens 0.800000 ChEMBL 10.1021/acsmedchemlett.9b00420 10.7270/Q2PV6PPZ 32184970 Farand, J; Kropf, JE; Blomgren, P; Xu, J; Schmitt, AC; Newby, ZE; Wang, T; Murakami, E; Barauskas, O; Sudhamsu, J; Feng, JY; Niedziela-Majka, A; Schultz, BE; Schwartz, K; Viatchenko-Karpinski, S; Kornyeyev, D; Kashishian, A; Fan, P; Chen, X; Lansdon, EB; Ports, MO; Currie, KS; Watkins, WJ; Notte, GT 3/12/2020 2/20/2021 Gilead Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50511439 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=9756&target=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50511439&enzyme=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search CJU 6JVR 17773877 440720021 1 MGASRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGARRELQEESGLTVDALHKVGQIVFEFVGEPELMDVHVFCTDSIQGTPVESDEMRPCWFQLDQIPFKDMWPDDSYWFPLLLQKKKFHGYFKFQGQDTILDYTLREVDTV 3Q93,6GLE,6EQ7,6EQ6,6EQ5,6EQ4,6EQ3,6EQ2,5ANT,5ANS,9FL6,5ANW,5ANV,5ANU,4C9X,4C9W,9GQL,6JVT,6JVS,6JVR,6JVQ,6JVP,6JVN,6JVM,6JVL,6JVK,6JVJ,6JVI,6JVH,6JVG,6JVF,5FSO,5FSN,5FSM,5FSL,5FSI,3ZR1,3ZR0,3WHW,1IRY,7N13,7N03,7ESF,8A3A,8A34,8A0T,8A0S,8A07,6US4,6US3,6US2,6F23,6F22,6F20,6F1X,5OTM,5NHY,5NGT,5NGS,5NGR,5FSK,4N1T,6QVO,4N1U,6JVO,6IMZ,6AA5,6AA4,6AA3,5MZF Oxidized purine nucleoside triphosphate hydrolase 8ODP_HUMAN P36639 A4D205 Q6LES7 Q6P0Y6 Q7Z7N6 Q8IV95 Q9UBM0 Q9UBM9 51571046 Nc1nc(NC2CC2)cc(n1)N1CCCCC1 InChI=1S/C12H19N5/c13-12-15-10(14-9-4-5-9)8-11(16-12)17-6-2-1-3-7-17/h8-9H,1-7H2,(H3,13,14,15,16) KEJKDPAZBYTTRQ-UHFFFAOYSA-N 50631857 CHEMBL5419782 Oxidized purine nucleoside triphosphate hydrolase Homo sapiens 6.0 ChEMBL 10.1021/acs.jmedchem.2c01827 10.7270/Q2VT1XJC 36622056 Walsh, L; Erlanson, DA; de Esch, IJP; Jahnke, W; Woodhead, A; Wren, E 1/26/2023 12/21/2024 Astex Pharmaceuticals http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50631857 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=9756&target=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50631857&enzyme=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search CJ9 6JVP 154815497 505036191 1 MGASRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGARRELQEESGLTVDALHKVGQIVFEFVGEPELMDVHVFCTDSIQGTPVESDEMRPCWFQLDQIPFKDMWPDDSYWFPLLLQKKKFHGYFKFQGQDTILDYTLREVDTV 3Q93,6GLE,6EQ7,6EQ6,6EQ5,6EQ4,6EQ3,6EQ2,5ANT,5ANS,5ANW,5ANV,5ANU,4C9X,4C9W,6JVT,6JVS,6JVR,6JVQ,6JVP,6JVN,6JVM,6JVL,6JVK,6JVJ,6JVI,6JVH,6JVG,6JVF,5FSO,5FSN,5FSM,5FSL,5FSI,3ZR1,3ZR0,3WHW,1IRY,7N13,7N03,7ESF,8A3A,8A34,8A0T,8A0S,8A07,6US4,6US3,6US2,6F23,6F22,6F20,6F1X,5OTM,5NHY,5NGT,5NGS,5NGR,5FSK,4N1T,6QVO,4N1U,6JVO,6IMZ,6AA5,6AA4,6AA3,5MZF Oxidized purine nucleoside triphosphate hydrolase 8ODP_HUMAN P36639 A4D205 Q6LES7 Q6P0Y6 Q7Z7N6 Q8IV95 Q9UBM0 Q9UBM9 51571045 CCc1c(C)nc(N)nc1N1CCOCC1 InChI=1S/C11H18N4O/c1-3-9-8(2)13-11(12)14-10(9)15-4-6-16-7-5-15/h3-7H2,1-2H3,(H2,12,13,14) VYZIWKYGVDQKSB-UHFFFAOYSA-N 50631856 CHEMBL4938738 Oxidized purine nucleoside triphosphate hydrolase Homo sapiens 1500 ChEMBL 10.1021/acs.jmedchem.2c01827 10.7270/Q2VT1XJC 36622056 Walsh, L; Erlanson, DA; de Esch, IJP; Jahnke, W; Woodhead, A; Wren, E 1/26/2023 12/21/2024 Astex Pharmaceuticals http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50631856 http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=9756&target=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50631856&enzyme=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search 95F 6JVG 879218 505036190 1 MGASRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGARRELQEESGLTVDALHKVGQIVFEFVGEPELMDVHVFCTDSIQGTPVESDEMRPCWFQLDQIPFKDMWPDDSYWFPLLLQKKKFHGYFKFQGQDTILDYTLREVDTV 3Q93,6GLE,6EQ7,6EQ6,6EQ5,6EQ4,6EQ3,6EQ2,5ANT,5ANS,5ANW,5ANV,5ANU,4C9X,4C9W,6JVT,6JVS,6JVR,6JVQ,6JVP,6JVN,6JVM,6JVL,6JVK,6JVJ,6JVI,6JVH,6JVG,6JVF,5FSO,5FSN,5FSM,5FSL,5FSI,3ZR1,3ZR0,3WHW,1IRY,7N13,7N03,7ESF,8A3A,8A34,8A0T,8A0S,8A07,6US4,6US3,6US2,6F23,6F22,6F20,6F1X,5OTM,5NHY,5NGT,5NGS,5NGR,5FSK,4N1T,6QVO,4N1U,6JVO,6IMZ,6AA5,6AA4,6AA3,5MZF Oxidized purine nucleoside triphosphate hydrolase 8ODP_HUMAN P36639 A4D205 Q6LES7 Q6P0Y6 Q7Z7N6 Q8IV95 Q9UBM0 Q9UBM9 51354949 CCOCc1nc2c(n1CC(C)(C)O)c3ccccc3nc2N InChI=1S/C17H22N4O2/c1-4-23-9-13-20-14-15(21(13)10-17(2,3)22)11-7-5-6-8-12(11)19-16(14)18/h5-8,22H,4,9-10H2,1-3H3,(H2,18,19) BXNMTOQRYBFHNZ-UHFFFAOYSA-N 50241029 1-[4-amino-2-(ethoxymethyl)-1H-imidazo[4,5-c]quinolin-1-yl]-2-methylpropan-2-ol::R 848::R-848::Resiquimod::CHEMBL383322::US9334268, resiquimod::US10457681, Compound Resiquimod::US10508115, Compound Resiquimod::US10487084, Compound Resiquimod::US10919895, Resiquimod::US10981914, Compound Resiquimod Oxidized purine nucleoside triphosphate hydrolase Homo sapiens 2056 ChEMBL 10.1021/acs.jmedchem.5b01760 10.7270/Q2TB1BHR 26878898 Kettle, JG; Alwan, H; Bista, M; Breed, J; Davies, NL; Eckersley, K; Fillery, S; Foote, KM; Goodwin, L; Jones, DR; Käck, H; Lau, A; Nissink, JW; Read, J; Scott, JS; Taylor, B; Walker, G; Wissler, L; Wylot, M 3/24/2016 3/22/2022 Astrazeneca http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50241029 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=9756&target=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50241029&enzyme=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search RX8 3W3L,3W3M,3W3N,5ANS,5GMH 159603 104098572 CHEMBL383322 1 MGASRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGARRELQEESGLTVDALHKVGQIVFEFVGEPELMDVHVFCTDSIQGTPVESDEMRPCWFQLDQIPFKDMWPDDSYWFPLLLQKKKFHGYFKFQGQDTILDYTLREVDTV 3Q93,6GLE,6EQ7,6EQ6,6EQ5,6EQ4,6EQ3,6EQ2,5ANT,5ANS,9FL6,5ANW,5ANV,5ANU,4C9X,4C9W,9GQL,6JVT,6JVS,6JVR,6JVQ,6JVP,6JVN,6JVM,6JVL,6JVK,6JVJ,6JVI,6JVH,6JVG,6JVF,5FSO,5FSN,5FSM,5FSL,5FSI,3ZR1,3ZR0,3WHW,1IRY,7N13,7N03,7ESF,9QUK,9QUH,9QUE,8A3A,8A34,8A0T,8A0S,8A07,6US4,6US3,6US2,6F23,6F22,6F20,6F1X,5OTM,5NHY,5NGT,5NGS,5NGR,5FSK,4N1T,6QVO,4N1U,6JVO,6IMZ,6AA5,6AA4,6AA3,5MZF Oxidized purine nucleoside triphosphate hydrolase 8ODP_HUMAN P36639 A4D205 Q6LES7 Q6P0Y6 Q7Z7N6 Q8IV95 Q9UBM0 Q9UBM9 51354913 CNc1c2c(nc(n1)OCCOC)N(C(=O)N2)Cc3ccccc3 InChI=1S/C16H19N5O3/c1-17-13-12-14(20-15(19-13)24-9-8-23-2)21(16(22)18-12)10-11-6-4-3-5-7-11/h3-7H,8-10H2,1-2H3,(H,18,22)(H,17,19,20) OSILWVXKFRDCIL-UHFFFAOYSA-N 50548111 CHEMBL4763327 Oxidized purine nucleoside triphosphate hydrolase Homo sapiens 1500 ChEMBL 10.1021/acs.jmedchem.5b01760 10.7270/Q2TB1BHR 26878898 Kettle, JG; Alwan, H; Bista, M; Breed, J; Davies, NL; Eckersley, K; Fillery, S; Foote, KM; Goodwin, L; Jones, DR; Käck, H; Lau, A; Nissink, JW; Read, J; Scott, JS; Taylor, B; Walker, G; Wissler, L; Wylot, M 3/24/2016 3/22/2022 Astrazeneca http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50548111 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=9756&target=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50548111&enzyme=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search RJE 5ANT 118704898 461678451 1 MGASRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGARRELQEESGLTVDALHKVGQIVFEFVGEPELMDVHVFCTDSIQGTPVESDEMRPCWFQLDQIPFKDMWPDDSYWFPLLLQKKKFHGYFKFQGQDTILDYTLREVDTV 3Q93,6GLE,6EQ7,6EQ6,6EQ5,6EQ4,6EQ3,6EQ2,5ANT,5ANS,9FL6,5ANW,5ANV,5ANU,4C9X,4C9W,9GQL,6JVT,6JVS,6JVR,6JVQ,6JVP,6JVN,6JVM,6JVL,6JVK,6JVJ,6JVI,6JVH,6JVG,6JVF,5FSO,5FSN,5FSM,5FSL,5FSI,3ZR1,3ZR0,3WHW,1IRY,7N13,7N03,7ESF,8A3A,8A34,8A0T,8A0S,8A07,6US4,6US3,6US2,6F23,6F22,6F20,6F1X,5OTM,5NHY,5NGT,5NGS,5NGR,5FSK,4N1T,6QVO,4N1U,6JVO,6IMZ,6AA5,6AA4,6AA3,5MZF Oxidized purine nucleoside triphosphate hydrolase 8ODP_HUMAN P36639 A4D205 Q6LES7 Q6P0Y6 Q7Z7N6 Q8IV95 Q9UBM0 Q9UBM9 51354921 CNc1c2c(nc(n1)OCCOC)N(C(=O)N2)Cc3ccccc3 InChI=1S/C16H19N5O3/c1-17-13-12-14(20-15(19-13)24-9-8-23-2)21(16(22)18-12)10-11-6-4-3-5-7-11/h3-7H,8-10H2,1-2H3,(H,18,22)(H,17,19,20) OSILWVXKFRDCIL-UHFFFAOYSA-N 50548111 CHEMBL4763327 Oxidized purine nucleoside triphosphate hydrolase Homo sapiens 440 ChEMBL 10.1021/acs.jmedchem.5b01760 10.7270/Q2TB1BHR 26878898 Kettle, JG; Alwan, H; Bista, M; Breed, J; Davies, NL; Eckersley, K; Fillery, S; Foote, KM; Goodwin, L; Jones, DR; Käck, H; Lau, A; Nissink, JW; Read, J; Scott, JS; Taylor, B; Walker, G; Wissler, L; Wylot, M 3/24/2016 3/22/2022 Astrazeneca http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50548111 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=9756&target=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50548111&enzyme=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search RJE 5ANT 118704898 461678451 1 MGASRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGARRELQEESGLTVDALHKVGQIVFEFVGEPELMDVHVFCTDSIQGTPVESDEMRPCWFQLDQIPFKDMWPDDSYWFPLLLQKKKFHGYFKFQGQDTILDYTLREVDTV 3Q93,6GLE,6EQ7,6EQ6,6EQ5,6EQ4,6EQ3,6EQ2,5ANT,5ANS,9FL6,5ANW,5ANV,5ANU,4C9X,4C9W,9GQL,6JVT,6JVS,6JVR,6JVQ,6JVP,6JVN,6JVM,6JVL,6JVK,6JVJ,6JVI,6JVH,6JVG,6JVF,5FSO,5FSN,5FSM,5FSL,5FSI,3ZR1,3ZR0,3WHW,1IRY,7N13,7N03,7ESF,8A3A,8A34,8A0T,8A0S,8A07,6US4,6US3,6US2,6F23,6F22,6F20,6F1X,5OTM,5NHY,5NGT,5NGS,5NGR,5FSK,4N1T,6QVO,4N1U,6JVO,6IMZ,6AA5,6AA4,6AA3,5MZF Oxidized purine nucleoside triphosphate hydrolase 8ODP_HUMAN P36639 A4D205 Q6LES7 Q6P0Y6 Q7Z7N6 Q8IV95 Q9UBM0 Q9UBM9 51354947 CNc1c2c(nc(n1)OCCOC)N(C(=O)N2)Cc3ccccc3 InChI=1S/C16H19N5O3/c1-17-13-12-14(20-15(19-13)24-9-8-23-2)21(16(22)18-12)10-11-6-4-3-5-7-11/h3-7H,8-10H2,1-2H3,(H,18,22)(H,17,19,20) OSILWVXKFRDCIL-UHFFFAOYSA-N 50548111 CHEMBL4763327 Oxidized purine nucleoside triphosphate hydrolase Homo sapiens 536 ChEMBL 10.1021/acs.jmedchem.5b01760 10.7270/Q2TB1BHR 26878898 Kettle, JG; Alwan, H; Bista, M; Breed, J; Davies, NL; Eckersley, K; Fillery, S; Foote, KM; Goodwin, L; Jones, DR; Käck, H; Lau, A; Nissink, JW; Read, J; Scott, JS; Taylor, B; Walker, G; Wissler, L; Wylot, M 3/24/2016 3/22/2022 Astrazeneca http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50548111 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=9756&target=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50548111&enzyme=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search RJE 5ANT 118704898 461678451 1 MGASRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGARRELQEESGLTVDALHKVGQIVFEFVGEPELMDVHVFCTDSIQGTPVESDEMRPCWFQLDQIPFKDMWPDDSYWFPLLLQKKKFHGYFKFQGQDTILDYTLREVDTV 3Q93,6GLE,6EQ7,6EQ6,6EQ5,6EQ4,6EQ3,6EQ2,5ANT,5ANS,9FL6,5ANW,5ANV,5ANU,4C9X,4C9W,9GQL,6JVT,6JVS,6JVR,6JVQ,6JVP,6JVN,6JVM,6JVL,6JVK,6JVJ,6JVI,6JVH,6JVG,6JVF,5FSO,5FSN,5FSM,5FSL,5FSI,3ZR1,3ZR0,3WHW,1IRY,7N13,7N03,7ESF,8A3A,8A34,8A0T,8A0S,8A07,6US4,6US3,6US2,6F23,6F22,6F20,6F1X,5OTM,5NHY,5NGT,5NGS,5NGR,5FSK,4N1T,6QVO,4N1U,6JVO,6IMZ,6AA5,6AA4,6AA3,5MZF Oxidized purine nucleoside triphosphate hydrolase 8ODP_HUMAN P36639 A4D205 Q6LES7 Q6P0Y6 Q7Z7N6 Q8IV95 Q9UBM0 Q9UBM9 50489900 CNc1c2c3nc(n1)OCCOCCOc4cccc(c4)CN3C(=O)N2 InChI=1S/C17H19N5O4/c1-18-14-13-15-21-16(20-14)26-8-6-24-5-7-25-12-4-2-3-11(9-12)10-22(15)17(23)19-13/h2-4,9H,5-8,10H2,1H3,(H,19,23)(H,18,20,21) OJHLJXROBUJUPQ-UHFFFAOYSA-N 50162075 CHEMBL3794167 Oxidized purine nucleoside triphosphate hydrolase Homo sapiens 0.500000 ChEMBL 10.1021/acs.jmedchem.6b00283 10.7270/Q2VX0JDP 26924380 Papeo, G 3/24/2016 8/7/2017 Nerviano Medical Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50162075 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=9756&target=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50162075&enzyme=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search 58T 5ANU 118704899 104048284 CHEMBL3794167 1 MGASRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGARRELQEESGLTVDALHKVGQIVFEFVGEPELMDVHVFCTDSIQGTPVESDEMRPCWFQLDQIPFKDMWPDDSYWFPLLLQKKKFHGYFKFQGQDTILDYTLREVDTV 3Q93,6GLE,6EQ7,6EQ6,6EQ5,6EQ4,6EQ3,6EQ2,5ANT,5ANS,9FL6,5ANW,5ANV,5ANU,4C9X,4C9W,9GQL,6JVT,6JVS,6JVR,6JVQ,6JVP,6JVN,6JVM,6JVL,6JVK,6JVJ,6JVI,6JVH,6JVG,6JVF,5FSO,5FSN,5FSM,5FSL,5FSI,3ZR1,3ZR0,3WHW,1IRY,7N13,7N03,7ESF,8A3A,8A34,8A0T,8A0S,8A07,6US4,6US3,6US2,6F23,6F22,6F20,6F1X,5OTM,5NHY,5NGT,5NGS,5NGR,5FSK,4N1T,6QVO,4N1U,6JVO,6IMZ,6AA5,6AA4,6AA3,5MZF Oxidized purine nucleoside triphosphate hydrolase 8ODP_HUMAN P36639 A4D205 Q6LES7 Q6P0Y6 Q7Z7N6 Q8IV95 Q9UBM0 Q9UBM9 51354911 CNc1c2c3nc(n1)OCCOCCOc4cccc(c4)CN3C(=O)N2 InChI=1S/C17H19N5O4/c1-18-14-13-15-21-16(20-14)26-8-6-24-5-7-25-12-4-2-3-11(9-12)10-22(15)17(23)19-13/h2-4,9H,5-8,10H2,1H3,(H,19,23)(H,18,20,21) OJHLJXROBUJUPQ-UHFFFAOYSA-N 50162075 CHEMBL3794167 Oxidized purine nucleoside triphosphate hydrolase Homo sapiens 3.0 ChEMBL 10.1021/acs.jmedchem.5b01760 10.7270/Q2TB1BHR 26878898 Kettle, JG; Alwan, H; Bista, M; Breed, J; Davies, NL; Eckersley, K; Fillery, S; Foote, KM; Goodwin, L; Jones, DR; Käck, H; Lau, A; Nissink, JW; Read, J; Scott, JS; Taylor, B; Walker, G; Wissler, L; Wylot, M 3/24/2016 3/22/2022 Astrazeneca http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50162075 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=9756&target=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50162075&enzyme=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search 58T 5ANU 118704899 104048284 CHEMBL3794167 1 MGASRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGARRELQEESGLTVDALHKVGQIVFEFVGEPELMDVHVFCTDSIQGTPVESDEMRPCWFQLDQIPFKDMWPDDSYWFPLLLQKKKFHGYFKFQGQDTILDYTLREVDTV 3Q93,6GLE,6EQ7,6EQ6,6EQ5,6EQ4,6EQ3,6EQ2,5ANT,5ANS,9FL6,5ANW,5ANV,5ANU,4C9X,4C9W,9GQL,6JVT,6JVS,6JVR,6JVQ,6JVP,6JVN,6JVM,6JVL,6JVK,6JVJ,6JVI,6JVH,6JVG,6JVF,5FSO,5FSN,5FSM,5FSL,5FSI,3ZR1,3ZR0,3WHW,1IRY,7N13,7N03,7ESF,8A3A,8A34,8A0T,8A0S,8A07,6US4,6US3,6US2,6F23,6F22,6F20,6F1X,5OTM,5NHY,5NGT,5NGS,5NGR,5FSK,4N1T,6QVO,4N1U,6JVO,6IMZ,6AA5,6AA4,6AA3,5MZF Oxidized purine nucleoside triphosphate hydrolase 8ODP_HUMAN P36639 A4D205 Q6LES7 Q6P0Y6 Q7Z7N6 Q8IV95 Q9UBM0 Q9UBM9 51354919 CNc1c2c3nc(n1)OCCOCCOc4cccc(c4)CN3C(=O)N2 InChI=1S/C17H19N5O4/c1-18-14-13-15-21-16(20-14)26-8-6-24-5-7-25-12-4-2-3-11(9-12)10-22(15)17(23)19-13/h2-4,9H,5-8,10H2,1H3,(H,19,23)(H,18,20,21) OJHLJXROBUJUPQ-UHFFFAOYSA-N 50162075 CHEMBL3794167 Oxidized purine nucleoside triphosphate hydrolase Homo sapiens 0.400000 ChEMBL 10.1021/acs.jmedchem.5b01760 10.7270/Q2TB1BHR 26878898 Kettle, JG; Alwan, H; Bista, M; Breed, J; Davies, NL; Eckersley, K; Fillery, S; Foote, KM; Goodwin, L; Jones, DR; Käck, H; Lau, A; Nissink, JW; Read, J; Scott, JS; Taylor, B; Walker, G; Wissler, L; Wylot, M 3/24/2016 3/22/2022 Astrazeneca http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50162075 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=9756&target=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50162075&enzyme=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search 58T 5ANU 118704899 104048284 CHEMBL3794167 1 MGASRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGARRELQEESGLTVDALHKVGQIVFEFVGEPELMDVHVFCTDSIQGTPVESDEMRPCWFQLDQIPFKDMWPDDSYWFPLLLQKKKFHGYFKFQGQDTILDYTLREVDTV 3Q93,6GLE,6EQ7,6EQ6,6EQ5,6EQ4,6EQ3,6EQ2,5ANT,5ANS,9FL6,5ANW,5ANV,5ANU,4C9X,4C9W,9GQL,6JVT,6JVS,6JVR,6JVQ,6JVP,6JVN,6JVM,6JVL,6JVK,6JVJ,6JVI,6JVH,6JVG,6JVF,5FSO,5FSN,5FSM,5FSL,5FSI,3ZR1,3ZR0,3WHW,1IRY,7N13,7N03,7ESF,8A3A,8A34,8A0T,8A0S,8A07,6US4,6US3,6US2,6F23,6F22,6F20,6F1X,5OTM,5NHY,5NGT,5NGS,5NGR,5FSK,4N1T,6QVO,4N1U,6JVO,6IMZ,6AA5,6AA4,6AA3,5MZF Oxidized purine nucleoside triphosphate hydrolase 8ODP_HUMAN P36639 A4D205 Q6LES7 Q6P0Y6 Q7Z7N6 Q8IV95 Q9UBM0 Q9UBM9 51354944 CNc1c2c3nc(n1)OCCOCCOc4cccc(c4)CN3C(=O)N2 InChI=1S/C17H19N5O4/c1-18-14-13-15-21-16(20-14)26-8-6-24-5-7-25-12-4-2-3-11(9-12)10-22(15)17(23)19-13/h2-4,9H,5-8,10H2,1H3,(H,19,23)(H,18,20,21) OJHLJXROBUJUPQ-UHFFFAOYSA-N 50162075 CHEMBL3794167 Oxidized purine nucleoside triphosphate hydrolase Homo sapiens 0.500000 ChEMBL 10.1021/acs.jmedchem.5b01760 10.7270/Q2TB1BHR 26878898 Kettle, JG; Alwan, H; Bista, M; Breed, J; Davies, NL; Eckersley, K; Fillery, S; Foote, KM; Goodwin, L; Jones, DR; Käck, H; Lau, A; Nissink, JW; Read, J; Scott, JS; Taylor, B; Walker, G; Wissler, L; Wylot, M 3/24/2016 3/22/2022 Astrazeneca http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50162075 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=9756&target=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50162075&enzyme=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search 58T 5ANU 118704899 104048284 CHEMBL3794167 1 MGASRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGARRELQEESGLTVDALHKVGQIVFEFVGEPELMDVHVFCTDSIQGTPVESDEMRPCWFQLDQIPFKDMWPDDSYWFPLLLQKKKFHGYFKFQGQDTILDYTLREVDTV 3Q93,6GLE,6EQ7,6EQ6,6EQ5,6EQ4,6EQ3,6EQ2,5ANT,5ANS,9FL6,5ANW,5ANV,5ANU,4C9X,4C9W,9GQL,6JVT,6JVS,6JVR,6JVQ,6JVP,6JVN,6JVM,6JVL,6JVK,6JVJ,6JVI,6JVH,6JVG,6JVF,5FSO,5FSN,5FSM,5FSL,5FSI,3ZR1,3ZR0,3WHW,1IRY,7N13,7N03,7ESF,8A3A,8A34,8A0T,8A0S,8A07,6US4,6US3,6US2,6F23,6F22,6F20,6F1X,5OTM,5NHY,5NGT,5NGS,5NGR,5FSK,4N1T,6QVO,4N1U,6JVO,6IMZ,6AA5,6AA4,6AA3,5MZF Oxidized purine nucleoside triphosphate hydrolase 8ODP_HUMAN P36639 A4D205 Q6LES7 Q6P0Y6 Q7Z7N6 Q8IV95 Q9UBM0 Q9UBM9 51354910 CNC(=O)c1cnc2cc(c(cc2c1Nc3ccc(cc3F)Cl)OC)OC InChI=1S/C19H17ClFN3O3/c1-22-19(25)12-9-23-15-8-17(27-3)16(26-2)7-11(15)18(12)24-14-5-4-10(20)6-13(14)21/h4-9H,1-3H3,(H,22,25)(H,23,24) MXBCVSLLTIRSIL-UHFFFAOYSA-N 50548109 CHEMBL4783492 Oxidized purine nucleoside triphosphate hydrolase Homo sapiens 7.0 ChEMBL 10.1021/acs.jmedchem.5b01760 10.7270/Q2TB1BHR 26878898 Kettle, JG; Alwan, H; Bista, M; Breed, J; Davies, NL; Eckersley, K; Fillery, S; Foote, KM; Goodwin, L; Jones, DR; Käck, H; Lau, A; Nissink, JW; Read, J; Scott, JS; Taylor, B; Walker, G; Wissler, L; Wylot, M 3/24/2016 3/22/2022 Astrazeneca http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50548109 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=9756&target=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50548109&enzyme=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search RGJ 5ANV 118704900 461678449 1 MGASRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGARRELQEESGLTVDALHKVGQIVFEFVGEPELMDVHVFCTDSIQGTPVESDEMRPCWFQLDQIPFKDMWPDDSYWFPLLLQKKKFHGYFKFQGQDTILDYTLREVDTV 3Q93,6GLE,6EQ7,6EQ6,6EQ5,6EQ4,6EQ3,6EQ2,5ANT,5ANS,9FL6,5ANW,5ANV,5ANU,4C9X,4C9W,9GQL,6JVT,6JVS,6JVR,6JVQ,6JVP,6JVN,6JVM,6JVL,6JVK,6JVJ,6JVI,6JVH,6JVG,6JVF,5FSO,5FSN,5FSM,5FSL,5FSI,3ZR1,3ZR0,3WHW,1IRY,7N13,7N03,7ESF,8A3A,8A34,8A0T,8A0S,8A07,6US4,6US3,6US2,6F23,6F22,6F20,6F1X,5OTM,5NHY,5NGT,5NGS,5NGR,5FSK,4N1T,6QVO,4N1U,6JVO,6IMZ,6AA5,6AA4,6AA3,5MZF Oxidized purine nucleoside triphosphate hydrolase 8ODP_HUMAN P36639 A4D205 Q6LES7 Q6P0Y6 Q7Z7N6 Q8IV95 Q9UBM0 Q9UBM9 51354918 CNC(=O)c1cnc2cc(c(cc2c1Nc3ccc(cc3F)Cl)OC)OC InChI=1S/C19H17ClFN3O3/c1-22-19(25)12-9-23-15-8-17(27-3)16(26-2)7-11(15)18(12)24-14-5-4-10(20)6-13(14)21/h4-9H,1-3H3,(H,22,25)(H,23,24) MXBCVSLLTIRSIL-UHFFFAOYSA-N 50548109 CHEMBL4783492 Oxidized purine nucleoside triphosphate hydrolase Homo sapiens 0.500000 ChEMBL 10.1021/acs.jmedchem.5b01760 10.7270/Q2TB1BHR 26878898 Kettle, JG; Alwan, H; Bista, M; Breed, J; Davies, NL; Eckersley, K; Fillery, S; Foote, KM; Goodwin, L; Jones, DR; Käck, H; Lau, A; Nissink, JW; Read, J; Scott, JS; Taylor, B; Walker, G; Wissler, L; Wylot, M 3/24/2016 3/22/2022 Astrazeneca http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50548109 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=9756&target=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50548109&enzyme=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search RGJ 5ANV 118704900 461678449 1 MGASRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGARRELQEESGLTVDALHKVGQIVFEFVGEPELMDVHVFCTDSIQGTPVESDEMRPCWFQLDQIPFKDMWPDDSYWFPLLLQKKKFHGYFKFQGQDTILDYTLREVDTV 3Q93,6GLE,6EQ7,6EQ6,6EQ5,6EQ4,6EQ3,6EQ2,5ANT,5ANS,9FL6,5ANW,5ANV,5ANU,4C9X,4C9W,9GQL,6JVT,6JVS,6JVR,6JVQ,6JVP,6JVN,6JVM,6JVL,6JVK,6JVJ,6JVI,6JVH,6JVG,6JVF,5FSO,5FSN,5FSM,5FSL,5FSI,3ZR1,3ZR0,3WHW,1IRY,7N13,7N03,7ESF,8A3A,8A34,8A0T,8A0S,8A07,6US4,6US3,6US2,6F23,6F22,6F20,6F1X,5OTM,5NHY,5NGT,5NGS,5NGR,5FSK,4N1T,6QVO,4N1U,6JVO,6IMZ,6AA5,6AA4,6AA3,5MZF Oxidized purine nucleoside triphosphate hydrolase 8ODP_HUMAN P36639 A4D205 Q6LES7 Q6P0Y6 Q7Z7N6 Q8IV95 Q9UBM0 Q9UBM9 51354938 CNC(=O)c1cnc2cc(c(cc2c1Nc3ccc(cc3F)Cl)OC)OC InChI=1S/C19H17ClFN3O3/c1-22-19(25)12-9-23-15-8-17(27-3)16(26-2)7-11(15)18(12)24-14-5-4-10(20)6-13(14)21/h4-9H,1-3H3,(H,22,25)(H,23,24) MXBCVSLLTIRSIL-UHFFFAOYSA-N 50548109 CHEMBL4783492 Oxidized purine nucleoside triphosphate hydrolase Homo sapiens 0.900000 ChEMBL 10.1021/acs.jmedchem.5b01760 10.7270/Q2TB1BHR 26878898 Kettle, JG; Alwan, H; Bista, M; Breed, J; Davies, NL; Eckersley, K; Fillery, S; Foote, KM; Goodwin, L; Jones, DR; Käck, H; Lau, A; Nissink, JW; Read, J; Scott, JS; Taylor, B; Walker, G; Wissler, L; Wylot, M 3/24/2016 3/22/2022 Astrazeneca http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50548109 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=9756&target=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50548109&enzyme=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search RGJ 5ANV 118704900 461678449 1 MGASRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGARRELQEESGLTVDALHKVGQIVFEFVGEPELMDVHVFCTDSIQGTPVESDEMRPCWFQLDQIPFKDMWPDDSYWFPLLLQKKKFHGYFKFQGQDTILDYTLREVDTV 3Q93,6GLE,6EQ7,6EQ6,6EQ5,6EQ4,6EQ3,6EQ2,5ANT,5ANS,9FL6,5ANW,5ANV,5ANU,4C9X,4C9W,9GQL,6JVT,6JVS,6JVR,6JVQ,6JVP,6JVN,6JVM,6JVL,6JVK,6JVJ,6JVI,6JVH,6JVG,6JVF,5FSO,5FSN,5FSM,5FSL,5FSI,3ZR1,3ZR0,3WHW,1IRY,7N13,7N03,7ESF,8A3A,8A34,8A0T,8A0S,8A07,6US4,6US3,6US2,6F23,6F22,6F20,6F1X,5OTM,5NHY,5NGT,5NGS,5NGR,5FSK,4N1T,6QVO,4N1U,6JVO,6IMZ,6AA5,6AA4,6AA3,5MZF Oxidized purine nucleoside triphosphate hydrolase 8ODP_HUMAN P36639 A4D205 Q6LES7 Q6P0Y6 Q7Z7N6 Q8IV95 Q9UBM0 Q9UBM9 50804969 CCNC(=O)c1cc2c(ccnc2[nH]1)N3CCOC[C@@H]3C InChI=1S/C15H20N4O2/c1-3-16-15(20)12-8-11-13(4-5-17-14(11)18-12)19-6-7-21-9-10(19)2/h4-5,8,10H,3,6-7,9H2,1-2H3,(H,16,20)(H,17,18) RPMGXDCRCWWCRY-UHFFFAOYSA-N 50255583 CHEMBL4096813 Oxidized purine nucleoside triphosphate hydrolase Homo sapiens 0.800000 ChEMBL 10.1021/acs.jmedchem.7b01884 10.7270/Q25D8V9Q 29485874 Rahm, F; Viklund, J; Trésaugues, L; Ellermann, M; Giese, A; Ericsson, U; Forsblom, R; Ginman, T; Günther, J; Hallberg, K; Lindström, J; Persson, LB; Silvander, C; Talagas, A; Díaz-Sáez, L; Fedorov, O; Huber, KVM; Panagakou, I; Siejka, P; Gorjánácz, M; Bauser, M; Andersson, M 3/22/2018 12/14/2019 Sprint Bioscience http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50255583 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=9756&target=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50255583&enzyme=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search 8XT 5NHY 129012086 402360383 1 MGASRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGARRELQEESGLTVDALHKVGQIVFEFVGEPELMDVHVFCTDSIQGTPVESDEMRPCWFQLDQIPFKDMWPDDSYWFPLLLQKKKFHGYFKFQGQDTILDYTLREVDTV 3Q93,6GLE,6EQ7,6EQ6,6EQ5,6EQ4,6EQ3,6EQ2,5ANT,5ANS,9FL6,5ANW,5ANV,5ANU,4C9X,4C9W,9GQL,6JVT,6JVS,6JVR,6JVQ,6JVP,6JVN,6JVM,6JVL,6JVK,6JVJ,6JVI,6JVH,6JVG,6JVF,5FSO,5FSN,5FSM,5FSL,5FSI,3ZR1,3ZR0,3WHW,1IRY,7N13,7N03,7ESF,8A3A,8A34,8A0T,8A0S,8A07,6US4,6US3,6US2,6F23,6F22,6F20,6F1X,5OTM,5NHY,5NGT,5NGS,5NGR,5FSK,4N1T,6QVO,4N1U,6JVO,6IMZ,6AA5,6AA4,6AA3,5MZF Oxidized purine nucleoside triphosphate hydrolase 8ODP_HUMAN P36639 A4D205 Q6LES7 Q6P0Y6 Q7Z7N6 Q8IV95 Q9UBM0 Q9UBM9 51250480 CCNC(=O)c1cc2c(ccnc2[nH]1)N3CCOC[C@@H]3C InChI=1S/C15H20N4O2/c1-3-16-15(20)12-8-11-13(4-5-17-14(11)18-12)19-6-7-21-9-10(19)2/h4-5,8,10H,3,6-7,9H2,1-2H3,(H,16,20)(H,17,18) RPMGXDCRCWWCRY-UHFFFAOYSA-N 50255583 CHEMBL4096813 Oxidized purine nucleoside triphosphate hydrolase Homo sapiens 2.3 ChEMBL 10.1021/acsmedchemlett.9b00420 10.7270/Q2PV6PPZ 32184970 Farand, J; Kropf, JE; Blomgren, P; Xu, J; Schmitt, AC; Newby, ZE; Wang, T; Murakami, E; Barauskas, O; Sudhamsu, J; Feng, JY; Niedziela-Majka, A; Schultz, BE; Schwartz, K; Viatchenko-Karpinski, S; Kornyeyev, D; Kashishian, A; Fan, P; Chen, X; Lansdon, EB; Ports, MO; Currie, KS; Watkins, WJ; Notte, GT 3/12/2020 2/20/2021 Gilead Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50255583 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=9756&target=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50255583&enzyme=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search 8XT 5NHY 129012086 402360383 1 MGASRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGARRELQEESGLTVDALHKVGQIVFEFVGEPELMDVHVFCTDSIQGTPVESDEMRPCWFQLDQIPFKDMWPDDSYWFPLLLQKKKFHGYFKFQGQDTILDYTLREVDTV 3Q93,6GLE,6EQ7,6EQ6,6EQ5,6EQ4,6EQ3,6EQ2,5ANT,5ANS,9FL6,5ANW,5ANV,5ANU,4C9X,4C9W,9GQL,6JVT,6JVS,6JVR,6JVQ,6JVP,6JVN,6JVM,6JVL,6JVK,6JVJ,6JVI,6JVH,6JVG,6JVF,5FSO,5FSN,5FSM,5FSL,5FSI,3ZR1,3ZR0,3WHW,1IRY,7N13,7N03,7ESF,8A3A,8A34,8A0T,8A0S,8A07,6US4,6US3,6US2,6F23,6F22,6F20,6F1X,5OTM,5NHY,5NGT,5NGS,5NGR,5FSK,4N1T,6QVO,4N1U,6JVO,6IMZ,6AA5,6AA4,6AA3,5MZF Oxidized purine nucleoside triphosphate hydrolase 8ODP_HUMAN P36639 A4D205 Q6LES7 Q6P0Y6 Q7Z7N6 Q8IV95 Q9UBM0 Q9UBM9 51623120 CCNC(=O)c1cc2c(ccnc2[nH]1)N3CCOC[C@@H]3C InChI=1S/C15H20N4O2/c1-3-16-15(20)12-8-11-13(4-5-17-14(11)18-12)19-6-7-21-9-10(19)2/h4-5,8,10H,3,6-7,9H2,1-2H3,(H,16,20)(H,17,18) RPMGXDCRCWWCRY-UHFFFAOYSA-N 50255583 CHEMBL4096813 Oxidized purine nucleoside triphosphate hydrolase Homo sapiens 2.3 ChEMBL 10.7270/Q2SX6JZH 28679043 Ellermann, M; Eheim, A; Rahm, F; Viklund, J; Guenther, J; Andersson, M; Ericsson, U; Forsblom, R; Ginman, T; Lindström, J; Silvander, C; Trésaugues, L; Giese, A; Bunse, S; Neuhaus, R; Weiske, J; Quanz, M; Glasauer, A; Nowak-Reppel, K; Bader, B; Irlbacher, H; Meyer, H; Queisser, N; Bauser, M; Haegebarth, A; Gorjánácz, M //0 10/13/2025 Bayer AG http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50255583 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=9756&target=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50255583&enzyme=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search 8XT 5NHY 129012086 402360383 1 MGASRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGARRELQEESGLTVDALHKVGQIVFEFVGEPELMDVHVFCTDSIQGTPVESDEMRPCWFQLDQIPFKDMWPDDSYWFPLLLQKKKFHGYFKFQGQDTILDYTLREVDTV 3Q93,6GLE,6EQ7,6EQ6,6EQ5,6EQ4,6EQ3,6EQ2,5ANT,5ANS,9FL6,5ANW,5ANV,5ANU,4C9X,4C9W,9GQL,6JVT,6JVS,6JVR,6JVQ,6JVP,6JVN,6JVM,6JVL,6JVK,6JVJ,6JVI,6JVH,6JVG,6JVF,5FSO,5FSN,5FSM,5FSL,5FSI,3ZR1,3ZR0,3WHW,1IRY,7N13,7N03,7ESF,9QUK,9QUH,9QUE,8A3A,8A34,8A0T,8A0S,8A07,6US4,6US3,6US2,6F23,6F22,6F20,6F1X,5OTM,5NHY,5NGT,5NGS,5NGR,5FSK,4N1T,6QVO,4N1U,6JVO,6IMZ,6AA5,6AA4,6AA3,5MZF Oxidized purine nucleoside triphosphate hydrolase 8ODP_HUMAN P36639 A4D205 Q6LES7 Q6P0Y6 Q7Z7N6 Q8IV95 Q9UBM0 Q9UBM9 51286589 Nc1nc2ncccc2[nH]1 InChI=1S/C6H6N4/c7-6-9-4-2-1-3-8-5(4)10-6/h1-3H,(H3,7,8,9,10) KXQPVJRJUJJWQJ-UHFFFAOYSA-N 50524488 CHEMBL4589188 Oxidized purine nucleoside triphosphate hydrolase Homo sapiens 1300 ChEMBL 10.1016/j.ejmech.2019.04.037 10.7270/Q2PN991Z 31077996 Wiedmer, L; Schärer, C; Spiliotopoulos, D; Hürzeler, M; Śledź, P; Caflisch, A 8/1/2019 2/24/2021 University of Zurich http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50524488 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=9756&target=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50524488&enzyme=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search BU8 6EQ2,6GLG,6GLH,6GLL,6GLM,6GLP,6GLQ,6GLU 179897 440733070 1 MGASRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGARRELQEESGLTVDALHKVGQIVFEFVGEPELMDVHVFCTDSIQGTPVESDEMRPCWFQLDQIPFKDMWPDDSYWFPLLLQKKKFHGYFKFQGQDTILDYTLREVDTV 3Q93,6GLE,6EQ7,6EQ6,6EQ5,6EQ4,6EQ3,6EQ2,5ANT,5ANS,9FL6,5ANW,5ANV,5ANU,4C9X,4C9W,9GQL,6JVT,6JVS,6JVR,6JVQ,6JVP,6JVN,6JVM,6JVL,6JVK,6JVJ,6JVI,6JVH,6JVG,6JVF,5FSO,5FSN,5FSM,5FSL,5FSI,3ZR1,3ZR0,3WHW,1IRY,7N13,7N03,7ESF,9QUK,9QUH,9QUE,8A3A,8A34,8A0T,8A0S,8A07,6US4,6US3,6US2,6F23,6F22,6F20,6F1X,5OTM,5NHY,5NGT,5NGS,5NGR,5FSK,4N1T,6QVO,4N1U,6JVO,6IMZ,6AA5,6AA4,6AA3,5MZF Oxidized purine nucleoside triphosphate hydrolase 8ODP_HUMAN P36639 A4D205 Q6LES7 Q6P0Y6 Q7Z7N6 Q8IV95 Q9UBM0 Q9UBM9 51286595 Nc1nc2ncccc2[nH]1 InChI=1S/C6H6N4/c7-6-9-4-2-1-3-8-5(4)10-6/h1-3H,(H3,7,8,9,10) KXQPVJRJUJJWQJ-UHFFFAOYSA-N 50524488 CHEMBL4589188 Oxidized purine nucleoside triphosphate hydrolase Homo sapiens 1100 ChEMBL 10.1016/j.ejmech.2019.04.037 10.7270/Q2PN991Z 31077996 Wiedmer, L; Schärer, C; Spiliotopoulos, D; Hürzeler, M; Śledź, P; Caflisch, A 8/1/2019 2/24/2021 University of Zurich http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50524488 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=9756&target=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50524488&enzyme=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search BU8 6EQ2,6GLG,6GLH,6GLL,6GLM,6GLP,6GLQ,6GLU 179897 440733070 1 MGASRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGARRELQEESGLTVDALHKVGQIVFEFVGEPELMDVHVFCTDSIQGTPVESDEMRPCWFQLDQIPFKDMWPDDSYWFPLLLQKKKFHGYFKFQGQDTILDYTLREVDTV 3Q93,6GLE,6EQ7,6EQ6,6EQ5,6EQ4,6EQ3,6EQ2,5ANT,5ANS,9FL6,5ANW,5ANV,5ANU,4C9X,4C9W,9GQL,6JVT,6JVS,6JVR,6JVQ,6JVP,6JVN,6JVM,6JVL,6JVK,6JVJ,6JVI,6JVH,6JVG,6JVF,5FSO,5FSN,5FSM,5FSL,5FSI,3ZR1,3ZR0,3WHW,1IRY,7N13,7N03,7ESF,9QUK,9QUH,9QUE,8A3A,8A34,8A0T,8A0S,8A07,6US4,6US3,6US2,6F23,6F22,6F20,6F1X,5OTM,5NHY,5NGT,5NGS,5NGR,5FSK,4N1T,6QVO,4N1U,6JVO,6IMZ,6AA5,6AA4,6AA3,5MZF Oxidized purine nucleoside triphosphate hydrolase 8ODP_HUMAN P36639 A4D205 Q6LES7 Q6P0Y6 Q7Z7N6 Q8IV95 Q9UBM0 Q9UBM9 51286588 Nc1nc2ccccc2[nH]1 InChI=1S/C7H7N3/c8-7-9-5-3-1-2-4-6(5)10-7/h1-4H,(H3,8,9,10) JWYUFVNJZUSCSM-UHFFFAOYSA-N 7960 CHEMBL305513::JMC524454 Compound 5::1H-1,3-benzodiazol-2-amine::CRA Fragment 9::2-Aminobenzimidazole::Imidazole C-2 deriv. 3::US11584714, Compound 46::US12195427, Compound 46 Oxidized purine nucleoside triphosphate hydrolase Homo sapiens 18000 ChEMBL 10.1016/j.ejmech.2019.04.037 10.7270/Q2PN991Z 31077996 Wiedmer, L; Schärer, C; Spiliotopoulos, D; Hürzeler, M; Śledź, P; Caflisch, A 8/1/2019 2/24/2021 University of Zurich http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=7960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=9756&target=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=7960&enzyme=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search AX7 1QA0,2FPZ,2FX6,3GN1,3KQS,5PAR,5SWG,5Z4H,5Z4O,5Z9B,5Z9E,5Z9F,5Z9L,5Z9P,5Z9Q,6EQ5,7DOR,7DPR,7DPS,7DQF,7DQH,7DQI,7DQJ,7DQL,7DQM,7DQS,7DQU,7DQW,7I05,9DRS 13624 11108721 CHEMBL305513 C10901 1 MGASRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGARRELQEESGLTVDALHKVGQIVFEFVGEPELMDVHVFCTDSIQGTPVESDEMRPCWFQLDQIPFKDMWPDDSYWFPLLLQKKKFHGYFKFQGQDTILDYTLREVDTV 3Q93,6GLE,6EQ7,6EQ6,6EQ5,6EQ4,6EQ3,6EQ2,5ANT,5ANS,9FL6,5ANW,5ANV,5ANU,4C9X,4C9W,9GQL,6JVT,6JVS,6JVR,6JVQ,6JVP,6JVN,6JVM,6JVL,6JVK,6JVJ,6JVI,6JVH,6JVG,6JVF,5FSO,5FSN,5FSM,5FSL,5FSI,3ZR1,3ZR0,3WHW,1IRY,7N13,7N03,7ESF,9QUK,9QUH,9QUE,8A3A,8A34,8A0T,8A0S,8A07,6US4,6US3,6US2,6F23,6F22,6F20,6F1X,5OTM,5NHY,5NGT,5NGS,5NGR,5FSK,4N1T,6QVO,4N1U,6JVO,6IMZ,6AA5,6AA4,6AA3,5MZF Oxidized purine nucleoside triphosphate hydrolase 8ODP_HUMAN P36639 A4D205 Q6LES7 Q6P0Y6 Q7Z7N6 Q8IV95 Q9UBM0 Q9UBM9 51286596 Nc1nc2ccccc2[nH]1 InChI=1S/C7H7N3/c8-7-9-5-3-1-2-4-6(5)10-7/h1-4H,(H3,8,9,10) JWYUFVNJZUSCSM-UHFFFAOYSA-N 7960 CHEMBL305513::JMC524454 Compound 5::1H-1,3-benzodiazol-2-amine::CRA Fragment 9::2-Aminobenzimidazole::Imidazole C-2 deriv. 3::US11584714, Compound 46::US12195427, Compound 46 Oxidized purine nucleoside triphosphate hydrolase Homo sapiens 44000 ChEMBL 10.1016/j.ejmech.2019.04.037 10.7270/Q2PN991Z 31077996 Wiedmer, L; Schärer, C; Spiliotopoulos, D; Hürzeler, M; Śledź, P; Caflisch, A 8/1/2019 2/24/2021 University of Zurich http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=7960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=9756&target=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=7960&enzyme=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search AX7 1QA0,2FPZ,2FX6,3GN1,3KQS,5PAR,5SWG,5Z4H,5Z4O,5Z9B,5Z9E,5Z9F,5Z9L,5Z9P,5Z9Q,6EQ5,7DOR,7DPR,7DPS,7DQF,7DQH,7DQI,7DQJ,7DQL,7DQM,7DQS,7DQU,7DQW,7I05,9DRS 13624 11108721 CHEMBL305513 C10901 1 MGASRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGARRELQEESGLTVDALHKVGQIVFEFVGEPELMDVHVFCTDSIQGTPVESDEMRPCWFQLDQIPFKDMWPDDSYWFPLLLQKKKFHGYFKFQGQDTILDYTLREVDTV 3Q93,6GLE,6EQ7,6EQ6,6EQ5,6EQ4,6EQ3,6EQ2,5ANT,5ANS,9FL6,5ANW,5ANV,5ANU,4C9X,4C9W,9GQL,6JVT,6JVS,6JVR,6JVQ,6JVP,6JVN,6JVM,6JVL,6JVK,6JVJ,6JVI,6JVH,6JVG,6JVF,5FSO,5FSN,5FSM,5FSL,5FSI,3ZR1,3ZR0,3WHW,1IRY,7N13,7N03,7ESF,9QUK,9QUH,9QUE,8A3A,8A34,8A0T,8A0S,8A07,6US4,6US3,6US2,6F23,6F22,6F20,6F1X,5OTM,5NHY,5NGT,5NGS,5NGR,5FSK,4N1T,6QVO,4N1U,6JVO,6IMZ,6AA5,6AA4,6AA3,5MZF Oxidized purine nucleoside triphosphate hydrolase 8ODP_HUMAN P36639 A4D205 Q6LES7 Q6P0Y6 Q7Z7N6 Q8IV95 Q9UBM0 Q9UBM9 51286583 c1ccc2c(c1)nc(c(n2)N3CCCC3)N InChI=1S/C12H14N4/c13-11-12(16-7-3-4-8-16)15-10-6-2-1-5-9(10)14-11/h1-2,5-6H,3-4,7-8H2,(H2,13,14) LWWDIFFPFOZSSB-UHFFFAOYSA-N 50524487 CHEMBL1232596 Oxidized purine nucleoside triphosphate hydrolase Homo sapiens 15000 ChEMBL 10.1016/j.ejmech.2019.04.037 10.7270/Q2PN991Z 31077996 Wiedmer, L; Schärer, C; Spiliotopoulos, D; Hürzeler, M; Śledź, P; Caflisch, A 8/1/2019 2/24/2021 University of Zurich http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50524487 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=9756&target=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50524487&enzyme=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search EV2 3HW1,6EQ6 2041326 440733069 1 MGASRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGARRELQEESGLTVDALHKVGQIVFEFVGEPELMDVHVFCTDSIQGTPVESDEMRPCWFQLDQIPFKDMWPDDSYWFPLLLQKKKFHGYFKFQGQDTILDYTLREVDTV 3Q93,6GLE,6EQ7,6EQ6,6EQ5,6EQ4,6EQ3,6EQ2,5ANT,5ANS,9FL6,5ANW,5ANV,5ANU,4C9X,4C9W,9GQL,6JVT,6JVS,6JVR,6JVQ,6JVP,6JVN,6JVM,6JVL,6JVK,6JVJ,6JVI,6JVH,6JVG,6JVF,5FSO,5FSN,5FSM,5FSL,5FSI,3ZR1,3ZR0,3WHW,1IRY,7N13,7N03,7ESF,8A3A,8A34,8A0T,8A0S,8A07,6US4,6US3,6US2,6F23,6F22,6F20,6F1X,5OTM,5NHY,5NGT,5NGS,5NGR,5FSK,4N1T,6QVO,4N1U,6JVO,6IMZ,6AA5,6AA4,6AA3,5MZF Oxidized purine nucleoside triphosphate hydrolase 8ODP_HUMAN P36639 A4D205 Q6LES7 Q6P0Y6 Q7Z7N6 Q8IV95 Q9UBM0 Q9UBM9 51286585 c1ccc2c(c1)nc(c(n2)N3CCCC3)N InChI=1S/C12H14N4/c13-11-12(16-7-3-4-8-16)15-10-6-2-1-5-9(10)14-11/h1-2,5-6H,3-4,7-8H2,(H2,13,14) LWWDIFFPFOZSSB-UHFFFAOYSA-N 50524487 CHEMBL1232596 Oxidized purine nucleoside triphosphate hydrolase Homo sapiens 23000 ChEMBL 10.1016/j.ejmech.2019.04.037 10.7270/Q2PN991Z 31077996 Wiedmer, L; Schärer, C; Spiliotopoulos, D; Hürzeler, M; Śledź, P; Caflisch, A 8/1/2019 2/24/2021 University of Zurich http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50524487 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=9756&target=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50524487&enzyme=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search EV2 3HW1,6EQ6 2041326 440733069 1 MGASRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGARRELQEESGLTVDALHKVGQIVFEFVGEPELMDVHVFCTDSIQGTPVESDEMRPCWFQLDQIPFKDMWPDDSYWFPLLLQKKKFHGYFKFQGQDTILDYTLREVDTV 3Q93,6GLE,6EQ7,6EQ6,6EQ5,6EQ4,6EQ3,6EQ2,5ANT,5ANS,9FL6,5ANW,5ANV,5ANU,4C9X,4C9W,9GQL,6JVT,6JVS,6JVR,6JVQ,6JVP,6JVN,6JVM,6JVL,6JVK,6JVJ,6JVI,6JVH,6JVG,6JVF,5FSO,5FSN,5FSM,5FSL,5FSI,3ZR1,3ZR0,3WHW,1IRY,7N13,7N03,7ESF,8A3A,8A34,8A0T,8A0S,8A07,6US4,6US3,6US2,6F23,6F22,6F20,6F1X,5OTM,5NHY,5NGT,5NGS,5NGR,5FSK,4N1T,6QVO,4N1U,6JVO,6IMZ,6AA5,6AA4,6AA3,5MZF Oxidized purine nucleoside triphosphate hydrolase 8ODP_HUMAN P36639 A4D205 Q6LES7 Q6P0Y6 Q7Z7N6 Q8IV95 Q9UBM0 Q9UBM9 50804996 CCNC(=O)c1cc2c(ccnc2[nH]1)c3cccc(c3)Cl InChI=1S/C16H14ClN3O/c1-2-18-16(21)14-9-13-12(6-7-19-15(13)20-14)10-4-3-5-11(17)8-10/h3-9H,2H2,1H3,(H,18,21)(H,19,20) AWWOSFPXOHAONT-UHFFFAOYSA-N 50255618 CHEMBL4104130 Oxidized purine nucleoside triphosphate hydrolase Homo sapiens 20 ChEMBL 10.1021/acs.jmedchem.7b01884 10.7270/Q25D8V9Q 29485874 Rahm, F; Viklund, J; Trésaugues, L; Ellermann, M; Giese, A; Ericsson, U; Forsblom, R; Ginman, T; Günther, J; Hallberg, K; Lindström, J; Persson, LB; Silvander, C; Talagas, A; Díaz-Sáez, L; Fedorov, O; Huber, KVM; Panagakou, I; Siejka, P; Gorjánácz, M; Bauser, M; Andersson, M 3/22/2018 12/14/2019 Sprint Bioscience http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50255618 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=9756&target=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50255618&enzyme=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search C9Q 6F1X 132451818 402360404 1 MGASRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGARRELQEESGLTVDALHKVGQIVFEFVGEPELMDVHVFCTDSIQGTPVESDEMRPCWFQLDQIPFKDMWPDDSYWFPLLLQKKKFHGYFKFQGQDTILDYTLREVDTV 3Q93,6GLE,6EQ7,6EQ6,6EQ5,6EQ4,6EQ3,6EQ2,5ANT,5ANS,9FL6,5ANW,5ANV,5ANU,4C9X,4C9W,9GQL,6JVT,6JVS,6JVR,6JVQ,6JVP,6JVN,6JVM,6JVL,6JVK,6JVJ,6JVI,6JVH,6JVG,6JVF,5FSO,5FSN,5FSM,5FSL,5FSI,3ZR1,3ZR0,3WHW,1IRY,7N13,7N03,7ESF,8A3A,8A34,8A0T,8A0S,8A07,6US4,6US3,6US2,6F23,6F22,6F20,6F1X,5OTM,5NHY,5NGT,5NGS,5NGR,5FSK,4N1T,6QVO,4N1U,6JVO,6IMZ,6AA5,6AA4,6AA3,5MZF Oxidized purine nucleoside triphosphate hydrolase 8ODP_HUMAN P36639 A4D205 Q6LES7 Q6P0Y6 Q7Z7N6 Q8IV95 Q9UBM0 Q9UBM9 50804903 CCOC(=O)c1ccnc2c1cc[nH]2 InChI=1S/C10H10N2O2/c1-2-14-10(13)8-4-6-12-9-7(8)3-5-11-9/h3-6H,2H2,1H3,(H,11,12) CKCBQXQNAUHBDX-UHFFFAOYSA-N 50255614 CHEMBL4087054 Oxidized purine nucleoside triphosphate hydrolase Homo sapiens 9900 ChEMBL 10.1021/acs.jmedchem.7b01884 10.7270/Q25D8V9Q 29485874 Rahm, F; Viklund, J; Trésaugues, L; Ellermann, M; Giese, A; Ericsson, U; Forsblom, R; Ginman, T; Günther, J; Hallberg, K; Lindström, J; Persson, LB; Silvander, C; Talagas, A; Díaz-Sáez, L; Fedorov, O; Huber, KVM; Panagakou, I; Siejka, P; Gorjánácz, M; Bauser, M; Andersson, M 3/22/2018 12/14/2019 Sprint Bioscience http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50255614 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=9756&target=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50255614&enzyme=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search C9E 6F20 56773892 402360400 1 MGASRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGARRELQEESGLTVDALHKVGQIVFEFVGEPELMDVHVFCTDSIQGTPVESDEMRPCWFQLDQIPFKDMWPDDSYWFPLLLQKKKFHGYFKFQGQDTILDYTLREVDTV 3Q93,6GLE,6EQ7,6EQ6,6EQ5,6EQ4,6EQ3,6EQ2,5ANT,5ANS,9FL6,5ANW,5ANV,5ANU,4C9X,4C9W,9GQL,6JVT,6JVS,6JVR,6JVQ,6JVP,6JVN,6JVM,6JVL,6JVK,6JVJ,6JVI,6JVH,6JVG,6JVF,5FSO,5FSN,5FSM,5FSL,5FSI,3ZR1,3ZR0,3WHW,1IRY,7N13,7N03,7ESF,8A3A,8A34,8A0T,8A0S,8A07,6US4,6US3,6US2,6F23,6F22,6F20,6F1X,5OTM,5NHY,5NGT,5NGS,5NGR,5FSK,4N1T,6QVO,4N1U,6JVO,6IMZ,6AA5,6AA4,6AA3,5MZF Oxidized purine nucleoside triphosphate hydrolase 8ODP_HUMAN P36639 A4D205 Q6LES7 Q6P0Y6 Q7Z7N6 Q8IV95 Q9UBM0 Q9UBM9 50804991 CCOC(=O)c1ccnc2c1cc[nH]2 InChI=1S/C10H10N2O2/c1-2-14-10(13)8-4-6-12-9-7(8)3-5-11-9/h3-6H,2H2,1H3,(H,11,12) CKCBQXQNAUHBDX-UHFFFAOYSA-N 50255614 CHEMBL4087054 Oxidized purine nucleoside triphosphate hydrolase Homo sapiens 49500 ChEMBL 10.1021/acs.jmedchem.7b01884 10.7270/Q25D8V9Q 29485874 Rahm, F; Viklund, J; Trésaugues, L; Ellermann, M; Giese, A; Ericsson, U; Forsblom, R; Ginman, T; Günther, J; Hallberg, K; Lindström, J; Persson, LB; Silvander, C; Talagas, A; Díaz-Sáez, L; Fedorov, O; Huber, KVM; Panagakou, I; Siejka, P; Gorjánácz, M; Bauser, M; Andersson, M 3/22/2018 12/14/2019 Sprint Bioscience http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50255614 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=9756&target=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50255614&enzyme=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search C9E 6F20 56773892 402360400 1 MGASRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGARRELQEESGLTVDALHKVGQIVFEFVGEPELMDVHVFCTDSIQGTPVESDEMRPCWFQLDQIPFKDMWPDDSYWFPLLLQKKKFHGYFKFQGQDTILDYTLREVDTV 3Q93,6GLE,6EQ7,6EQ6,6EQ5,6EQ4,6EQ3,6EQ2,5ANT,5ANS,9FL6,5ANW,5ANV,5ANU,4C9X,4C9W,9GQL,6JVT,6JVS,6JVR,6JVQ,6JVP,6JVN,6JVM,6JVL,6JVK,6JVJ,6JVI,6JVH,6JVG,6JVF,5FSO,5FSN,5FSM,5FSL,5FSI,3ZR1,3ZR0,3WHW,1IRY,7N13,7N03,7ESF,8A3A,8A34,8A0T,8A0S,8A07,6US4,6US3,6US2,6F23,6F22,6F20,6F1X,5OTM,5NHY,5NGT,5NGS,5NGR,5FSK,4N1T,6QVO,4N1U,6JVO,6IMZ,6AA5,6AA4,6AA3,5MZF Oxidized purine nucleoside triphosphate hydrolase 8ODP_HUMAN P36639 A4D205 Q6LES7 Q6P0Y6 Q7Z7N6 Q8IV95 Q9UBM0 Q9UBM9 50804905 c1ccc(cc1)[C@H]2CCCN2c3ccnc4c3cc[nH]4 InChI=1S/C17H17N3/c1-2-5-13(6-3-1)15-7-4-12-20(15)16-9-11-19-17-14(16)8-10-18-17/h1-3,5-6,8-11,15H,4,7,12H2,(H,18,19) GUMMAYIOLPYJKE-UHFFFAOYSA-N 50255615 CHEMBL4061204 Oxidized purine nucleoside triphosphate hydrolase Homo sapiens 63 ChEMBL 10.1021/acs.jmedchem.7b01884 10.7270/Q25D8V9Q 29485874 Rahm, F; Viklund, J; Trésaugues, L; Ellermann, M; Giese, A; Ericsson, U; Forsblom, R; Ginman, T; Günther, J; Hallberg, K; Lindström, J; Persson, LB; Silvander, C; Talagas, A; Díaz-Sáez, L; Fedorov, O; Huber, KVM; Panagakou, I; Siejka, P; Gorjánácz, M; Bauser, M; Andersson, M 3/22/2018 12/14/2019 Sprint Bioscience http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50255615 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=9756&target=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50255615&enzyme=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search C8Z 6F23 137637041 402360401 1 MGASRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGARRELQEESGLTVDALHKVGQIVFEFVGEPELMDVHVFCTDSIQGTPVESDEMRPCWFQLDQIPFKDMWPDDSYWFPLLLQKKKFHGYFKFQGQDTILDYTLREVDTV 3Q93,6GLE,6EQ7,6EQ6,6EQ5,6EQ4,6EQ3,6EQ2,5ANT,5ANS,9FL6,5ANW,5ANV,5ANU,4C9X,4C9W,9GQL,6JVT,6JVS,6JVR,6JVQ,6JVP,6JVN,6JVM,6JVL,6JVK,6JVJ,6JVI,6JVH,6JVG,6JVF,5FSO,5FSN,5FSM,5FSL,5FSI,3ZR1,3ZR0,3WHW,1IRY,7N13,7N03,7ESF,8A3A,8A34,8A0T,8A0S,8A07,6US4,6US3,6US2,6F23,6F22,6F20,6F1X,5OTM,5NHY,5NGT,5NGS,5NGR,5FSK,4N1T,6QVO,4N1U,6JVO,6IMZ,6AA5,6AA4,6AA3,5MZF Oxidized purine nucleoside triphosphate hydrolase 8ODP_HUMAN P36639 A4D205 Q6LES7 Q6P0Y6 Q7Z7N6 Q8IV95 Q9UBM0 Q9UBM9 50805003 c1ccc(cc1)[C@H]2CCCN2c3ccnc4c3cc[nH]4 InChI=1S/C17H17N3/c1-2-5-13(6-3-1)15-7-4-12-20(15)16-9-11-19-17-14(16)8-10-18-17/h1-3,5-6,8-11,15H,4,7,12H2,(H,18,19) GUMMAYIOLPYJKE-UHFFFAOYSA-N 50255615 CHEMBL4061204 Oxidized purine nucleoside triphosphate hydrolase Homo sapiens 5.0 ChEMBL 10.1021/acs.jmedchem.7b01884 10.7270/Q25D8V9Q 29485874 Rahm, F; Viklund, J; Trésaugues, L; Ellermann, M; Giese, A; Ericsson, U; Forsblom, R; Ginman, T; Günther, J; Hallberg, K; Lindström, J; Persson, LB; Silvander, C; Talagas, A; Díaz-Sáez, L; Fedorov, O; Huber, KVM; Panagakou, I; Siejka, P; Gorjánácz, M; Bauser, M; Andersson, M 3/22/2018 12/14/2019 Sprint Bioscience http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50255615 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=9756&target=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50255615&enzyme=Oxidized+purine+nucleoside+triphosphate+hydrolase&column=ki&startPg=0&Increment=50&submit=Search C8Z 6F23 137637041 402360401 1 MGASRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGARRELQEESGLTVDALHKVGQIVFEFVGEPELMDVHVFCTDSIQGTPVESDEMRPCWFQLDQIPFKDMWPDDSYWFPLLLQKKKFHGYFKFQGQDTILDYTLREVDTV 3Q93,6GLE,6EQ7,6EQ6,6EQ5,6EQ4,6EQ3,6EQ2,5ANT,5ANS,9FL6,5ANW,5ANV,5ANU,4C9X,4C9W,9GQL,6JVT,6JVS,6JVR,6JVQ,6JVP,6JVN,6JVM,6JVL,6JVK,6JVJ,6JVI,6JVH,6JVG,6JVF,5FSO,5FSN,5FSM,5FSL,5FSI,3ZR1,3ZR0,3WHW,1IRY,7N13,7N03,7ESF,8A3A,8A34,8A0T,8A0S,8A07,6US4,6US3,6US2,6F23,6F22,6F20,6F1X,5OTM,5NHY,5NGT,5NGS,5NGR,5FSK,4N1T,6QVO,4N1U,6JVO,6IMZ,6AA5,6AA4,6AA3,5MZF Oxidized purine nucleoside triphosphate hydrolase 8ODP_HUMAN P36639 A4D205 Q6LES7 Q6P0Y6 Q7Z7N6 Q8IV95 Q9UBM0 Q9UBM9 159156 c1ccc2c(c1)ccc(n2)CNc3nc4c(ncnc4n3[C@H]5[C@@H]([C@@H]([C@H](O5)CO)O)O)N InChI=1S/C20H21N7O4/c21-17-14-18(24-9-23-17)27(19-16(30)15(29)13(8-28)31-19)20(26-14)22-7-11-6-5-10-3-1-2-4-12(10)25-11/h1-6,9,13,15-16,19,28-30H,7-8H2,(H,22,26)(H2,21,23,24) NAHSCHKAPXMNFP-UHFFFAOYSA-N 82129 (2R,3R,4S,5R)-2-{6-Amino-8-[(quinolin-2-ylmethyl)amino]- purin-9-yl}-5-hydroxymethyltetrahydrofuran-3,4-diol::adenosine-derived inhibitor (Grp78), 10 Endoplasmic reticulum chaperone BiP Homo sapiens 2.41e+3 0.4 7.4000 25.00 C Curated from the literature by BindingDB 10.1021/jm101625x 10.7270/Q2R49P83 21526763 aid1799592 Macias, AT; Williamson, DS; Allen, N; Borgognoni, J; Clay, A; Daniels, Z; Dokurno, P; Drysdale, MJ; Francis, GL; Graham, CJ; Howes, R; Matassova, N; Murray, JB; Parsons, R; Shaw, T; Surgenor, AE; Terry, L; Wang, Y; Wood, M; Massey, AJ 6/23/2011 12/8/2011 Vernalis (R&D) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=82129 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=49001168&target=Endoplasmic+reticulum+chaperone+BiP&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=82129&enzyme=Endoplasmic+reticulum+chaperone+BiP&column=ki&startPg=0&Increment=50&submit=Search 3P1 3LDQ,3LDP 49843461 131342703 1 MKLSLVAAMLLLLSAARAEEEDKKEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTGDLVLLDVCPLTLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDVNGILRVTAEDKGTGNKNKITITNDQNRLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDKEKLGGKLSSEDKETMEKAVEEKIEWLESHQDADIEDFKAKKKELEEIVQPIISKLYGSAGPPPTGEEDTAEKDEL 7N1R,6ASY,3IUC,5F2R,5F1X,5F0X,5EY4,5EXW,5EX5,5EVZ,3LDP,3LDO,3LDN,3LDL,6DWS,6DO2,6DFO,6DFM,6CZ1,5E85 Endoplasmic reticulum chaperone BiP BIP_HUMAN P11021 B0QZ61 Q2EF78 Q9NPF1 Q9UK02 50249354 C[C@]1(C(=O)NC(=O)N1)CNC(=O)COc2ccc(cc2)Cl InChI=1S/C13H14ClN3O4/c1-13(11(19)16-12(20)17-13)7-15-10(18)6-21-9-4-2-8(14)3-5-9/h2-5H,6-7H2,1H3,(H,15,18)(H2,16,17,19,20) LNIRXDCIYOBRPL-UHFFFAOYSA-N 50033809 CHEMBL3358151 A disintegrin and metalloproteinase with thrombospondin motifs 4 Homo sapiens 74 ChEMBL 10.1021/jm501522n 10.7270/Q2K35W85 25415648 Durham, TB; Klimkowski, VJ; Rito, CJ; Marimuthu, J; Toth, JL; Liu, C; Durbin, JD; Stout, SL; Adams, L; Swearingen, C; Lin, C; Chambers, MG; Thirunavukkarasu, K; Wiley, MR 12/29/2014 3/13/2016 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50033809 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5138&target=A+disintegrin+and+metalloproteinase+with+thrombospondin+motifs+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50033809&enzyme=A+disintegrin+and+metalloproteinase+with+thrombospondin+motifs+4&column=ki&startPg=0&Increment=50&submit=Search 3PQ 4WK7 86287514 103942057 CHEMBL3358151 1 MSQTGSHPGRGLAGRWLWGAQPCLLLPIVPLSWLVWLLLLLLASLLPSARLASPLPREEEIVFPEKLNGSVLPGSGAPARLLCRLQAFGETLLLELEQDSGVQVEGLTVQYLGQAPELLGGAEPGTYLTGTINGDPESVASLHWDGGALLGVLQYRGAELHLQPLEGGTPNSAGGPGAHILRRKSPASGQGPMCNVKAPLGSPSPRPRRAKRFASLSRFVETLVVADDKMAAFHGAGLKRYLLTVMAAAAKAFKHPSIRNPVSLVVTRLVILGSGEEGPQVGPSAAQTLRSFCAWQRGLNTPEDSDPDHFDTAILFTRQDLCGVSTCDTLGMADVGTVCDPARSCAIVEDDGLQSAFTAAHELGHVFNMLHDNSKPCISLNGPLSTSRHVMAPVMAHVDPEEPWSPCSARFITDFLDNGYGHCLLDKPEAPLHLPVTFPGKDYDADRQCQLTFGPDSRHCPQLPPPCAALWCSGHLNGHAMCQTKHSPWADGTPCGPAQACMGGRCLHMDQLQDFNIPQAGGWGPWGPWGDCSRTCGGGVQFSSRDCTRPVPRNGGKYCEGRRTRFRSCNTEDCPTGSALTFREEQCAAYNHRTDLFKSFPGPMDWVPRYTGVAPQDQCKLTCQAQALGYYYVLEPRVVDGTPCSPDSSSVCVQGRCIHAGCDRIIGSKKKFDKCMVCGGDGSGCSKQSGSFRKFRYGYNNVVTIPAGATHILVRQQGNPGHRSIYLALKLPDGSYALNGEYTLMPSPTDVVLPGAVSLRYSGATAASETLSGHGPLAQPLTLQVLVAGNPQDTRLRYSFFVPRPTPSTPRPTPQDWLHRRAQILEILRRRPWAGRK 4WKI,4WKE,4WK7 A disintegrin and metalloproteinase with thrombospondin motifs 4 ATS4_HUMAN O75173 Q2HYD0 Q5VTW2 Q6P4Q8 Q6UWA8 Q9UN83 50249358 c1cc2c(cc1Cl)cc(o2)C(=O)NC[C@@]3(C(=O)NC(=O)N3)c4nccs4 InChI=1S/C16H11ClN4O4S/c17-9-1-2-10-8(5-9)6-11(25-10)12(22)19-7-16(14-18-3-4-26-14)13(23)20-15(24)21-16/h1-6H,7H2,(H,19,22)(H2,20,21,23,24) LBVBVIKJOWWVJX-UHFFFAOYSA-N 50033805 CHEMBL3358155 A disintegrin and metalloproteinase with thrombospondin motifs 4 Homo sapiens 8.0 ChEMBL 10.1021/jm501522n 10.7270/Q2K35W85 25415648 Durham, TB; Klimkowski, VJ; Rito, CJ; Marimuthu, J; Toth, JL; Liu, C; Durbin, JD; Stout, SL; Adams, L; Swearingen, C; Lin, C; Chambers, MG; Thirunavukkarasu, K; Wiley, MR 12/29/2014 3/13/2016 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50033805 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5138&target=A+disintegrin+and+metalloproteinase+with+thrombospondin+motifs+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50033805&enzyme=A+disintegrin+and+metalloproteinase+with+thrombospondin+motifs+4&column=ki&startPg=0&Increment=50&submit=Search 3PU 4WKE 86287515 103942053 CHEMBL3358155 1 MSQTGSHPGRGLAGRWLWGAQPCLLLPIVPLSWLVWLLLLLLASLLPSARLASPLPREEEIVFPEKLNGSVLPGSGAPARLLCRLQAFGETLLLELEQDSGVQVEGLTVQYLGQAPELLGGAEPGTYLTGTINGDPESVASLHWDGGALLGVLQYRGAELHLQPLEGGTPNSAGGPGAHILRRKSPASGQGPMCNVKAPLGSPSPRPRRAKRFASLSRFVETLVVADDKMAAFHGAGLKRYLLTVMAAAAKAFKHPSIRNPVSLVVTRLVILGSGEEGPQVGPSAAQTLRSFCAWQRGLNTPEDSDPDHFDTAILFTRQDLCGVSTCDTLGMADVGTVCDPARSCAIVEDDGLQSAFTAAHELGHVFNMLHDNSKPCISLNGPLSTSRHVMAPVMAHVDPEEPWSPCSARFITDFLDNGYGHCLLDKPEAPLHLPVTFPGKDYDADRQCQLTFGPDSRHCPQLPPPCAALWCSGHLNGHAMCQTKHSPWADGTPCGPAQACMGGRCLHMDQLQDFNIPQAGGWGPWGPWGDCSRTCGGGVQFSSRDCTRPVPRNGGKYCEGRRTRFRSCNTEDCPTGSALTFREEQCAAYNHRTDLFKSFPGPMDWVPRYTGVAPQDQCKLTCQAQALGYYYVLEPRVVDGTPCSPDSSSVCVQGRCIHAGCDRIIGSKKKFDKCMVCGGDGSGCSKQSGSFRKFRYGYNNVVTIPAGATHILVRQQGNPGHRSIYLALKLPDGSYALNGEYTLMPSPTDVVLPGAVSLRYSGATAASETLSGHGPLAQPLTLQVLVAGNPQDTRLRYSFFVPRPTPSTPRPTPQDWLHRRAQILEILRRRPWAGRK 4WKI,4WKE,4WK7 A disintegrin and metalloproteinase with thrombospondin motifs 4 ATS4_HUMAN O75173 Q2HYD0 Q5VTW2 Q6P4Q8 Q6UWA8 Q9UN83 51312117 c1cc2c(cc1Cl)cc(o2)C(=O)NC[C@@]3(C(=O)NC(=O)N3)c4nccs4 InChI=1S/C16H11ClN4O4S/c17-9-1-2-10-8(5-9)6-11(25-10)12(22)19-7-16(14-18-3-4-26-14)13(23)20-15(24)21-16/h1-6H,7H2,(H,19,22)(H2,20,21,23,24) LBVBVIKJOWWVJX-UHFFFAOYSA-N 50033805 CHEMBL3358155 A disintegrin and metalloproteinase with thrombospondin motifs 4 Homo sapiens 8.0 ChEMBL 10.1021/acs.jmedchem.6b00398 10.7270/Q280563T 27194201 Wiley, MR; Durham, TB; Adams, LA; Chambers, MG; Lin, C; Liu, C; Marimuthu, J; Mitchell, PG; Mudra, DR; Swearingen, CA; Toth, JL; Weller, JM; Thirunavukkarasu, K 6/23/2016 2/27/2021 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50033805 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5138&target=A+disintegrin+and+metalloproteinase+with+thrombospondin+motifs+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50033805&enzyme=A+disintegrin+and+metalloproteinase+with+thrombospondin+motifs+4&column=ki&startPg=0&Increment=50&submit=Search 3PU 4WKE 86287515 103942053 CHEMBL3358155 1 MSQTGSHPGRGLAGRWLWGAQPCLLLPIVPLSWLVWLLLLLLASLLPSARLASPLPREEEIVFPEKLNGSVLPGSGAPARLLCRLQAFGETLLLELEQDSGVQVEGLTVQYLGQAPELLGGAEPGTYLTGTINGDPESVASLHWDGGALLGVLQYRGAELHLQPLEGGTPNSAGGPGAHILRRKSPASGQGPMCNVKAPLGSPSPRPRRAKRFASLSRFVETLVVADDKMAAFHGAGLKRYLLTVMAAAAKAFKHPSIRNPVSLVVTRLVILGSGEEGPQVGPSAAQTLRSFCAWQRGLNTPEDSDPDHFDTAILFTRQDLCGVSTCDTLGMADVGTVCDPARSCAIVEDDGLQSAFTAAHELGHVFNMLHDNSKPCISLNGPLSTSRHVMAPVMAHVDPEEPWSPCSARFITDFLDNGYGHCLLDKPEAPLHLPVTFPGKDYDADRQCQLTFGPDSRHCPQLPPPCAALWCSGHLNGHAMCQTKHSPWADGTPCGPAQACMGGRCLHMDQLQDFNIPQAGGWGPWGPWGDCSRTCGGGVQFSSRDCTRPVPRNGGKYCEGRRTRFRSCNTEDCPTGSALTFREEQCAAYNHRTDLFKSFPGPMDWVPRYTGVAPQDQCKLTCQAQALGYYYVLEPRVVDGTPCSPDSSSVCVQGRCIHAGCDRIIGSKKKFDKCMVCGGDGSGCSKQSGSFRKFRYGYNNVVTIPAGATHILVRQQGNPGHRSIYLALKLPDGSYALNGEYTLMPSPTDVVLPGAVSLRYSGATAASETLSGHGPLAQPLTLQVLVAGNPQDTRLRYSFFVPRPTPSTPRPTPQDWLHRRAQILEILRRRPWAGRK 4WKI,4WKE,4WK7 A disintegrin and metalloproteinase with thrombospondin motifs 4 ATS4_HUMAN O75173 Q2HYD0 Q5VTW2 Q6P4Q8 Q6UWA8 Q9UN83 51312144 c1cc2c(cc1Cl)cc(o2)C(=O)NC[C@@]3(C(=O)NC(=O)N3)c4nccs4 InChI=1S/C16H11ClN4O4S/c17-9-1-2-10-8(5-9)6-11(25-10)12(22)19-7-16(14-18-3-4-26-14)13(23)20-15(24)21-16/h1-6H,7H2,(H,19,22)(H2,20,21,23,24) LBVBVIKJOWWVJX-UHFFFAOYSA-N 50033805 CHEMBL3358155 A disintegrin and metalloproteinase with thrombospondin motifs 4 Homo sapiens 8.0 ChEMBL 10.1021/acs.jmedchem.6b00398 10.7270/Q280563T 27194201 Wiley, MR; Durham, TB; Adams, LA; Chambers, MG; Lin, C; Liu, C; Marimuthu, J; Mitchell, PG; Mudra, DR; Swearingen, CA; Toth, JL; Weller, JM; Thirunavukkarasu, K 6/23/2016 2/27/2021 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50033805 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5138&target=A+disintegrin+and+metalloproteinase+with+thrombospondin+motifs+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50033805&enzyme=A+disintegrin+and+metalloproteinase+with+thrombospondin+motifs+4&column=ki&startPg=0&Increment=50&submit=Search 3PU 4WKE 86287515 103942053 CHEMBL3358155 1 MSQTGSHPGRGLAGRWLWGAQPCLLLPIVPLSWLVWLLLLLLASLLPSARLASPLPREEEIVFPEKLNGSVLPGSGAPARLLCRLQAFGETLLLELEQDSGVQVEGLTVQYLGQAPELLGGAEPGTYLTGTINGDPESVASLHWDGGALLGVLQYRGAELHLQPLEGGTPNSAGGPGAHILRRKSPASGQGPMCNVKAPLGSPSPRPRRAKRFASLSRFVETLVVADDKMAAFHGAGLKRYLLTVMAAAAKAFKHPSIRNPVSLVVTRLVILGSGEEGPQVGPSAAQTLRSFCAWQRGLNTPEDSDPDHFDTAILFTRQDLCGVSTCDTLGMADVGTVCDPARSCAIVEDDGLQSAFTAAHELGHVFNMLHDNSKPCISLNGPLSTSRHVMAPVMAHVDPEEPWSPCSARFITDFLDNGYGHCLLDKPEAPLHLPVTFPGKDYDADRQCQLTFGPDSRHCPQLPPPCAALWCSGHLNGHAMCQTKHSPWADGTPCGPAQACMGGRCLHMDQLQDFNIPQAGGWGPWGPWGDCSRTCGGGVQFSSRDCTRPVPRNGGKYCEGRRTRFRSCNTEDCPTGSALTFREEQCAAYNHRTDLFKSFPGPMDWVPRYTGVAPQDQCKLTCQAQALGYYYVLEPRVVDGTPCSPDSSSVCVQGRCIHAGCDRIIGSKKKFDKCMVCGGDGSGCSKQSGSFRKFRYGYNNVVTIPAGATHILVRQQGNPGHRSIYLALKLPDGSYALNGEYTLMPSPTDVVLPGAVSLRYSGATAASETLSGHGPLAQPLTLQVLVAGNPQDTRLRYSFFVPRPTPSTPRPTPQDWLHRRAQILEILRRRPWAGRK 4WKI,4WKE,4WK7 A disintegrin and metalloproteinase with thrombospondin motifs 4 ATS4_HUMAN O75173 Q2HYD0 Q5VTW2 Q6P4Q8 Q6UWA8 Q9UN83 50249359 Cn1ccnc1[C@]2(C(=O)NC(=O)N2)CNC(=O)c3cc4cc(ccc4o3)Cl InChI=1S/C17H14ClN5O4/c1-23-5-4-19-14(23)17(15(25)21-16(26)22-17)8-20-13(24)12-7-9-6-10(18)2-3-11(9)27-12/h2-7H,8H2,1H3,(H,20,24)(H2,21,22,25,26) NPWGFJCNOCYDSO-UHFFFAOYSA-N 50033806 CHEMBL3358156 A disintegrin and metalloproteinase with thrombospondin motifs 4 Homo sapiens 5.0 ChEMBL 10.1021/jm501522n 10.7270/Q2K35W85 25415648 Durham, TB; Klimkowski, VJ; Rito, CJ; Marimuthu, J; Toth, JL; Liu, C; Durbin, JD; Stout, SL; Adams, L; Swearingen, C; Lin, C; Chambers, MG; Thirunavukkarasu, K; Wiley, MR 12/29/2014 3/13/2016 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50033806 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5138&target=A+disintegrin+and+metalloproteinase+with+thrombospondin+motifs+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50033806&enzyme=A+disintegrin+and+metalloproteinase+with+thrombospondin+motifs+4&column=ki&startPg=0&Increment=50&submit=Search 3PW 4WKI 86287516 103942054 CHEMBL3358156 1 MSQTGSHPGRGLAGRWLWGAQPCLLLPIVPLSWLVWLLLLLLASLLPSARLASPLPREEEIVFPEKLNGSVLPGSGAPARLLCRLQAFGETLLLELEQDSGVQVEGLTVQYLGQAPELLGGAEPGTYLTGTINGDPESVASLHWDGGALLGVLQYRGAELHLQPLEGGTPNSAGGPGAHILRRKSPASGQGPMCNVKAPLGSPSPRPRRAKRFASLSRFVETLVVADDKMAAFHGAGLKRYLLTVMAAAAKAFKHPSIRNPVSLVVTRLVILGSGEEGPQVGPSAAQTLRSFCAWQRGLNTPEDSDPDHFDTAILFTRQDLCGVSTCDTLGMADVGTVCDPARSCAIVEDDGLQSAFTAAHELGHVFNMLHDNSKPCISLNGPLSTSRHVMAPVMAHVDPEEPWSPCSARFITDFLDNGYGHCLLDKPEAPLHLPVTFPGKDYDADRQCQLTFGPDSRHCPQLPPPCAALWCSGHLNGHAMCQTKHSPWADGTPCGPAQACMGGRCLHMDQLQDFNIPQAGGWGPWGPWGDCSRTCGGGVQFSSRDCTRPVPRNGGKYCEGRRTRFRSCNTEDCPTGSALTFREEQCAAYNHRTDLFKSFPGPMDWVPRYTGVAPQDQCKLTCQAQALGYYYVLEPRVVDGTPCSPDSSSVCVQGRCIHAGCDRIIGSKKKFDKCMVCGGDGSGCSKQSGSFRKFRYGYNNVVTIPAGATHILVRQQGNPGHRSIYLALKLPDGSYALNGEYTLMPSPTDVVLPGAVSLRYSGATAASETLSGHGPLAQPLTLQVLVAGNPQDTRLRYSFFVPRPTPSTPRPTPQDWLHRRAQILEILRRRPWAGRK 4WKI,4WKE,4WK7 A disintegrin and metalloproteinase with thrombospondin motifs 4 ATS4_HUMAN O75173 Q2HYD0 Q5VTW2 Q6P4Q8 Q6UWA8 Q9UN83 51312138 Cn1ccnc1[C@]2(C(=O)NC(=O)N2)CNC(=O)c3cc4cc(ccc4o3)Cl InChI=1S/C17H14ClN5O4/c1-23-5-4-19-14(23)17(15(25)21-16(26)22-17)8-20-13(24)12-7-9-6-10(18)2-3-11(9)27-12/h2-7H,8H2,1H3,(H,20,24)(H2,21,22,25,26) NPWGFJCNOCYDSO-UHFFFAOYSA-N 50033806 CHEMBL3358156 A disintegrin and metalloproteinase with thrombospondin motifs 4 Homo sapiens 3.0 ChEMBL 10.1021/acs.jmedchem.6b00398 10.7270/Q280563T 27194201 Wiley, MR; Durham, TB; Adams, LA; Chambers, MG; Lin, C; Liu, C; Marimuthu, J; Mitchell, PG; Mudra, DR; Swearingen, CA; Toth, JL; Weller, JM; Thirunavukkarasu, K 6/23/2016 2/27/2021 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50033806 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5138&target=A+disintegrin+and+metalloproteinase+with+thrombospondin+motifs+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50033806&enzyme=A+disintegrin+and+metalloproteinase+with+thrombospondin+motifs+4&column=ki&startPg=0&Increment=50&submit=Search 3PW 4WKI 86287516 103942054 CHEMBL3358156 1 MSQTGSHPGRGLAGRWLWGAQPCLLLPIVPLSWLVWLLLLLLASLLPSARLASPLPREEEIVFPEKLNGSVLPGSGAPARLLCRLQAFGETLLLELEQDSGVQVEGLTVQYLGQAPELLGGAEPGTYLTGTINGDPESVASLHWDGGALLGVLQYRGAELHLQPLEGGTPNSAGGPGAHILRRKSPASGQGPMCNVKAPLGSPSPRPRRAKRFASLSRFVETLVVADDKMAAFHGAGLKRYLLTVMAAAAKAFKHPSIRNPVSLVVTRLVILGSGEEGPQVGPSAAQTLRSFCAWQRGLNTPEDSDPDHFDTAILFTRQDLCGVSTCDTLGMADVGTVCDPARSCAIVEDDGLQSAFTAAHELGHVFNMLHDNSKPCISLNGPLSTSRHVMAPVMAHVDPEEPWSPCSARFITDFLDNGYGHCLLDKPEAPLHLPVTFPGKDYDADRQCQLTFGPDSRHCPQLPPPCAALWCSGHLNGHAMCQTKHSPWADGTPCGPAQACMGGRCLHMDQLQDFNIPQAGGWGPWGPWGDCSRTCGGGVQFSSRDCTRPVPRNGGKYCEGRRTRFRSCNTEDCPTGSALTFREEQCAAYNHRTDLFKSFPGPMDWVPRYTGVAPQDQCKLTCQAQALGYYYVLEPRVVDGTPCSPDSSSVCVQGRCIHAGCDRIIGSKKKFDKCMVCGGDGSGCSKQSGSFRKFRYGYNNVVTIPAGATHILVRQQGNPGHRSIYLALKLPDGSYALNGEYTLMPSPTDVVLPGAVSLRYSGATAASETLSGHGPLAQPLTLQVLVAGNPQDTRLRYSFFVPRPTPSTPRPTPQDWLHRRAQILEILRRRPWAGRK 4WKI,4WKE,4WK7 A disintegrin and metalloproteinase with thrombospondin motifs 4 ATS4_HUMAN O75173 Q2HYD0 Q5VTW2 Q6P4Q8 Q6UWA8 Q9UN83 51312161 Cn1ccnc1[C@]2(C(=O)NC(=O)N2)CNC(=O)c3cc4cc(ccc4o3)Cl InChI=1S/C17H14ClN5O4/c1-23-5-4-19-14(23)17(15(25)21-16(26)22-17)8-20-13(24)12-7-9-6-10(18)2-3-11(9)27-12/h2-7H,8H2,1H3,(H,20,24)(H2,21,22,25,26) NPWGFJCNOCYDSO-UHFFFAOYSA-N 50033806 CHEMBL3358156 A disintegrin and metalloproteinase with thrombospondin motifs 4 Homo sapiens 3.0 ChEMBL 10.1021/acs.jmedchem.6b00398 10.7270/Q280563T 27194201 Wiley, MR; Durham, TB; Adams, LA; Chambers, MG; Lin, C; Liu, C; Marimuthu, J; Mitchell, PG; Mudra, DR; Swearingen, CA; Toth, JL; Weller, JM; Thirunavukkarasu, K 6/23/2016 2/27/2021 Eli Lilly http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50033806 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5138&target=A+disintegrin+and+metalloproteinase+with+thrombospondin+motifs+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50033806&enzyme=A+disintegrin+and+metalloproteinase+with+thrombospondin+motifs+4&column=ki&startPg=0&Increment=50&submit=Search 3PW 4WKI 86287516 103942054 CHEMBL3358156 1 MSQTGSHPGRGLAGRWLWGAQPCLLLPIVPLSWLVWLLLLLLASLLPSARLASPLPREEEIVFPEKLNGSVLPGSGAPARLLCRLQAFGETLLLELEQDSGVQVEGLTVQYLGQAPELLGGAEPGTYLTGTINGDPESVASLHWDGGALLGVLQYRGAELHLQPLEGGTPNSAGGPGAHILRRKSPASGQGPMCNVKAPLGSPSPRPRRAKRFASLSRFVETLVVADDKMAAFHGAGLKRYLLTVMAAAAKAFKHPSIRNPVSLVVTRLVILGSGEEGPQVGPSAAQTLRSFCAWQRGLNTPEDSDPDHFDTAILFTRQDLCGVSTCDTLGMADVGTVCDPARSCAIVEDDGLQSAFTAAHELGHVFNMLHDNSKPCISLNGPLSTSRHVMAPVMAHVDPEEPWSPCSARFITDFLDNGYGHCLLDKPEAPLHLPVTFPGKDYDADRQCQLTFGPDSRHCPQLPPPCAALWCSGHLNGHAMCQTKHSPWADGTPCGPAQACMGGRCLHMDQLQDFNIPQAGGWGPWGPWGDCSRTCGGGVQFSSRDCTRPVPRNGGKYCEGRRTRFRSCNTEDCPTGSALTFREEQCAAYNHRTDLFKSFPGPMDWVPRYTGVAPQDQCKLTCQAQALGYYYVLEPRVVDGTPCSPDSSSVCVQGRCIHAGCDRIIGSKKKFDKCMVCGGDGSGCSKQSGSFRKFRYGYNNVVTIPAGATHILVRQQGNPGHRSIYLALKLPDGSYALNGEYTLMPSPTDVVLPGAVSLRYSGATAASETLSGHGPLAQPLTLQVLVAGNPQDTRLRYSFFVPRPTPSTPRPTPQDWLHRRAQILEILRRRPWAGRK 4WKI,4WKE,4WK7 A disintegrin and metalloproteinase with thrombospondin motifs 4 ATS4_HUMAN O75173 Q2HYD0 Q5VTW2 Q6P4Q8 Q6UWA8 Q9UN83 771773 COC(=O)N1CCC[C@@H]([C@@H]1COC2CCC(CC2)c3ccccc3)NS(=O)(=O)C InChI=1S/C21H32N2O5S/c1-27-21(24)23-14-6-9-19(22-29(2,25)26)20(23)15-28-18-12-10-17(11-13-18)16-7-4-3-5-8-16/h3-5,7-8,17-20,22H,6,9-15H2,1-2H3 UXZAJSZFFARTEI-UHFFFAOYSA-N 386067 methyl (2R,3S)-3- ((methylsulfonyl)amino)-2-(((cis-4- phenylcyclohexyl)oxy)methyl)- piperidine-1-carboxylate::US10287305, Example 5::US10508083, Example 191::US11292766, Example 191 Orexin receptor type 2 Homo sapiens 2.20 US Patent 10.7270/Q2Z321Z2 aid1798665 US10287305 Fujimoto, T; Rikimaru, K; Sugimoto, H; Matsumoto, T 5/14/2019 2/27/2020 Takeda Pharmaceutical http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=386067 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5447&target=Orexin+receptor+type+2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=386067&enzyme=Orexin+receptor+type+2&column=ki&startPg=0&Increment=50&submit=Search A6F 7SQO,7SR8 130310079 404855226 1 MSGTKLEDSPPCRNWSSASELNETQEPFLNPTDYDDEEFLRYLWREYLHPKEYEWVLIAGYIIVFVVALIGNVLVCVAVWKNHHMRTVTNYFIVNLSLADVLVTITCLPATLVVDITETWFFGQSLCKVIPYLQTVSVSVSVLTLSCIALDRWYAICHPLMFKSTAKRARNSIVIIWIVSCIIMIPQAIVMECSTVFPGLANKTTLFTVCDERWGGEIYPKMYHICFFLVTYMAPLCLMVLAYLQIFRKLWCRQIPGTSSVVQRKWKPLQPVSQPRGPGQPTKSRMSAVAAEIKQIRARRKTARMLMIVLLVFAICYLPISILNVLKRVFGMFAHTEDRETVYAWFTFSHWLVYANSAANPIIYNFLSGKFREEFKAAFSCCCLGVHHRQEDRLTRGRTSTESRKSLTTQISNFDNISKLSEQVVLTSISTLPAANGAGPLQNW 4S0V,5WS3,5WQC Orexin receptor type 2 OX2R_HUMAN O43614 Q5VTM0 849682 COC(=O)N1CCC[C@@H]([C@@H]1COC2CCC(CC2)c3ccccc3)NS(=O)(=O)C InChI=1S/C21H32N2O5S/c1-27-21(24)23-14-6-9-19(22-29(2,25)26)20(23)15-28-18-12-10-17(11-13-18)16-7-4-3-5-8-16/h3-5,7-8,17-20,22H,6,9-15H2,1-2H3 UXZAJSZFFARTEI-UHFFFAOYSA-N 386067 methyl (2R,3S)-3- ((methylsulfonyl)amino)-2-(((cis-4- phenylcyclohexyl)oxy)methyl)- piperidine-1-carboxylate::US10287305, Example 5::US10508083, Example 191::US11292766, Example 191 Orexin receptor type 2 Homo sapiens 2.20 US Patent 10.7270/Q29S1TD1 aid1804003 US10508083 Fujimoto, T; Rikimaru, K; Fukuda, K; Sugimoto, H; Matsumoto, T 12/17/2019 10/2/2020 Takeda Pharmaceutical http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=386067 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5447&target=Orexin+receptor+type+2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=386067&enzyme=Orexin+receptor+type+2&column=ki&startPg=0&Increment=50&submit=Search A6F 7SQO,7SR8 130310079 404855226 1 MSGTKLEDSPPCRNWSSASELNETQEPFLNPTDYDDEEFLRYLWREYLHPKEYEWVLIAGYIIVFVVALIGNVLVCVAVWKNHHMRTVTNYFIVNLSLADVLVTITCLPATLVVDITETWFFGQSLCKVIPYLQTVSVSVSVLTLSCIALDRWYAICHPLMFKSTAKRARNSIVIIWIVSCIIMIPQAIVMECSTVFPGLANKTTLFTVCDERWGGEIYPKMYHICFFLVTYMAPLCLMVLAYLQIFRKLWCRQIPGTSSVVQRKWKPLQPVSQPRGPGQPTKSRMSAVAAEIKQIRARRKTARMLMIVLLVFAICYLPISILNVLKRVFGMFAHTEDRETVYAWFTFSHWLVYANSAANPIIYNFLSGKFREEFKAAFSCCCLGVHHRQEDRLTRGRTSTESRKSLTTQISNFDNISKLSEQVVLTSISTLPAANGAGPLQNW 4S0V,5WS3,5WQC Orexin receptor type 2 OX2R_HUMAN O43614 Q5VTM0 849808 COC(=O)N1CCC[C@@H]([C@@H]1COC2CCC(CC2)c3ccccc3)NS(=O)(=O)C InChI=1S/C21H32N2O5S/c1-27-21(24)23-14-6-9-19(22-29(2,25)26)20(23)15-28-18-12-10-17(11-13-18)16-7-4-3-5-8-16/h3-5,7-8,17-20,22H,6,9-15H2,1-2H3 UXZAJSZFFARTEI-UHFFFAOYSA-N 386067 methyl (2R,3S)-3- ((methylsulfonyl)amino)-2-(((cis-4- phenylcyclohexyl)oxy)methyl)- piperidine-1-carboxylate::US10287305, Example 5::US10508083, Example 191::US11292766, Example 191 Orexin receptor type 2 Homo sapiens 2.90 US Patent 10.7270/Q29S1TD1 aid1804003 US10508083 Fujimoto, T; Rikimaru, K; Fukuda, K; Sugimoto, H; Matsumoto, T 12/17/2019 10/2/2020 Takeda Pharmaceutical http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=386067 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5447&target=Orexin+receptor+type+2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=386067&enzyme=Orexin+receptor+type+2&column=ki&startPg=0&Increment=50&submit=Search A6F 7SQO,7SR8 130310079 404855226 1 MSGTKLEDSPPCRNWSSASELNETQEPFLNPTDYDDEEFLRYLWREYLHPKEYEWVLIAGYIIVFVVALIGNVLVCVAVWKNHHMRTVTNYFIVNLSLADVLVTITCLPATLVVDITETWFFGQSLCKVIPYLQTVSVSVSVLTLSCIALDRWYAICHPLMFKSTAKRARNSIVIIWIVSCIIMIPQAIVMECSTVFPGLANKTTLFTVCDERWGGEIYPKMYHICFFLVTYMAPLCLMVLAYLQIFRKLWCRQIPGTSSVVQRKWKPLQPVSQPRGPGQPTKSRMSAVAAEIKQIRARRKTARMLMIVLLVFAICYLPISILNVLKRVFGMFAHTEDRETVYAWFTFSHWLVYANSAANPIIYNFLSGKFREEFKAAFSCCCLGVHHRQEDRLTRGRTSTESRKSLTTQISNFDNISKLSEQVVLTSISTLPAANGAGPLQNW 4S0V,5WS3,5WQC Orexin receptor type 2 OX2R_HUMAN O43614 Q5VTM0 1155373 COC(=O)N1CCC[C@@H]([C@@H]1COC2CCC(CC2)c3ccccc3)NS(=O)(=O)C InChI=1S/C21H32N2O5S/c1-27-21(24)23-14-6-9-19(22-29(2,25)26)20(23)15-28-18-12-10-17(11-13-18)16-7-4-3-5-8-16/h3-5,7-8,17-20,22H,6,9-15H2,1-2H3 UXZAJSZFFARTEI-UHFFFAOYSA-N 386067 methyl (2R,3S)-3- ((methylsulfonyl)amino)-2-(((cis-4- phenylcyclohexyl)oxy)methyl)- piperidine-1-carboxylate::US10287305, Example 5::US10508083, Example 191::US11292766, Example 191 Orexin receptor type 2 Homo sapiens 2.20 US Patent 10.7270/Q2CZ3BCW aid1806423 US11292766 Fujimoto, T; Rikimaru, K; Fukuda, K; Sugimoto, H; Matsumoto, T; Tokunaga, N; Hirozane, M 4/5/2022 7/21/2022 Takeda Pharmaceutical http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=386067 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5447&target=Orexin+receptor+type+2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=386067&enzyme=Orexin+receptor+type+2&column=ki&startPg=0&Increment=50&submit=Search A6F 7SQO,7SR8 130310079 404855226 1 MSGTKLEDSPPCRNWSSASELNETQEPFLNPTDYDDEEFLRYLWREYLHPKEYEWVLIAGYIIVFVVALIGNVLVCVAVWKNHHMRTVTNYFIVNLSLADVLVTITCLPATLVVDITETWFFGQSLCKVIPYLQTVSVSVSVLTLSCIALDRWYAICHPLMFKSTAKRARNSIVIIWIVSCIIMIPQAIVMECSTVFPGLANKTTLFTVCDERWGGEIYPKMYHICFFLVTYMAPLCLMVLAYLQIFRKLWCRQIPGTSSVVQRKWKPLQPVSQPRGPGQPTKSRMSAVAAEIKQIRARRKTARMLMIVLLVFAICYLPISILNVLKRVFGMFAHTEDRETVYAWFTFSHWLVYANSAANPIIYNFLSGKFREEFKAAFSCCCLGVHHRQEDRLTRGRTSTESRKSLTTQISNFDNISKLSEQVVLTSISTLPAANGAGPLQNW 4S0V,5WS3,5WQC Orexin receptor type 2 OX2R_HUMAN O43614 Q5VTM0 1155499 COC(=O)N1CCC[C@@H]([C@@H]1COC2CCC(CC2)c3ccccc3)NS(=O)(=O)C InChI=1S/C21H32N2O5S/c1-27-21(24)23-14-6-9-19(22-29(2,25)26)20(23)15-28-18-12-10-17(11-13-18)16-7-4-3-5-8-16/h3-5,7-8,17-20,22H,6,9-15H2,1-2H3 UXZAJSZFFARTEI-UHFFFAOYSA-N 386067 methyl (2R,3S)-3- ((methylsulfonyl)amino)-2-(((cis-4- phenylcyclohexyl)oxy)methyl)- piperidine-1-carboxylate::US10287305, Example 5::US10508083, Example 191::US11292766, Example 191 Orexin receptor type 2 Homo sapiens 2.90 US Patent 10.7270/Q2CZ3BCW aid1806423 US11292766 Fujimoto, T; Rikimaru, K; Fukuda, K; Sugimoto, H; Matsumoto, T; Tokunaga, N; Hirozane, M 4/5/2022 7/21/2022 Takeda Pharmaceutical http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=386067 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5447&target=Orexin+receptor+type+2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=386067&enzyme=Orexin+receptor+type+2&column=ki&startPg=0&Increment=50&submit=Search A6F 7SQO,7SR8 130310079 404855226 1 MSGTKLEDSPPCRNWSSASELNETQEPFLNPTDYDDEEFLRYLWREYLHPKEYEWVLIAGYIIVFVVALIGNVLVCVAVWKNHHMRTVTNYFIVNLSLADVLVTITCLPATLVVDITETWFFGQSLCKVIPYLQTVSVSVSVLTLSCIALDRWYAICHPLMFKSTAKRARNSIVIIWIVSCIIMIPQAIVMECSTVFPGLANKTTLFTVCDERWGGEIYPKMYHICFFLVTYMAPLCLMVLAYLQIFRKLWCRQIPGTSSVVQRKWKPLQPVSQPRGPGQPTKSRMSAVAAEIKQIRARRKTARMLMIVLLVFAICYLPISILNVLKRVFGMFAHTEDRETVYAWFTFSHWLVYANSAANPIIYNFLSGKFREEFKAAFSCCCLGVHHRQEDRLTRGRTSTESRKSLTTQISNFDNISKLSEQVVLTSISTLPAANGAGPLQNW 4S0V,5WS3,5WQC Orexin receptor type 2 OX2R_HUMAN O43614 Q5VTM0 51435079 COC(=O)N1CCC[C@@H]([C@@H]1COC2CCC(CC2)c3ccccc3)NS(=O)(=O)C InChI=1S/C21H32N2O5S/c1-27-21(24)23-14-6-9-19(22-29(2,25)26)20(23)15-28-18-12-10-17(11-13-18)16-7-4-3-5-8-16/h3-5,7-8,17-20,22H,6,9-15H2,1-2H3 UXZAJSZFFARTEI-UHFFFAOYSA-N 386067 methyl (2R,3S)-3- ((methylsulfonyl)amino)-2-(((cis-4- phenylcyclohexyl)oxy)methyl)- piperidine-1-carboxylate::US10287305, Example 5::US10508083, Example 191::US11292766, Example 191 Orexin receptor type 2 Homo sapiens 5500 ChEMBL 10.1021/acs.jmedchem.1c00841 10.7270/Q2W66QMS 34101446 Zhang, D; Perrey, DA; Decker, AM; Langston, TL; Mavanji, V; Harris, DL; Kotz, CM; Zhang, Y 6/24/2021 3/4/2023 Research Triangle Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=386067 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5447&target=Orexin+receptor+type+2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=386067&enzyme=Orexin+receptor+type+2&column=ki&startPg=0&Increment=50&submit=Search A6F 7SQO,7SR8 130310079 404855226 1 MSGTKLEDSPPCRNWSSASELNETQEPFLNPTDYDDEEFLRYLWREYLHPKEYEWVLIAGYIIVFVVALIGNVLVCVAVWKNHHMRTVTNYFIVNLSLADVLVTITCLPATLVVDITETWFFGQSLCKVIPYLQTVSVSVSVLTLSCIALDRWYAICHPLMFKSTAKRARNSIVIIWIVSCIIMIPQAIVMECSTVFPGLANKTTLFTVCDERWGGEIYPKMYHICFFLVTYMAPLCLMVLAYLQIFRKLWCRQIPGTSSVVQRKWKPLQPVSQPRGPGQPTKSRMSAVAAEIKQIRARRKTARMLMIVLLVFAICYLPISILNVLKRVFGMFAHTEDRETVYAWFTFSHWLVYANSAANPIIYNFLSGKFREEFKAAFSCCCLGVHHRQEDRLTRGRTSTESRKSLTTQISNFDNISKLSEQVVLTSISTLPAANGAGPLQNW 4S0V,5WS3,5WQC Orexin receptor type 2 OX2R_HUMAN O43614 Q5VTM0 51451928 COC(=O)N1CCC[C@@H]([C@@H]1COC2CCC(CC2)c3ccccc3)NS(=O)(=O)C InChI=1S/C21H32N2O5S/c1-27-21(24)23-14-6-9-19(22-29(2,25)26)20(23)15-28-18-12-10-17(11-13-18)16-7-4-3-5-8-16/h3-5,7-8,17-20,22H,6,9-15H2,1-2H3 UXZAJSZFFARTEI-UHFFFAOYSA-N 386067 methyl (2R,3S)-3- ((methylsulfonyl)amino)-2-(((cis-4- phenylcyclohexyl)oxy)methyl)- piperidine-1-carboxylate::US10287305, Example 5::US10508083, Example 191::US11292766, Example 191 Orexin receptor type 2 Homo sapiens 5.5 ChEMBL 10.1021/acsmedchemlett.1c00626 10.7270/Q2NS0ZTS 35295087 Fujimoto, T; Rikimaru, K; Fukuda, K; Sugimoto, H; Masuda, K; Ohyabu, N; Banno, Y; Tokunaga, N; Kawamoto, T; Tomata, Y; Kumagai, Y; Iida, M; Nagano, Y; Yoneyama-Hirozane, M; Shimizu, Y; Sasa, K; Ishikawa, T; Yukitake, H; Ito, M; Aoyama, K; Matsumoto, T 3/10/2022 3/7/2023 Takeda Pharmaceutical http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=386067 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5447&target=Orexin+receptor+type+2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=386067&enzyme=Orexin+receptor+type+2&column=ki&startPg=0&Increment=50&submit=Search A6F 7SQO,7SR8 130310079 404855226 1 MSGTKLEDSPPCRNWSSASELNETQEPFLNPTDYDDEEFLRYLWREYLHPKEYEWVLIAGYIIVFVVALIGNVLVCVAVWKNHHMRTVTNYFIVNLSLADVLVTITCLPATLVVDITETWFFGQSLCKVIPYLQTVSVSVSVLTLSCIALDRWYAICHPLMFKSTAKRARNSIVIIWIVSCIIMIPQAIVMECSTVFPGLANKTTLFTVCDERWGGEIYPKMYHICFFLVTYMAPLCLMVLAYLQIFRKLWCRQIPGTSSVVQRKWKPLQPVSQPRGPGQPTKSRMSAVAAEIKQIRARRKTARMLMIVLLVFAICYLPISILNVLKRVFGMFAHTEDRETVYAWFTFSHWLVYANSAANPIIYNFLSGKFREEFKAAFSCCCLGVHHRQEDRLTRGRTSTESRKSLTTQISNFDNISKLSEQVVLTSISTLPAANGAGPLQNW 4S0V,5WS3,5WQC Orexin receptor type 2 OX2R_HUMAN O43614 Q5VTM0 51479461 COC(=O)N1CCC[C@@H]([C@@H]1COC2CCC(CC2)c3ccccc3)NS(=O)(=O)C InChI=1S/C21H32N2O5S/c1-27-21(24)23-14-6-9-19(22-29(2,25)26)20(23)15-28-18-12-10-17(11-13-18)16-7-4-3-5-8-16/h3-5,7-8,17-20,22H,6,9-15H2,1-2H3 UXZAJSZFFARTEI-UHFFFAOYSA-N 386067 methyl (2R,3S)-3- ((methylsulfonyl)amino)-2-(((cis-4- phenylcyclohexyl)oxy)methyl)- piperidine-1-carboxylate::US10287305, Example 5::US10508083, Example 191::US11292766, Example 191 Orexin receptor type 2 Homo sapiens 5.5 ChEMBL 10.7270/Q28919WZ 35007725 Hino, T; Saitoh, T; Nagumo, Y; Yamamoto, N; Kutsumura, N; Irukayama-Tomobe, Y; Ishikawa, Y; Tanimura, R; Yanagisawa, M; Nagase, H 3/1/2022 6/22/2023 University of Tsukuba http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=386067 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5447&target=Orexin+receptor+type+2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=386067&enzyme=Orexin+receptor+type+2&column=ki&startPg=0&Increment=50&submit=Search A6F 7SQO,7SR8 130310079 404855226 1 MSGTKLEDSPPCRNWSSASELNETQEPFLNPTDYDDEEFLRYLWREYLHPKEYEWVLIAGYIIVFVVALIGNVLVCVAVWKNHHMRTVTNYFIVNLSLADVLVTITCLPATLVVDITETWFFGQSLCKVIPYLQTVSVSVSVLTLSCIALDRWYAICHPLMFKSTAKRARNSIVIIWIVSCIIMIPQAIVMECSTVFPGLANKTTLFTVCDERWGGEIYPKMYHICFFLVTYMAPLCLMVLAYLQIFRKLWCRQIPGTSSVVQRKWKPLQPVSQPRGPGQPTKSRMSAVAAEIKQIRARRKTARMLMIVLLVFAICYLPISILNVLKRVFGMFAHTEDRETVYAWFTFSHWLVYANSAANPIIYNFLSGKFREEFKAAFSCCCLGVHHRQEDRLTRGRTSTESRKSLTTQISNFDNISKLSEQVVLTSISTLPAANGAGPLQNW 4S0V,5WS3,5WQC Orexin receptor type 2 OX2R_HUMAN O43614 Q5VTM0 51479863 COC(=O)N1CCC[C@@H]([C@@H]1COC2CCC(CC2)c3ccccc3)NS(=O)(=O)C InChI=1S/C21H32N2O5S/c1-27-21(24)23-14-6-9-19(22-29(2,25)26)20(23)15-28-18-12-10-17(11-13-18)16-7-4-3-5-8-16/h3-5,7-8,17-20,22H,6,9-15H2,1-2H3 UXZAJSZFFARTEI-UHFFFAOYSA-N 386067 methyl (2R,3S)-3- ((methylsulfonyl)amino)-2-(((cis-4- phenylcyclohexyl)oxy)methyl)- piperidine-1-carboxylate::US10287305, Example 5::US10508083, Example 191::US11292766, Example 191 Orexin receptor type 2 Homo sapiens 5.5 ChEMBL 10.7270/Q23J3J0T 35051577 Iio, K; Saitoh, T; Ohshita, R; Hino, T; Amezawa, M; Takayama, Y; Nagumo, Y; Yamamoto, N; Kutsumura, N; Irukayama-Tomobe, Y; Ishikawa, Y; Tanimura, R; Yanagisawa, M; Nagase, H 3/15/2022 6/22/2023 University of Tsukuba http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=386067 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5447&target=Orexin+receptor+type+2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=386067&enzyme=Orexin+receptor+type+2&column=ki&startPg=0&Increment=50&submit=Search A6F 7SQO,7SR8 130310079 404855226 1 MSGTKLEDSPPCRNWSSASELNETQEPFLNPTDYDDEEFLRYLWREYLHPKEYEWVLIAGYIIVFVVALIGNVLVCVAVWKNHHMRTVTNYFIVNLSLADVLVTITCLPATLVVDITETWFFGQSLCKVIPYLQTVSVSVSVLTLSCIALDRWYAICHPLMFKSTAKRARNSIVIIWIVSCIIMIPQAIVMECSTVFPGLANKTTLFTVCDERWGGEIYPKMYHICFFLVTYMAPLCLMVLAYLQIFRKLWCRQIPGTSSVVQRKWKPLQPVSQPRGPGQPTKSRMSAVAAEIKQIRARRKTARMLMIVLLVFAICYLPISILNVLKRVFGMFAHTEDRETVYAWFTFSHWLVYANSAANPIIYNFLSGKFREEFKAAFSCCCLGVHHRQEDRLTRGRTSTESRKSLTTQISNFDNISKLSEQVVLTSISTLPAANGAGPLQNW 4S0V,5WS3,5WQC Orexin receptor type 2 OX2R_HUMAN O43614 Q5VTM0 771899 COC(=O)N1CCC[C@@H]([C@@H]1COC2CCC(CC2)c3ccccc3)NS(=O)(=O)C InChI=1S/C21H32N2O5S/c1-27-21(24)23-14-6-9-19(22-29(2,25)26)20(23)15-28-18-12-10-17(11-13-18)16-7-4-3-5-8-16/h3-5,7-8,17-20,22H,6,9-15H2,1-2H3 UXZAJSZFFARTEI-UHFFFAOYSA-N 386216 methyl-d3 (2R,3S)-3- ((methylsulfonyl)amino)-2-(((cis-4- phenylcyclohexyl)oxy)methyl)- piperidine-1-carboxylate::US10287305, Example 191 Orexin receptor type 2 Homo sapiens 2.90 US Patent 10.7270/Q2Z321Z2 aid1798665 US10287305 Fujimoto, T; Rikimaru, K; Sugimoto, H; Matsumoto, T 5/14/2019 2/27/2020 Takeda Pharmaceutical http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=386216 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5447&target=Orexin+receptor+type+2&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=386216&enzyme=Orexin+receptor+type+2&column=ki&startPg=0&Increment=50&submit=Search A6F 7SQO,7SR8 130310079 404855373 1 MSGTKLEDSPPCRNWSSASELNETQEPFLNPTDYDDEEFLRYLWREYLHPKEYEWVLIAGYIIVFVVALIGNVLVCVAVWKNHHMRTVTNYFIVNLSLADVLVTITCLPATLVVDITETWFFGQSLCKVIPYLQTVSVSVSVLTLSCIALDRWYAICHPLMFKSTAKRARNSIVIIWIVSCIIMIPQAIVMECSTVFPGLANKTTLFTVCDERWGGEIYPKMYHICFFLVTYMAPLCLMVLAYLQIFRKLWCRQIPGTSSVVQRKWKPLQPVSQPRGPGQPTKSRMSAVAAEIKQIRARRKTARMLMIVLLVFAICYLPISILNVLKRVFGMFAHTEDRETVYAWFTFSHWLVYANSAANPIIYNFLSGKFREEFKAAFSCCCLGVHHRQEDRLTRGRTSTESRKSLTTQISNFDNISKLSEQVVLTSISTLPAANGAGPLQNW 4S0V,5WS3,5WQC Orexin receptor type 2 OX2R_HUMAN O43614 Q5VTM0 605121 CCCN1c2ccc(cc2CCC1=O)NS(=O)(=O)Cc3ccc(cc3)C InChI=1S/C20H24N2O3S/c1-3-12-22-19-10-9-18(13-17(19)8-11-20(22)23)21-26(24,25)14-16-6-4-15(2)5-7-16/h4-7,9-10,13,21H,3,8,11-12,14H2,1-2H3 IVHKSUMLZQXFPR-UHFFFAOYSA-N 313186 US10167261, Compound Quinabactin Abscisic acid receptor PYL1/Protein phosphatase 2C 16 Mouse-ear cress 104 US Patent 10.7270/Q2HQ420V aid1796429 US10167261 Loiseleur, O; Wendeborn, SV; Cutler, SR 1/1/2019 4/24/2019 University of California http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=313186 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=173&target=Abscisic+acid+receptor+PYL1%2FProtein+phosphatase+2C+16&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=313186&enzyme=Abscisic+acid+receptor+PYL1%2FProtein+phosphatase+2C+16&column=ki&startPg=0&Increment=50&submit=Search A1O 4LA7,8AYA,4LG5 16927350 383540105 2 MEEMTPAVAMTLSLAANTMCESSPVEITQLKNVTDAADLLSDSENQSFCNGGTECTMEDVSELEEVGEQDLLKTLSDTRSGSSNVFDEDDVLSVVEDNSAVISEGLLVVDAGSELSLSNTAMEIDNGRVLATAIIVGESSIEQVPTAEVLIAGVNQDTNTSEVVIRLPDENSNHLVKGRSVYELDCIPLWGTVSIQGNRSEMEDAFAVSPHFLKLPIKMLMGDHEGMSPSLTHLTGHFFGVYDGHGGHKVADYCRDRLHFALAEEIERIKDELCKRNTGEGRQVQWDKVFTSCFLTVDGEIEGKIGRAVVGSSDKVLEAVASETVGSTAVVALVCSSHIVVSNCGDSRAVLFRGKEAMPLSVDHKPDREDEYARIENAGGKVIQWQGARVFGVLAMSRSIGDRYLKPYVIPEPEVTFMPRSREDECLILASDGLWDVMNNQEVCEIARRRILMWHKKNGAPPLAERGKGIDPACQAAADYLSMLALQKGSKDNISIIVIDLKAQRKFKTRT 4DS8,5VT7,5VSR,5VSQ,5VS5,5VRO,5VR7,4LGB,4LGA,4LG5,3NMT,5JO2,5JO1,5OR6,5OR2,3ZVU,3QN1,8AY8,7AVW,4WVO,4LA7,6ZUC,3KB3 Protein phosphatase 2C 16 P2C16_ARATH Q9CAJ0 C0Z251 O81709 Q0WLM7 MANSESSSSPVNEEENSQRISTLHHQTMPSDLTQDEFTQLSQSIAEFHTYQLGNGRCSSLLAQRIHAPPETVWSVVRRFDRPQIYKHFIKSCNVSEDFEMRVGCTRDVNVISGLPANTSRERLDLLDDDRRVTGFSITGGEHRLRNYKSVTTVHRFEKEEEEERIWTVVLESYVVDVPEGNSEEDTRLFADTVIRLNLQKLASITEAMNRNNNNNNSSQVR 3JRS,3NEG,3NEF,3KDJ,3JRQ,3NMN,3KAY,9J6I Abscisic acid receptor PYL1 PYL1_ARATH Q8VZS8 Q9FIP6 605122 CCCN1c2ccc(cc2CCC1=O)NS(=O)(=O)Cc3ccc(cc3)C InChI=1S/C20H24N2O3S/c1-3-12-22-19-10-9-18(13-17(19)8-11-20(22)23)21-26(24,25)14-16-6-4-15(2)5-7-16/h4-7,9-10,13,21H,3,8,11-12,14H2,1-2H3 IVHKSUMLZQXFPR-UHFFFAOYSA-N 313186 US10167261, Compound Quinabactin Abscisic acid receptor PYL2/Protein phosphatase 2C 16 Mouse-ear cress 262 US Patent 10.7270/Q2HQ420V aid1796429 US10167261 Loiseleur, O; Wendeborn, SV; Cutler, SR 1/1/2019 4/24/2019 University of California http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=313186 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=176&target=Abscisic+acid+receptor+PYL2%2FProtein+phosphatase+2C+16&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=313186&enzyme=Abscisic+acid+receptor+PYL2%2FProtein+phosphatase+2C+16&column=ki&startPg=0&Increment=50&submit=Search A1O 4LA7,8AYA,4LG5 16927350 383540105 2 MEEMTPAVAMTLSLAANTMCESSPVEITQLKNVTDAADLLSDSENQSFCNGGTECTMEDVSELEEVGEQDLLKTLSDTRSGSSNVFDEDDVLSVVEDNSAVISEGLLVVDAGSELSLSNTAMEIDNGRVLATAIIVGESSIEQVPTAEVLIAGVNQDTNTSEVVIRLPDENSNHLVKGRSVYELDCIPLWGTVSIQGNRSEMEDAFAVSPHFLKLPIKMLMGDHEGMSPSLTHLTGHFFGVYDGHGGHKVADYCRDRLHFALAEEIERIKDELCKRNTGEGRQVQWDKVFTSCFLTVDGEIEGKIGRAVVGSSDKVLEAVASETVGSTAVVALVCSSHIVVSNCGDSRAVLFRGKEAMPLSVDHKPDREDEYARIENAGGKVIQWQGARVFGVLAMSRSIGDRYLKPYVIPEPEVTFMPRSREDECLILASDGLWDVMNNQEVCEIARRRILMWHKKNGAPPLAERGKGIDPACQAAADYLSMLALQKGSKDNISIIVIDLKAQRKFKTRT 4DS8,5VT7,5VSR,5VSQ,5VS5,5VRO,5VR7,4LGB,4LGA,4LG5,3NMT,5JO2,5JO1,5OR6,5OR2,3ZVU,3QN1,8AY8,7AVW,4WVO,4LA7,6ZUC,3KB3 Protein phosphatase 2C 16 P2C16_ARATH Q9CAJ0 C0Z251 O81709 Q0WLM7 MSSSPAVKGLTDEEQKTLEPVIKTYHQFEPDPTTCTSLITQRIHAPASVVWPLIRRFDNPERYKHFVKRCRLISGDGDVGSVREVTVISGLPASTSTERLEFVDDDHRVLSFRVVGGEHRLKNYKSVTSVNEFLNQDSGKVYTVVLESYTVDIPEGNTEEDTKMFVDTVVKLNLQKLGVAATSAPMHDDE 5JNN,3NS2,3NR4,3KL1,3KDI,3KDH,4LA7,3NJ0,3NMH,3KB3,3KB0,3KAZ,5VT7,5VSR,5VSQ,5VS5,5VRO,5VR7,4LGB,4LGA,4LG5,3UJL Abscisic acid receptor PYL2 PYL2_ARATH O80992 605121 CCCN1c2ccc(cc2CCC1=O)NS(=O)(=O)Cc3ccc(cc3)C InChI=1S/C20H24N2O3S/c1-3-12-22-19-10-9-18(13-17(19)8-11-20(22)23)21-26(24,25)14-16-6-4-15(2)5-7-16/h4-7,9-10,13,21H,3,8,11-12,14H2,1-2H3 IVHKSUMLZQXFPR-UHFFFAOYSA-N 313186 US10167261, Compound Quinabactin Abscisic acid receptor PYL1/Protein phosphatase 2C 16 Mouse-ear cress 104 US Patent 10.7270/Q2HQ420V aid1796429 US10167261 Loiseleur, O; Wendeborn, SV; Cutler, SR 1/1/2019 4/24/2019 University of California http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=313186 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=173&target=Abscisic+acid+receptor+PYL1%2FProtein+phosphatase+2C+16&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=313186&enzyme=Abscisic+acid+receptor+PYL1%2FProtein+phosphatase+2C+16&column=ki&startPg=0&Increment=50&submit=Search A1O 4LA7,8AYA,4LG5 16927350 383540105 2 MEEMTPAVAMTLSLAANTMCESSPVEITQLKNVTDAADLLSDSENQSFCNGGTECTMEDVSELEEVGEQDLLKTLSDTRSGSSNVFDEDDVLSVVEDNSAVISEGLLVVDAGSELSLSNTAMEIDNGRVLATAIIVGESSIEQVPTAEVLIAGVNQDTNTSEVVIRLPDENSNHLVKGRSVYELDCIPLWGTVSIQGNRSEMEDAFAVSPHFLKLPIKMLMGDHEGMSPSLTHLTGHFFGVYDGHGGHKVADYCRDRLHFALAEEIERIKDELCKRNTGEGRQVQWDKVFTSCFLTVDGEIEGKIGRAVVGSSDKVLEAVASETVGSTAVVALVCSSHIVVSNCGDSRAVLFRGKEAMPLSVDHKPDREDEYARIENAGGKVIQWQGARVFGVLAMSRSIGDRYLKPYVIPEPEVTFMPRSREDECLILASDGLWDVMNNQEVCEIARRRILMWHKKNGAPPLAERGKGIDPACQAAADYLSMLALQKGSKDNISIIVIDLKAQRKFKTRT 4DS8,5VT7,5VSR,5VSQ,5VS5,5VRO,5VR7,4LGB,4LGA,4LG5,3NMT,5JO2,5JO1,5OR6,5OR2,3ZVU,3QN1,8AY8,7AVW,4WVO,4LA7,6ZUC,3KB3 Protein phosphatase 2C 16 P2C16_ARATH Q9CAJ0 C0Z251 O81709 Q0WLM7 MANSESSSSPVNEEENSQRISTLHHQTMPSDLTQDEFTQLSQSIAEFHTYQLGNGRCSSLLAQRIHAPPETVWSVVRRFDRPQIYKHFIKSCNVSEDFEMRVGCTRDVNVISGLPANTSRERLDLLDDDRRVTGFSITGGEHRLRNYKSVTTVHRFEKEEEEERIWTVVLESYVVDVPEGNSEEDTRLFADTVIRLNLQKLASITEAMNRNNNNNNSSQVR 3JRS,3NEG,3NEF,3KDJ,3JRQ,3NMN,3KAY,9J6I Abscisic acid receptor PYL1 PYL1_ARATH Q8VZS8 Q9FIP6 605122 CCCN1c2ccc(cc2CCC1=O)NS(=O)(=O)Cc3ccc(cc3)C InChI=1S/C20H24N2O3S/c1-3-12-22-19-10-9-18(13-17(19)8-11-20(22)23)21-26(24,25)14-16-6-4-15(2)5-7-16/h4-7,9-10,13,21H,3,8,11-12,14H2,1-2H3 IVHKSUMLZQXFPR-UHFFFAOYSA-N 313186 US10167261, Compound Quinabactin Abscisic acid receptor PYL2/Protein phosphatase 2C 16 Mouse-ear cress 262 US Patent 10.7270/Q2HQ420V aid1796429 US10167261 Loiseleur, O; Wendeborn, SV; Cutler, SR 1/1/2019 4/24/2019 University of California http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=313186 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=176&target=Abscisic+acid+receptor+PYL2%2FProtein+phosphatase+2C+16&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=313186&enzyme=Abscisic+acid+receptor+PYL2%2FProtein+phosphatase+2C+16&column=ki&startPg=0&Increment=50&submit=Search A1O 4LA7,8AYA,4LG5 16927350 383540105 2 MEEMTPAVAMTLSLAANTMCESSPVEITQLKNVTDAADLLSDSENQSFCNGGTECTMEDVSELEEVGEQDLLKTLSDTRSGSSNVFDEDDVLSVVEDNSAVISEGLLVVDAGSELSLSNTAMEIDNGRVLATAIIVGESSIEQVPTAEVLIAGVNQDTNTSEVVIRLPDENSNHLVKGRSVYELDCIPLWGTVSIQGNRSEMEDAFAVSPHFLKLPIKMLMGDHEGMSPSLTHLTGHFFGVYDGHGGHKVADYCRDRLHFALAEEIERIKDELCKRNTGEGRQVQWDKVFTSCFLTVDGEIEGKIGRAVVGSSDKVLEAVASETVGSTAVVALVCSSHIVVSNCGDSRAVLFRGKEAMPLSVDHKPDREDEYARIENAGGKVIQWQGARVFGVLAMSRSIGDRYLKPYVIPEPEVTFMPRSREDECLILASDGLWDVMNNQEVCEIARRRILMWHKKNGAPPLAERGKGIDPACQAAADYLSMLALQKGSKDNISIIVIDLKAQRKFKTRT 4DS8,5VT7,5VSR,5VSQ,5VS5,5VRO,5VR7,4LGB,4LGA,4LG5,3NMT,5JO2,5JO1,5OR6,5OR2,3ZVU,3QN1,8AY8,7AVW,4WVO,4LA7,6ZUC,3KB3 Protein phosphatase 2C 16 P2C16_ARATH Q9CAJ0 C0Z251 O81709 Q0WLM7 MSSSPAVKGLTDEEQKTLEPVIKTYHQFEPDPTTCTSLITQRIHAPASVVWPLIRRFDNPERYKHFVKRCRLISGDGDVGSVREVTVISGLPASTSTERLEFVDDDHRVLSFRVVGGEHRLKNYKSVTSVNEFLNQDSGKVYTVVLESYTVDIPEGNTEEDTKMFVDTVVKLNLQKLGVAATSAPMHDDE 5JNN,3NS2,3NR4,3KL1,3KDI,3KDH,4LA7,3NJ0,3NMH,3KB3,3KB0,3KAZ,5VT7,5VSR,5VSQ,5VS5,5VRO,5VR7,4LGB,4LGA,4LG5,3UJL Abscisic acid receptor PYL2 PYL2_ARATH O80992 51040378 CCOC(=O)c1ccccc1S(=O)(=O)NC(=O)Nc2nc(cc(n2)Cl)OC InChI=1S/C15H15ClN4O6S/c1-3-26-13(21)9-6-4-5-7-10(9)27(23,24)20-15(22)19-14-17-11(16)8-12(18-14)25-2/h4-8H,3H2,1-2H3,(H2,17,18,19,20,22) NSWAMPCUPHPTTC-UHFFFAOYSA-N 50424585 Chlorimuron Ethyl::CHEMBL1231791 Acetolactate synthase catalytic subunit, mitochondrial Saccharomyces cerevisiae (strain ATCC 204508 / S288c) 3.3 ChEMBL 10.1021/jm301501k 10.7270/Q22Z16TH 23237384 Lee, YT; Cui, CJ; Chow, EW; Pue, N; Lonhienne, T; Wang, JG; Fraser, JA; Guddat, LW 1/10/2013 9/24/2013 The University of Queensland http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50424585 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50004480&target=Acetolactate+synthase+catalytic+subunit%2C+mitochondrial&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50424585&enzyme=Acetolactate+synthase+catalytic+subunit%2C+mitochondrial&column=ki&startPg=0&Increment=50&submit=Search CIE 1N0H,1YBH,6DEL,7STQ,7U1D,7YD2,8IVE,8IW3 56160 164153460 CHEMBL1231791 C10943 1 MIRQSTLKNFAIKRCFQHIAYRNTPAMRSVALAQRFYSSSSRYYSASPLPASKRPEPAPSFNVDPLEQPAEPSKLAKKLRAEPDMDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPSNALNQLTSRAQDEFVMQSINKAADLINLAKKPVLYVGAGILNHADGPRLLKELSDRAQIPVTTTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPEARRAAAEGRGGIIHFEVSPKNINKVVQTQIAVEGDATTNLGKMMSKIFPVKERSEWFAQINKWKKEYPYAYMEETPGSKIKPQTVIKKLSKVANDTGRHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNEEQGMVTQWQSLFYEHRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLEVEVDKKVPVLPMVAGGSGLDEFINFDPEVERQQTELRHKRTGGKH 1JSC,6BD9,6BD3,5WKC,5IMS,5FEM,1T9D,1T9C,1T9B,1T9A,1N0H,6U9D Acetolactate synthase catalytic subunit, mitochondrial ILVB_YEAST P07342 D6VZT1 51040376 COc1cc(nc(n1)NC(=O)NS(=O)(=O)Cc2ccccc2C(=O)OC)OC InChI=1S/C16H18N4O7S/c1-25-12-8-13(26-2)18-15(17-12)19-16(22)20-28(23,24)9-10-6-4-5-7-11(10)14(21)27-3/h4-8H,9H2,1-3H3,(H2,17,18,19,20,22) XMQFTWRPUQYINF-UHFFFAOYSA-N 50424591 Bensulfuron Methyl::CHEMBL2313154 Acetolactate synthase catalytic subunit, mitochondrial Saccharomyces cerevisiae (strain ATCC 204508 / S288c) 4.4 ChEMBL 10.1021/jm301501k 10.7270/Q22Z16TH 23237384 Lee, YT; Cui, CJ; Chow, EW; Pue, N; Lonhienne, T; Wang, JG; Fraser, JA; Guddat, LW 1/10/2013 9/24/2013 The University of Queensland http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50424591 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50004480&target=Acetolactate+synthase+catalytic+subunit%2C+mitochondrial&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50424591&enzyme=Acetolactate+synthase+catalytic+subunit%2C+mitochondrial&column=ki&startPg=0&Increment=50&submit=Search 60G 5FEM,6DEM,6U9D,8J7G 54960 164153466 CHEMBL2313154 C10937 1 MIRQSTLKNFAIKRCFQHIAYRNTPAMRSVALAQRFYSSSSRYYSASPLPASKRPEPAPSFNVDPLEQPAEPSKLAKKLRAEPDMDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPSNALNQLTSRAQDEFVMQSINKAADLINLAKKPVLYVGAGILNHADGPRLLKELSDRAQIPVTTTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPEARRAAAEGRGGIIHFEVSPKNINKVVQTQIAVEGDATTNLGKMMSKIFPVKERSEWFAQINKWKKEYPYAYMEETPGSKIKPQTVIKKLSKVANDTGRHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNEEQGMVTQWQSLFYEHRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLEVEVDKKVPVLPMVAGGSGLDEFINFDPEVERQQTELRHKRTGGKH 1JSC,6BD9,6BD3,5WKC,5IMS,5FEM,1T9D,1T9C,1T9B,1T9A,1N0H,6U9D Acetolactate synthase catalytic subunit, mitochondrial ILVB_YEAST P07342 D6VZT1 51040376 COc1cc(nc(n1)NC(=O)NS(=O)(=O)Cc2ccccc2C(=O)OC)OC InChI=1S/C16H18N4O7S/c1-25-12-8-13(26-2)18-15(17-12)19-16(22)20-28(23,24)9-10-6-4-5-7-11(10)14(21)27-3/h4-8H,9H2,1-3H3,(H2,17,18,19,20,22) XMQFTWRPUQYINF-UHFFFAOYSA-N 50424591 Bensulfuron Methyl::CHEMBL2313154 Acetolactate synthase catalytic subunit, mitochondrial Saccharomyces cerevisiae (strain ATCC 204508 / S288c) 4.4 ChEMBL 10.1021/jm301501k 10.7270/Q22Z16TH 23237384 Lee, YT; Cui, CJ; Chow, EW; Pue, N; Lonhienne, T; Wang, JG; Fraser, JA; Guddat, LW 1/10/2013 9/24/2013 The University of Queensland http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50424591 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50004480&target=Acetolactate+synthase+catalytic+subunit%2C+mitochondrial&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50424591&enzyme=Acetolactate+synthase+catalytic+subunit%2C+mitochondrial&column=ki&startPg=0&Increment=50&submit=Search 60G 5FEM,6DEM,6U9D,8J7G 54960 164153466 CHEMBL2313154 C10937 1 MIRQSTLKNFAIKRCFQHIAYRNTPAMRSVALAQRFYSSSSRYYSASPLPASKRPEPAPSFNVDPLEQPAEPSKLAKKLRAEPDMDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPSNALNQLTSRAQDEFVMQSINKAADLINLAKKPVLYVGAGILNHADGPRLLKELSDRAQIPVTTTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPEARRAAAEGRGGIIHFEVSPKNINKVVQTQIAVEGDATTNLGKMMSKIFPVKERSEWFAQINKWKKEYPYAYMEETPGSKIKPQTVIKKLSKVANDTGRHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNEEQGMVTQWQSLFYEHRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLEVEVDKKVPVLPMVAGGSGLDEFINFDPEVERQQTELRHKRTGGKH 1JSC,6BD9,6BD3,5WKC,5IMS,5FEM,1T9D,1T9C,1T9B,1T9A,1N0H,6U9D Acetolactate synthase catalytic subunit, mitochondrial ILVB_YEAST P07342 D6VZT1 51040373 Cc1cc(nc(n1)NC(=O)NS(=O)(=O)c2ccccc2C(=O)OC)C InChI=1S/C15H16N4O5S/c1-9-8-10(2)17-14(16-9)18-15(21)19-25(22,23)12-7-5-4-6-11(12)13(20)24-3/h4-8H,1-3H3,(H2,16,17,18,19,21) ZDXMLEQEMNLCQG-UHFFFAOYSA-N 50424588 SULFOMETURON METHYL Acetolactate synthase catalytic subunit, mitochondrial Saccharomyces cerevisiae (strain ATCC 204508 / S288c) 51 ChEMBL 10.1021/jm301501k 10.7270/Q22Z16TH 23237384 Lee, YT; Cui, CJ; Chow, EW; Pue, N; Lonhienne, T; Wang, JG; Fraser, JA; Guddat, LW 1/10/2013 9/24/2013 The University of Queensland http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50424588 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50004480&target=Acetolactate+synthase+catalytic+subunit%2C+mitochondrial&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50424588&enzyme=Acetolactate+synthase+catalytic+subunit%2C+mitochondrial&column=ki&startPg=0&Increment=50&submit=Search 1SM 1T9C,1YI0,6DEP,8IW6,8J7I 52997 164153463 C10955 1 MIRQSTLKNFAIKRCFQHIAYRNTPAMRSVALAQRFYSSSSRYYSASPLPASKRPEPAPSFNVDPLEQPAEPSKLAKKLRAEPDMDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPSNALNQLTSRAQDEFVMQSINKAADLINLAKKPVLYVGAGILNHADGPRLLKELSDRAQIPVTTTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPEARRAAAEGRGGIIHFEVSPKNINKVVQTQIAVEGDATTNLGKMMSKIFPVKERSEWFAQINKWKKEYPYAYMEETPGSKIKPQTVIKKLSKVANDTGRHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNEEQGMVTQWQSLFYEHRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLEVEVDKKVPVLPMVAGGSGLDEFINFDPEVERQQTELRHKRTGGKH 1JSC,6BD9,6BD3,5WKC,5IMS,5FEM,1T9D,1T9C,1T9B,1T9A,1N0H,6U9D Acetolactate synthase catalytic subunit, mitochondrial ILVB_YEAST P07342 D6VZT1 51040371 Cc1nc(nc(n1)OC)N(C)C(=O)NS(=O)(=O)c2ccccc2C(=O)OC InChI=1S/C15H17N5O6S/c1-9-16-13(18-14(17-9)26-4)20(2)15(22)19-27(23,24)11-8-6-5-7-10(11)12(21)25-3/h5-8H,1-4H3,(H,19,22) VLCQZHSMCYCDJL-UHFFFAOYSA-N 50424586 Tribenuron Methyl::CHEMBL1229780 Acetolactate synthase catalytic subunit, mitochondrial Saccharomyces cerevisiae (strain ATCC 204508 / S288c) 400 ChEMBL 10.1021/jm301501k 10.7270/Q22Z16TH 23237384 Lee, YT; Cui, CJ; Chow, EW; Pue, N; Lonhienne, T; Wang, JG; Fraser, JA; Guddat, LW 1/10/2013 9/24/2013 The University of Queensland http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50424586 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50004480&target=Acetolactate+synthase+catalytic+subunit%2C+mitochondrial&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50424586&enzyme=Acetolactate+synthase+catalytic+subunit%2C+mitochondrial&column=ki&startPg=0&Increment=50&submit=Search 1TB 1T9A,1YI1,8IVT 153909 164153461 CHEMBL1229780 C10962 1 MIRQSTLKNFAIKRCFQHIAYRNTPAMRSVALAQRFYSSSSRYYSASPLPASKRPEPAPSFNVDPLEQPAEPSKLAKKLRAEPDMDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPSNALNQLTSRAQDEFVMQSINKAADLINLAKKPVLYVGAGILNHADGPRLLKELSDRAQIPVTTTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPEARRAAAEGRGGIIHFEVSPKNINKVVQTQIAVEGDATTNLGKMMSKIFPVKERSEWFAQINKWKKEYPYAYMEETPGSKIKPQTVIKKLSKVANDTGRHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNEEQGMVTQWQSLFYEHRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLEVEVDKKVPVLPMVAGGSGLDEFINFDPEVERQQTELRHKRTGGKH 1JSC,6BD9,6BD3,5WKC,5IMS,5FEM,1T9D,1T9C,1T9B,1T9A,1N0H,6U9D Acetolactate synthase catalytic subunit, mitochondrial ILVB_YEAST P07342 D6VZT1 51040374 Cc1nc(nc(n1)OC)NC(=O)NS(=O)(=O)c2ccccc2Cl InChI=1S/C12H12ClN5O4S/c1-7-14-10(17-12(15-7)22-2)16-11(19)18-23(20,21)9-6-4-3-5-8(9)13/h3-6H,1-2H3,(H2,14,15,16,17,18,19) VJYIFXVZLXQVHO-UHFFFAOYSA-N 50424589 DNDI1246776::CHEMBL1229721 Acetolactate synthase catalytic subunit, mitochondrial Saccharomyces cerevisiae (strain ATCC 204508 / S288c) 127 ChEMBL 10.1021/jm301501k 10.7270/Q22Z16TH 23237384 Lee, YT; Cui, CJ; Chow, EW; Pue, N; Lonhienne, T; Wang, JG; Fraser, JA; Guddat, LW 1/10/2013 9/24/2013 The University of Queensland http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50424589 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50004480&target=Acetolactate+synthase+catalytic+subunit%2C+mitochondrial&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50424589&enzyme=Acetolactate+synthase+catalytic+subunit%2C+mitochondrial&column=ki&startPg=0&Increment=50&submit=Search 1CS 1T9B,1YHZ,9DT5 47491 164153464 CHEMBL1229721 C05071 1 MIRQSTLKNFAIKRCFQHIAYRNTPAMRSVALAQRFYSSSSRYYSASPLPASKRPEPAPSFNVDPLEQPAEPSKLAKKLRAEPDMDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPSNALNQLTSRAQDEFVMQSINKAADLINLAKKPVLYVGAGILNHADGPRLLKELSDRAQIPVTTTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPEARRAAAEGRGGIIHFEVSPKNINKVVQTQIAVEGDATTNLGKMMSKIFPVKERSEWFAQINKWKKEYPYAYMEETPGSKIKPQTVIKKLSKVANDTGRHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNEEQGMVTQWQSLFYEHRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLEVEVDKKVPVLPMVAGGSGLDEFINFDPEVERQQTELRHKRTGGKH 1JSC,6BD9,6BD3,5WKC,5IMS,5FEM,1T9D,1T9C,1T9B,1T9A,1N0H,6U9D Acetolactate synthase catalytic subunit, mitochondrial ILVB_YEAST P07342 D6VZT1 51041376 C[C@H](CCOc1nccn1C)N(C)C InChI=1S/C10H19N3O/c1-9(12(2)3)5-8-14-10-11-6-7-13(10)4/h6-7,9H,5,8H2,1-4H3 VPQCJEWNIYWNLE-UHFFFAOYSA-N 50425041 CHEMBL2312565 Acetylcholine-binding protein Lymnaea stagnalis 45 ChEMBL 10.1021/jm301409f 10.7270/Q2RJ4KST 23256554 Ussing, CA; Hansen, CP; Petersen, JG; Jensen, AA; Rohde, LA; Ahring, PK; Nielsen, EØ; Kastrup, JS; Gajhede, M; Frolund, B; Balle, T 2/15/2013 9/24/2013 University of Copenhagen http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50425041 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5104&target=Acetylcholine-binding+protein&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50425041&enzyme=Acetylcholine-binding+protein&column=ki&startPg=0&Increment=50&submit=Search XRS 3ZDH 70701321 164153916 CHEMBL2312565 1 MRRNIFCLACLWIVQACLSLDRADILYNIRQTSRPDVIPTQRDRPVAVSVSLKFINILEVNEITNEVDVVFWQQTTWSDRTLAWNSSHSPDQVSVPISSLWVPDLAAYNAISKPEVLTPQLARVVSDGEVLYMPSIRQRFSCDVSGVDTESGATCRIKIGSWTHHSREISVDPTTENSDDSEYFSQYSRFEILDVTQKKNSVTYSCCPEAYEDVEVSLNFRKKGRSEIL 8P1F,8P1E,8P11,7NDV,7NDP,4ALX,3WIP,7N43,5T90,4NZB,3ZDH,3ZDG,3U8N,3U8M,3U8L,3U8K,3U8J,1YI5,1UV6,5J5I,5J5H,5J5G,5J5F,5BP0,4ZRU,4ZR6,4ZK1,4ZJT,4QAC,4QAB,4QAA,9SG3 Acetylcholine-binding protein ACHP_LYMST P58154 51041377 C[C@H](CCOC(=O)N(C)C)N(C)C InChI=1S/C9H20N2O2/c1-8(10(2)3)6-7-13-9(12)11(4)5/h8H,6-7H2,1-5H3 VVGQXMCHKFOTKZ-UHFFFAOYSA-N 50425042 (R)-3-(Dimethylamino)Butyl Dimethylcarbamate::CHEMBL2312568 Acetylcholine-binding protein Lymnaea stagnalis 79 ChEMBL 10.1021/jm301409f 10.7270/Q2RJ4KST 23256554 Ussing, CA; Hansen, CP; Petersen, JG; Jensen, AA; Rohde, LA; Ahring, PK; Nielsen, EØ; Kastrup, JS; Gajhede, M; Frolund, B; Balle, T 2/15/2013 9/24/2013 University of Copenhagen http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50425042 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5104&target=Acetylcholine-binding+protein&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50425042&enzyme=Acetylcholine-binding+protein&column=ki&startPg=0&Increment=50&submit=Search XRX 3ZDG 9836977 164153917 CHEMBL2312568 1 MRRNIFCLACLWIVQACLSLDRADILYNIRQTSRPDVIPTQRDRPVAVSVSLKFINILEVNEITNEVDVVFWQQTTWSDRTLAWNSSHSPDQVSVPISSLWVPDLAAYNAISKPEVLTPQLARVVSDGEVLYMPSIRQRFSCDVSGVDTESGATCRIKIGSWTHHSREISVDPTTENSDDSEYFSQYSRFEILDVTQKKNSVTYSCCPEAYEDVEVSLNFRKKGRSEIL 8P1F,8P1E,8P11,7NDV,7NDP,4ALX,3WIP,7N43,5T90,4NZB,3ZDH,3ZDG,3U8N,3U8M,3U8L,3U8K,3U8J,1YI5,1UV6,5J5I,5J5H,5J5G,5J5F,5BP0,4ZRU,4ZR6,4ZK1,4ZJT,4QAC,4QAB,4QAA,9SG3 Acetylcholine-binding protein ACHP_LYMST P58154 50049787 CC(=O)OCC[N+](C)(C)C InChI=1S/C7H16NO2/c1-7(9)10-6-5-8(2,3)4/h5-6H2,1-4H3/q+1 OIPILFWXSMYKGL-UHFFFAOYSA-N 10759 2-acetoxyethyl(trimethyl)ammonium;perchlorate::2-acetoxyethyl(trimethyl)ammonium;bromide::acetylcholine chloride::cid_6060::CHEMBL667::[2-(acetyloxy)ethyl]trimethylazanium::acetylcholine::US10667515, Compound ACh Acetylcholine receptor subunit delta Tetronarce californica 40000 ChEMBL 10.1021/jm970377o 10.7270/Q2QF8TH9 9435889 Holladay, MW; Dart, MJ; Lynch, JK 2/13/1998 11/5/2012 Abbott Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10759 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50002857&target=Acetylcholine+receptor+subunit+delta&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10759&enzyme=Acetylcholine+receptor+subunit+delta&column=ki&startPg=0&Increment=50&submit=Search ACH 2ACE,2HA4,2J0H,2RIN,2XZ5,3Q5S,3RQW,3WIP,6V1R,7PRR,7T8X,7T90,7T94,7T96,7TRS,8SSZ,8ST0,8ST1,8ST2,8ST3,8ST4,8XTW,8ZMS,9AVU,9AWJ,9DMH,9DMQ,9E3E,9E3G,9EJZ,9GU2,9GU3 187 172097188 CHEMBL667 DB03128 C01996 1 MGNIHFVYLLISCLYYSGCSGVNEEERLINDLLIVNKYNKHVRPVKHNNEVVNIALSLTLSNLISLKETDETLTSNVWMDHAWYDHRLTWNASEYSDISILRLPPELVWIPDIVLQNNNDGQYHVAYFCNVLVRPNGYVTWLPPAIFRSSCPINVLYFPFDWQNCSLKFTALNYDANEITMDLMTDTIDGKDYPIEWIIIDPEAFTENGEWEIIHKPAKKNIYPDKFPNGTNYQDVTFYLIIRRKPLFYVINFITPCVLISFLASLAFYLPAESGEKMSTAISVLLAQAVFLLLTSQRLPETALAVPLIGKYLMFIMSLVTGVIVNCGIVLNFHFRTPSTHVLSTRVKQIFLEKLPRILHMSRADESEQPDWQNDLKLRRSSSVGYISKAQEYFNIKSRSELMFEKQSERHGLVPRVTPRIGFGNNNENIAASDQLHDEIKSGIDSTNYIVKQIKEKNAYDEEVGNWNLVGQTIDRLSMFIITPVMVLGTIFIFVMGNFNHPPAKPFEGDPFDYSSDHPRCA 9E3G,9E3F,9E3E,8YQN,8QQM,8ESK,7Z14,7SMT,7SMS,7SMR,7SMQ,7SMM,7QL6,7QL5,7QKO,6UWZ,8F6Z,8F6Y,8F2S,9NX2,1OED Acetylcholine receptor subunit delta ACHD_TETCF P02718 50049787 CC(=O)OCC[N+](C)(C)C InChI=1S/C7H16NO2/c1-7(9)10-6-5-8(2,3)4/h5-6H2,1-4H3/q+1 OIPILFWXSMYKGL-UHFFFAOYSA-N 10759 2-acetoxyethyl(trimethyl)ammonium;perchlorate::2-acetoxyethyl(trimethyl)ammonium;bromide::acetylcholine chloride::cid_6060::CHEMBL667::[2-(acetyloxy)ethyl]trimethylazanium::acetylcholine::US10667515, Compound ACh Acetylcholine receptor subunit delta Tetronarce californica 40000 ChEMBL 10.1021/jm970377o 10.7270/Q2QF8TH9 9435889 Holladay, MW; Dart, MJ; Lynch, JK 2/13/1998 11/5/2012 Abbott Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10759 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50002857&target=Acetylcholine+receptor+subunit+delta&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10759&enzyme=Acetylcholine+receptor+subunit+delta&column=ki&startPg=0&Increment=50&submit=Search ACH 2ACE,2HA4,2J0H,2RIN,2XZ5,3Q5S,3RQW,3WIP,6V1R,7PRR,7T8X,7T90,7T94,7T96,7TRS,8SSZ,8ST0,8ST1,8ST2,8ST3,8ST4,8XTW,8ZMS,9AVU,9AWJ,9DMH,9DMQ,9E3E,9E3G,9EJZ,9GU2,9GU3 187 172097188 CHEMBL667 DB03128 C01996 1 MGNIHFVYLLISCLYYSGCSGVNEEERLINDLLIVNKYNKHVRPVKHNNEVVNIALSLTLSNLISLKETDETLTSNVWMDHAWYDHRLTWNASEYSDISILRLPPELVWIPDIVLQNNNDGQYHVAYFCNVLVRPNGYVTWLPPAIFRSSCPINVLYFPFDWQNCSLKFTALNYDANEITMDLMTDTIDGKDYPIEWIIIDPEAFTENGEWEIIHKPAKKNIYPDKFPNGTNYQDVTFYLIIRRKPLFYVINFITPCVLISFLASLAFYLPAESGEKMSTAISVLLAQAVFLLLTSQRLPETALAVPLIGKYLMFIMSLVTGVIVNCGIVLNFHFRTPSTHVLSTRVKQIFLEKLPRILHMSRADESEQPDWQNDLKLRRSSSVGYISKAQEYFNIKSRSELMFEKQSERHGLVPRVTPRIGFGNNNENIAASDQLHDEIKSGIDSTNYIVKQIKEKNAYDEEVGNWNLVGQTIDRLSMFIITPVMVLGTIFIFVMGNFNHPPAKPFEGDPFDYSSDHPRCA 9E3G,9E3F,9E3E,8YQN,8QQM,8ESK,7Z14,7SMT,7SMS,7SMR,7SMQ,7SMM,7QL6,7QL5,7QKO,6UWZ,8F6Z,8F6Y,8F2S,9NX2,1OED Acetylcholine receptor subunit delta ACHD_TETCF P02718 50207963 CCOC(=O)c1cncn1[C@H](C)c2ccccc2 InChI=1S/C14H16N2O2/c1-3-18-14(17)13-9-15-10-16(13)11(2)12-7-5-4-6-8-12/h4-11H,3H2,1-2H3 NPUKDXXFDDZOKR-UHFFFAOYSA-N 50125935 CHEMBL681::R(+)-etomidate::Amidate::(R)-1-(1-phenylethyl)-1H-imidazole-5-carboxylic acid ethyl ester::Etomidate::(R)-1-(1-phenylethyl)-1H-imidazole-5-carboxylicacid ethyl ester::3-((R)-1-Phenyl-ethyl)-3H-imidazole-4-carboxylic acid ethyl ester::R-ETOMIDATE Acetylcholine receptor subunit alpha/beta/delta/gamma Tetronarce californica 41000 ChEMBL 10.1021/jm020465v 10.7270/Q24J0FVZ 12646036 Husain, SS; Ziebell, MR; Ruesch, D; Hong, F; Arevalo, E; Kosterlitz, JA; Olsen, RW; Forman, SA; Cohen, JB; Miller, KW 3/20/2003 11/30/2012 Massachusetts General Hospital http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50125935 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000173&target=Acetylcholine+receptor+subunit+alpha%2Fbeta%2Fdelta%2Fgamma&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50125935&enzyme=Acetylcholine+receptor+subunit+alpha%2Fbeta%2Fdelta%2Fgamma&column=ki&startPg=0&Increment=50&submit=Search V8D 6X3V,8F6Y,8PVB,9FG9,9FGG,9HNT 667484 104018111 CHEMBL681 DB00292 C07522 4 MENVRRMALGLVVMMALALSGVGASVMEDTLLSVLFETYNPKVRPAQTVGDKVTVRVGLTLTNLLILNEKIEEMTTNVFLNLAWTDYRLQWDPAAYEGIKDLRIPSSDVWQPDIVLMNNNDGSFEITLHVNVLVQHTGAVSWQPSAIYRSSCTIKVMYFPFDWQNCTMVFKSYTYDTSEVTLQHALDAKGEREVKEIVINKDAFTENGQWSIEHKPSRKNWRSDDPSYEDVTFYLIIQRKPLFYIVYTIIPCILISILAILVFYLPPDAGEKMSLSISALLAVTVFLLLLADKVPETSLSVPIIIRYLMFIMILVAFSVILSVVVLNLHHRSPNTHTMPNWIRQIFIETLPPFLWIQRPVTTPSPDSKPTIISRANDEYFIRKPAGDFVCPVDNARVAVQPERLFSEMKWHLNGLTQPVTLPQDLKEAVEAIKYIAEQLESASEFDDLKKDWQYVAMVADRLFLYVFFVICSIGTFSIFLDASHNVPPDNPFA 4BOT,4BOR,4BOO,4BON,4BOI,4BOG,4AQ9,4AQ5,9NX2,9E3G,9E3F,9E3E,8YQN,8QQM,8F6Z,8F6Y,8F2S,8ESK,7Z14,7SMT,7SMS,7SMR,7SMQ,7SMM,7QL6,7QL5,7QKO,6UWZ,1OED Acetylcholine receptor subunit beta ACHB_TETCF P02712 MVLTLLLIICLALEVRSENEEGRLIEKLLGDYDKRIIPAKTLDHIIDVTLKLTLTNLISLNEKEEALTTNVWIEIQWNDYRLSWNTSEYEGIDLVRIPSELLWLPDVVLENNVDGQFEVAYYANVLVYNDGSMYWLPPAIYRSTCPIAVTYFPFDWQNCSLVFRSQTYNAHEVNLQLSAEEGEAVEWIHIDPEDFTENGEWTIRHRPAKKNYNWQLTKDDTDFQEIIFFLIIQRKPLFYIINIIAPCVLISSLVVLVYFLPAQAGGQKCTLSISVLLAQTIFLFLIAQKVPETSLNVPLIGKYLIFVMFVSMLIVMNCVIVLNVSLRTPNTHSLSEKIKHLFLGFLPKYLGMQLEPSEETPEKPQPRRRSSFGIMIKAEEYILKKPRSELMFEEQKDRHGLKRVNKMTSDIDIGTTVDLYKDLANFAPEIKSCVEACNFIAKSTKEQNDSGSENENWVLIGKVIDKACFWIALLLFSIGTLAIFLTGHFNQVPEFPFPGDPRKYVP 4BOT,4BOR,4BOO,4BON,4BOI,4BOG,9NX2,8YQN,8QQM,8F6Z,8F6Y,8F2S,8ESK,7Z14,7SMT,7SMS,7SMR,7SMQ,7SMM,7QL6,7QL5,7QKO,6UWZ,9E3G,9E3F,9E3E,1OED Acetylcholine receptor subunit gamma ACHG_TETCF P02714 MILCSYWHVGLVLLLFSCCGLVLGSEHETRLVANLLENYNKVIRPVEHHTHFVDITVGLQLIQLISVDEVNQIVETNVRLRQQWIDVRLRWNPADYGGIKKIRLPSDDVWLPDLVLYNNADGDFAIVHMTKLLLDYTGKIMWTPPAIFKSYCEIIVTHFPFDQQNCTMKLGIWTYDGTKVSISPESDRPDLSTFMESGEWVMKDYRGWKHWVYYTCCPDTPYLDITYHFIMQRIPLYFVVNVIIPCLLFSFLTGLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMIFVISSIIITVVVINTHHRSPSTHTMPQWVRKIFIDTIPNVMFFSTMKRASKEKQENKIFADDIDISDISGKQVTGEVIFQTPLIKNPDVKSAIEGVKYIAEHMKSDEESSNAAEEWKYVAMVIDHILLCVFMLICIIGTVSVFAGRLIELSQEG 9E3G,9E3F,9E3E,8YQN,8QQM,8ESK,7Z14,7SMT,7SMS,7SMR,7SMQ,7SMM,7QL6,7QL5,7QKO,6UWZ,8F6Z,8F6Y,8F2S,1OED Acetylcholine receptor subunit alpha ACHA_TETCF P02710 MGNIHFVYLLISCLYYSGCSGVNEEERLINDLLIVNKYNKHVRPVKHNNEVVNIALSLTLSNLISLKETDETLTSNVWMDHAWYDHRLTWNASEYSDISILRLPPELVWIPDIVLQNNNDGQYHVAYFCNVLVRPNGYVTWLPPAIFRSSCPINVLYFPFDWQNCSLKFTALNYDANEITMDLMTDTIDGKDYPIEWIIIDPEAFTENGEWEIIHKPAKKNIYPDKFPNGTNYQDVTFYLIIRRKPLFYVINFITPCVLISFLASLAFYLPAESGEKMSTAISVLLAQAVFLLLTSQRLPETALAVPLIGKYLMFIMSLVTGVIVNCGIVLNFHFRTPSTHVLSTRVKQIFLEKLPRILHMSRADESEQPDWQNDLKLRRSSSVGYISKAQEYFNIKSRSELMFEKQSERHGLVPRVTPRIGFGNNNENIAASDQLHDEIKSGIDSTNYIVKQIKEKNAYDEEVGNWNLVGQTIDRLSMFIITPVMVLGTIFIFVMGNFNHPPAKPFEGDPFDYSSDHPRCA 9E3G,9E3F,9E3E,8YQN,8QQM,8ESK,7Z14,7SMT,7SMS,7SMR,7SMQ,7SMM,7QL6,7QL5,7QKO,6UWZ,8F6Z,8F6Y,8F2S,9NX2,1OED Acetylcholine receptor subunit delta ACHD_TETCF P02718 50491421 C[N@H+]1CCc2cc(c3cc2[C@@H]1Cc4ccc(cc4)Oc5c6c(cc(c5O)OC)CC[N+]([C@@H]6Cc7ccc(c(c7)O3)O)(C)C)OC InChI=1S/C37H40N2O6/c1-38-14-12-24-19-32(42-4)33-21-27(24)28(38)16-22-6-9-26(10-7-22)44-37-35-25(20-34(43-5)36(37)41)13-15-39(2,3)29(35)17-23-8-11-30(40)31(18-23)45-33/h6-11,18-21,28-29H,12-17H2,1-5H3,(H-,40,41)/p+2 JFJZZMVDLULRGK-UHFFFAOYSA-P 50000690 Tubocurarine,d::10,25-dimethoxy-15,15,30-trimethyl-(1S,16R)-7,23-dioxa-15,30-diazoniaheptacyclo[22.6.2.23,6.112,16.118,22.08,36.027,31]hexatriaconta-3,5,8,10,12(36),18,20,22(35),24(32),25,27(31),33-dodecaene-9,21-diol,dichloride(tubocurarine)::Tubocurarine dichloride::CHEMBL501646::Tubocurarine Acetylcholine receptor subunit alpha/beta/delta/gamma Tetronarce californica 3200000 ChEMBL 10.1021/jm00110a007 10.7270/Q2TX3DBZ 1676426 Abramson, SN; Trischman, JA; Tapiolas, DM; Harold, EE; Fenical, W; Taylor, P 8/6/1991 11/10/2009 University of California San Diego http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50000690 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000173&target=Acetylcholine+receptor+subunit+alpha%2Fbeta%2Fdelta%2Fgamma&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50000690&enzyme=Acetylcholine+receptor+subunit+alpha%2Fbeta%2Fdelta%2Fgamma&column=ki&startPg=0&Increment=50&submit=Search TC9 2XYT,7SMS,7SMT 452970 103915238 CHEMBL501646 C07547 4 MENVRRMALGLVVMMALALSGVGASVMEDTLLSVLFETYNPKVRPAQTVGDKVTVRVGLTLTNLLILNEKIEEMTTNVFLNLAWTDYRLQWDPAAYEGIKDLRIPSSDVWQPDIVLMNNNDGSFEITLHVNVLVQHTGAVSWQPSAIYRSSCTIKVMYFPFDWQNCTMVFKSYTYDTSEVTLQHALDAKGEREVKEIVINKDAFTENGQWSIEHKPSRKNWRSDDPSYEDVTFYLIIQRKPLFYIVYTIIPCILISILAILVFYLPPDAGEKMSLSISALLAVTVFLLLLADKVPETSLSVPIIIRYLMFIMILVAFSVILSVVVLNLHHRSPNTHTMPNWIRQIFIETLPPFLWIQRPVTTPSPDSKPTIISRANDEYFIRKPAGDFVCPVDNARVAVQPERLFSEMKWHLNGLTQPVTLPQDLKEAVEAIKYIAEQLESASEFDDLKKDWQYVAMVADRLFLYVFFVICSIGTFSIFLDASHNVPPDNPFA 4BOT,4BOR,4BOO,4BON,4BOI,4BOG,4AQ9,4AQ5,9NX2,9E3G,9E3F,9E3E,8YQN,8QQM,8F6Z,8F6Y,8F2S,8ESK,7Z14,7SMT,7SMS,7SMR,7SMQ,7SMM,7QL6,7QL5,7QKO,6UWZ,1OED Acetylcholine receptor subunit beta ACHB_TETCF P02712 MVLTLLLIICLALEVRSENEEGRLIEKLLGDYDKRIIPAKTLDHIIDVTLKLTLTNLISLNEKEEALTTNVWIEIQWNDYRLSWNTSEYEGIDLVRIPSELLWLPDVVLENNVDGQFEVAYYANVLVYNDGSMYWLPPAIYRSTCPIAVTYFPFDWQNCSLVFRSQTYNAHEVNLQLSAEEGEAVEWIHIDPEDFTENGEWTIRHRPAKKNYNWQLTKDDTDFQEIIFFLIIQRKPLFYIINIIAPCVLISSLVVLVYFLPAQAGGQKCTLSISVLLAQTIFLFLIAQKVPETSLNVPLIGKYLIFVMFVSMLIVMNCVIVLNVSLRTPNTHSLSEKIKHLFLGFLPKYLGMQLEPSEETPEKPQPRRRSSFGIMIKAEEYILKKPRSELMFEEQKDRHGLKRVNKMTSDIDIGTTVDLYKDLANFAPEIKSCVEACNFIAKSTKEQNDSGSENENWVLIGKVIDKACFWIALLLFSIGTLAIFLTGHFNQVPEFPFPGDPRKYVP 4BOT,4BOR,4BOO,4BON,4BOI,4BOG,9NX2,8YQN,8QQM,8F6Z,8F6Y,8F2S,8ESK,7Z14,7SMT,7SMS,7SMR,7SMQ,7SMM,7QL6,7QL5,7QKO,6UWZ,9E3G,9E3F,9E3E,1OED Acetylcholine receptor subunit gamma ACHG_TETCF P02714 MILCSYWHVGLVLLLFSCCGLVLGSEHETRLVANLLENYNKVIRPVEHHTHFVDITVGLQLIQLISVDEVNQIVETNVRLRQQWIDVRLRWNPADYGGIKKIRLPSDDVWLPDLVLYNNADGDFAIVHMTKLLLDYTGKIMWTPPAIFKSYCEIIVTHFPFDQQNCTMKLGIWTYDGTKVSISPESDRPDLSTFMESGEWVMKDYRGWKHWVYYTCCPDTPYLDITYHFIMQRIPLYFVVNVIIPCLLFSFLTGLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMIFVISSIIITVVVINTHHRSPSTHTMPQWVRKIFIDTIPNVMFFSTMKRASKEKQENKIFADDIDISDISGKQVTGEVIFQTPLIKNPDVKSAIEGVKYIAEHMKSDEESSNAAEEWKYVAMVIDHILLCVFMLICIIGTVSVFAGRLIELSQEG 9E3G,9E3F,9E3E,8YQN,8QQM,8ESK,7Z14,7SMT,7SMS,7SMR,7SMQ,7SMM,7QL6,7QL5,7QKO,6UWZ,8F6Z,8F6Y,8F2S,1OED Acetylcholine receptor subunit alpha ACHA_TETCF P02710 MGNIHFVYLLISCLYYSGCSGVNEEERLINDLLIVNKYNKHVRPVKHNNEVVNIALSLTLSNLISLKETDETLTSNVWMDHAWYDHRLTWNASEYSDISILRLPPELVWIPDIVLQNNNDGQYHVAYFCNVLVRPNGYVTWLPPAIFRSSCPINVLYFPFDWQNCSLKFTALNYDANEITMDLMTDTIDGKDYPIEWIIIDPEAFTENGEWEIIHKPAKKNIYPDKFPNGTNYQDVTFYLIIRRKPLFYVINFITPCVLISFLASLAFYLPAESGEKMSTAISVLLAQAVFLLLTSQRLPETALAVPLIGKYLMFIMSLVTGVIVNCGIVLNFHFRTPSTHVLSTRVKQIFLEKLPRILHMSRADESEQPDWQNDLKLRRSSSVGYISKAQEYFNIKSRSELMFEKQSERHGLVPRVTPRIGFGNNNENIAASDQLHDEIKSGIDSTNYIVKQIKEKNAYDEEVGNWNLVGQTIDRLSMFIITPVMVLGTIFIFVMGNFNHPPAKPFEGDPFDYSSDHPRCA 9E3G,9E3F,9E3E,8YQN,8QQM,8ESK,7Z14,7SMT,7SMS,7SMR,7SMQ,7SMM,7QL6,7QL5,7QKO,6UWZ,8F6Z,8F6Y,8F2S,9NX2,1OED Acetylcholine receptor subunit delta ACHD_TETCF P02718 50491421 C[N@H+]1CCc2cc(c3cc2[C@@H]1Cc4ccc(cc4)Oc5c6c(cc(c5O)OC)CC[N+]([C@@H]6Cc7ccc(c(c7)O3)O)(C)C)OC InChI=1S/C37H40N2O6/c1-38-14-12-24-19-32(42-4)33-21-27(24)28(38)16-22-6-9-26(10-7-22)44-37-35-25(20-34(43-5)36(37)41)13-15-39(2,3)29(35)17-23-8-11-30(40)31(18-23)45-33/h6-11,18-21,28-29H,12-17H2,1-5H3,(H-,40,41)/p+2 JFJZZMVDLULRGK-UHFFFAOYSA-P 50000690 Tubocurarine,d::10,25-dimethoxy-15,15,30-trimethyl-(1S,16R)-7,23-dioxa-15,30-diazoniaheptacyclo[22.6.2.23,6.112,16.118,22.08,36.027,31]hexatriaconta-3,5,8,10,12(36),18,20,22(35),24(32),25,27(31),33-dodecaene-9,21-diol,dichloride(tubocurarine)::Tubocurarine dichloride::CHEMBL501646::Tubocurarine Acetylcholine receptor subunit alpha/beta/delta/gamma Tetronarce californica 3200000 ChEMBL 10.1021/jm00110a007 10.7270/Q2TX3DBZ 1676426 Abramson, SN; Trischman, JA; Tapiolas, DM; Harold, EE; Fenical, W; Taylor, P 8/6/1991 11/10/2009 University of California San Diego http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50000690 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000173&target=Acetylcholine+receptor+subunit+alpha%2Fbeta%2Fdelta%2Fgamma&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50000690&enzyme=Acetylcholine+receptor+subunit+alpha%2Fbeta%2Fdelta%2Fgamma&column=ki&startPg=0&Increment=50&submit=Search TC9 2XYT,7SMS,7SMT 452970 103915238 CHEMBL501646 C07547 4 MENVRRMALGLVVMMALALSGVGASVMEDTLLSVLFETYNPKVRPAQTVGDKVTVRVGLTLTNLLILNEKIEEMTTNVFLNLAWTDYRLQWDPAAYEGIKDLRIPSSDVWQPDIVLMNNNDGSFEITLHVNVLVQHTGAVSWQPSAIYRSSCTIKVMYFPFDWQNCTMVFKSYTYDTSEVTLQHALDAKGEREVKEIVINKDAFTENGQWSIEHKPSRKNWRSDDPSYEDVTFYLIIQRKPLFYIVYTIIPCILISILAILVFYLPPDAGEKMSLSISALLAVTVFLLLLADKVPETSLSVPIIIRYLMFIMILVAFSVILSVVVLNLHHRSPNTHTMPNWIRQIFIETLPPFLWIQRPVTTPSPDSKPTIISRANDEYFIRKPAGDFVCPVDNARVAVQPERLFSEMKWHLNGLTQPVTLPQDLKEAVEAIKYIAEQLESASEFDDLKKDWQYVAMVADRLFLYVFFVICSIGTFSIFLDASHNVPPDNPFA 4BOT,4BOR,4BOO,4BON,4BOI,4BOG,4AQ9,4AQ5,9NX2,9E3G,9E3F,9E3E,8YQN,8QQM,8F6Z,8F6Y,8F2S,8ESK,7Z14,7SMT,7SMS,7SMR,7SMQ,7SMM,7QL6,7QL5,7QKO,6UWZ,1OED Acetylcholine receptor subunit beta ACHB_TETCF P02712 MVLTLLLIICLALEVRSENEEGRLIEKLLGDYDKRIIPAKTLDHIIDVTLKLTLTNLISLNEKEEALTTNVWIEIQWNDYRLSWNTSEYEGIDLVRIPSELLWLPDVVLENNVDGQFEVAYYANVLVYNDGSMYWLPPAIYRSTCPIAVTYFPFDWQNCSLVFRSQTYNAHEVNLQLSAEEGEAVEWIHIDPEDFTENGEWTIRHRPAKKNYNWQLTKDDTDFQEIIFFLIIQRKPLFYIINIIAPCVLISSLVVLVYFLPAQAGGQKCTLSISVLLAQTIFLFLIAQKVPETSLNVPLIGKYLIFVMFVSMLIVMNCVIVLNVSLRTPNTHSLSEKIKHLFLGFLPKYLGMQLEPSEETPEKPQPRRRSSFGIMIKAEEYILKKPRSELMFEEQKDRHGLKRVNKMTSDIDIGTTVDLYKDLANFAPEIKSCVEACNFIAKSTKEQNDSGSENENWVLIGKVIDKACFWIALLLFSIGTLAIFLTGHFNQVPEFPFPGDPRKYVP 4BOT,4BOR,4BOO,4BON,4BOI,4BOG,9NX2,8YQN,8QQM,8F6Z,8F6Y,8F2S,8ESK,7Z14,7SMT,7SMS,7SMR,7SMQ,7SMM,7QL6,7QL5,7QKO,6UWZ,9E3G,9E3F,9E3E,1OED Acetylcholine receptor subunit gamma ACHG_TETCF P02714 MILCSYWHVGLVLLLFSCCGLVLGSEHETRLVANLLENYNKVIRPVEHHTHFVDITVGLQLIQLISVDEVNQIVETNVRLRQQWIDVRLRWNPADYGGIKKIRLPSDDVWLPDLVLYNNADGDFAIVHMTKLLLDYTGKIMWTPPAIFKSYCEIIVTHFPFDQQNCTMKLGIWTYDGTKVSISPESDRPDLSTFMESGEWVMKDYRGWKHWVYYTCCPDTPYLDITYHFIMQRIPLYFVVNVIIPCLLFSFLTGLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMIFVISSIIITVVVINTHHRSPSTHTMPQWVRKIFIDTIPNVMFFSTMKRASKEKQENKIFADDIDISDISGKQVTGEVIFQTPLIKNPDVKSAIEGVKYIAEHMKSDEESSNAAEEWKYVAMVIDHILLCVFMLICIIGTVSVFAGRLIELSQEG 9E3G,9E3F,9E3E,8YQN,8QQM,8ESK,7Z14,7SMT,7SMS,7SMR,7SMQ,7SMM,7QL6,7QL5,7QKO,6UWZ,8F6Z,8F6Y,8F2S,1OED Acetylcholine receptor subunit alpha ACHA_TETCF P02710 MGNIHFVYLLISCLYYSGCSGVNEEERLINDLLIVNKYNKHVRPVKHNNEVVNIALSLTLSNLISLKETDETLTSNVWMDHAWYDHRLTWNASEYSDISILRLPPELVWIPDIVLQNNNDGQYHVAYFCNVLVRPNGYVTWLPPAIFRSSCPINVLYFPFDWQNCSLKFTALNYDANEITMDLMTDTIDGKDYPIEWIIIDPEAFTENGEWEIIHKPAKKNIYPDKFPNGTNYQDVTFYLIIRRKPLFYVINFITPCVLISFLASLAFYLPAESGEKMSTAISVLLAQAVFLLLTSQRLPETALAVPLIGKYLMFIMSLVTGVIVNCGIVLNFHFRTPSTHVLSTRVKQIFLEKLPRILHMSRADESEQPDWQNDLKLRRSSSVGYISKAQEYFNIKSRSELMFEKQSERHGLVPRVTPRIGFGNNNENIAASDQLHDEIKSGIDSTNYIVKQIKEKNAYDEEVGNWNLVGQTIDRLSMFIITPVMVLGTIFIFVMGNFNHPPAKPFEGDPFDYSSDHPRCA 9E3G,9E3F,9E3E,8YQN,8QQM,8ESK,7Z14,7SMT,7SMS,7SMR,7SMQ,7SMM,7QL6,7QL5,7QKO,6UWZ,8F6Z,8F6Y,8F2S,9NX2,1OED Acetylcholine receptor subunit delta ACHD_TETCF P02718 200268 c1cc(cnc1)N2CCCNCC2 InChI=1S/C10H15N3/c1-3-10(9-12-4-1)13-7-2-5-11-6-8-13/h1,3-4,9,11H,2,5-8H2 JBOVXXZNZSULJJ-UHFFFAOYSA-N 50088438 CHEMBL71085::1-Pyridin-3-yl-[1,4]diazepane::NS3531, 1::1-(pyridin-3-yl)-1,4-diazepane Acetylcholine-binding protein Lymnaea stagnalis 3.1 Curated from the literature by BindingDB 10.1074/jbc.M111.292243 10.7270/Q2J964Z5 22170047 aid1799761 Rohde, LA; Ahring, PK; Jensen, ML; Nielsen, EØ; Peters, D; Helgstrand, C; Krintel, C; Harpsøe, K; Gajhede, M; Kastrup, JS; Balle, T 2/3/2012 8/27/2012 University of Copenhagen http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50088438 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5104&target=Acetylcholine-binding+protein&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50088438&enzyme=Acetylcholine-binding+protein&column=ki&startPg=0&Increment=50&submit=Search 09O 3U8J 10654891 103987353 CHEMBL71085 1 MRRNIFCLACLWIVQACLSLDRADILYNIRQTSRPDVIPTQRDRPVAVSVSLKFINILEVNEITNEVDVVFWQQTTWSDRTLAWNSSHSPDQVSVPISSLWVPDLAAYNAISKPEVLTPQLARVVSDGEVLYMPSIRQRFSCDVSGVDTESGATCRIKIGSWTHHSREISVDPTTENSDDSEYFSQYSRFEILDVTQKKNSVTYSCCPEAYEDVEVSLNFRKKGRSEIL 8P1F,8P1E,8P11,7NDV,7NDP,4ALX,3WIP,7N43,5T90,4NZB,3ZDH,3ZDG,3U8N,3U8M,3U8L,3U8K,3U8J,1YI5,1UV6,5J5I,5J5H,5J5G,5J5F,5BP0,4ZRU,4ZR6,4ZK1,4ZJT,4QAC,4QAB,4QAA,9QM8 Acetylcholine-binding protein ACHP_LYMST P58154 200271 CCOc1cc(cnc1)N2CCCNCC2 InChI=1S/C12H19N3O/c1-2-16-12-8-11(9-14-10-12)15-6-3-4-13-5-7-15/h8-10,13H,2-7H2,1H3 RQXFSCANOMMTFZ-UHFFFAOYSA-N 92377 NS3573, 2 Acetylcholine-binding protein Lymnaea stagnalis 2.2 Curated from the literature by BindingDB 10.1074/jbc.M111.292243 10.7270/Q2J964Z5 22170047 aid1799761 Rohde, LA; Ahring, PK; Jensen, ML; Nielsen, EØ; Peters, D; Helgstrand, C; Krintel, C; Harpsøe, K; Gajhede, M; Kastrup, JS; Balle, T 2/3/2012 8/27/2012 University of Copenhagen http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=92377 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5104&target=Acetylcholine-binding+protein&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=92377&enzyme=Acetylcholine-binding+protein&column=ki&startPg=0&Increment=50&submit=Search 09P 4UM1,3U8K 22053540 160844874 1 MRRNIFCLACLWIVQACLSLDRADILYNIRQTSRPDVIPTQRDRPVAVSVSLKFINILEVNEITNEVDVVFWQQTTWSDRTLAWNSSHSPDQVSVPISSLWVPDLAAYNAISKPEVLTPQLARVVSDGEVLYMPSIRQRFSCDVSGVDTESGATCRIKIGSWTHHSREISVDPTTENSDDSEYFSQYSRFEILDVTQKKNSVTYSCCPEAYEDVEVSLNFRKKGRSEIL 8P1F,8P1E,8P11,7NDV,7NDP,4ALX,3WIP,7N43,5T90,4NZB,3ZDH,3ZDG,3U8N,3U8M,3U8L,3U8K,3U8J,1YI5,1UV6,5J5I,5J5H,5J5G,5J5F,5BP0,4ZRU,4ZR6,4ZK1,4ZJT,4QAC,4QAB,4QAA,9QM8 Acetylcholine-binding protein ACHP_LYMST P58154 200277 c1cc(ncc1N2CCCNCC2)Br InChI=1S/C10H14BrN3/c11-10-3-2-9(8-13-10)14-6-1-4-12-5-7-14/h2-3,8,12H,1,4-7H2 JRNYLCIPPWHNEJ-UHFFFAOYSA-N 50088454 NS3920, 4::CHEMBL306387::1-(6-bromopyridin-3-yl)-1,4-diazepane::1-(6-Bromo-pyridin-3-yl)-[1,4]diazepane Acetylcholine-binding protein Lymnaea stagnalis 1.3 Curated from the literature by BindingDB 10.1074/jbc.M111.292243 10.7270/Q2J964Z5 22170047 aid1799761 Rohde, LA; Ahring, PK; Jensen, ML; Nielsen, EØ; Peters, D; Helgstrand, C; Krintel, C; Harpsøe, K; Gajhede, M; Kastrup, JS; Balle, T 2/3/2012 8/27/2012 University of Copenhagen http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50088454 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5104&target=Acetylcholine-binding+protein&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50088454&enzyme=Acetylcholine-binding+protein&column=ki&startPg=0&Increment=50&submit=Search 09R 4UM3,3U8M 10131290 103987369 CHEMBL306387 1 MRRNIFCLACLWIVQACLSLDRADILYNIRQTSRPDVIPTQRDRPVAVSVSLKFINILEVNEITNEVDVVFWQQTTWSDRTLAWNSSHSPDQVSVPISSLWVPDLAAYNAISKPEVLTPQLARVVSDGEVLYMPSIRQRFSCDVSGVDTESGATCRIKIGSWTHHSREISVDPTTENSDDSEYFSQYSRFEILDVTQKKNSVTYSCCPEAYEDVEVSLNFRKKGRSEIL 8P1F,8P1E,8P11,7NDV,7NDP,4ALX,3WIP,7N43,5T90,4NZB,3ZDH,3ZDG,3U8N,3U8M,3U8L,3U8K,3U8J,1YI5,1UV6,5J5I,5J5H,5J5G,5J5F,5BP0,4ZRU,4ZR6,4ZK1,4ZJT,4QAC,4QAB,4QAA,9QM8 Acetylcholine-binding protein ACHP_LYMST P58154 200280 CCOc1cc(cnc1Br)N2CCCNCC2 InChI=1S/C12H18BrN3O/c1-2-17-11-8-10(9-15-12(11)13)16-6-3-4-14-5-7-16/h8-9,14H,2-7H2,1H3 UGNNTIXQGYYUAP-UHFFFAOYSA-N 50088453 CHEMBL72433::NS3570, 5::1-(6-bromo-5-ethoxypyridin-3-yl)-1,4-diazepane::1-(6-Bromo-5-ethoxy-pyridin-3-yl)-[1,4]diazepane Acetylcholine-binding protein Lymnaea stagnalis 0.067 Curated from the literature by BindingDB 10.1074/jbc.M111.292243 10.7270/Q2J964Z5 22170047 aid1799761 Rohde, LA; Ahring, PK; Jensen, ML; Nielsen, EØ; Peters, D; Helgstrand, C; Krintel, C; Harpsøe, K; Gajhede, M; Kastrup, JS; Balle, T 2/3/2012 8/27/2012 University of Copenhagen http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50088453 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5104&target=Acetylcholine-binding+protein&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50088453&enzyme=Acetylcholine-binding+protein&column=ki&startPg=0&Increment=50&submit=Search 09S 3U8N 10402507 103987368 CHEMBL72433 1 MRRNIFCLACLWIVQACLSLDRADILYNIRQTSRPDVIPTQRDRPVAVSVSLKFINILEVNEITNEVDVVFWQQTTWSDRTLAWNSSHSPDQVSVPISSLWVPDLAAYNAISKPEVLTPQLARVVSDGEVLYMPSIRQRFSCDVSGVDTESGATCRIKIGSWTHHSREISVDPTTENSDDSEYFSQYSRFEILDVTQKKNSVTYSCCPEAYEDVEVSLNFRKKGRSEIL 8P1F,8P1E,8P11,7NDV,7NDP,4ALX,3WIP,7N43,5T90,4NZB,3ZDH,3ZDG,3U8N,3U8M,3U8L,3U8K,3U8J,1YI5,1UV6,5J5I,5J5H,5J5G,5J5F,5BP0,4ZRU,4ZR6,4ZK1,4ZJT,4QAC,4QAB,4QAA,9QM8 Acetylcholine-binding protein ACHP_LYMST P58154 201531 CC(=O)OCC[N+](C)(C)C InChI=1S/C7H16NO2/c1-7(9)10-6-5-8(2,3)4/h5-6H2,1-4H3/q+1 OIPILFWXSMYKGL-UHFFFAOYSA-N 10759 2-acetoxyethyl(trimethyl)ammonium;perchlorate::2-acetoxyethyl(trimethyl)ammonium;bromide::acetylcholine chloride::cid_6060::CHEMBL667::[2-(acetyloxy)ethyl]trimethylazanium::acetylcholine::US10667515, Compound ACh Acetylcholine-binding protein Lymnaea stagnalis 458 7.4000 25.00 C Curated from the literature by BindingDB 10.1021/bi1006354 10.7270/Q2TB15HP 20701394 aid1799850 Geitmann, M; Retra, K; de Kloe, GE; Homan, E; Smit, AB; de Esch, IJ; Danielson, UH 9/21/2010 3/4/2013 Beactica http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10759 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5104&target=Acetylcholine-binding+protein&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10759&enzyme=Acetylcholine-binding+protein&column=ki&startPg=0&Increment=50&submit=Search ACH 9AVU,7T8X,8ZMS,3Q5S,2XZ5,7T90,7T96,7T94,3WIP,8ST3,8ST2,8ST1,8ST0,8ST4,7TRS,8SSZ,2RIN,2ACE,7PRR,2HA4,6V1R,2J0H,9AWJ,3RQW 187 172097188 CHEMBL667 DB03128 C01996 1 MRRNIFCLACLWIVQACLSLDRADILYNIRQTSRPDVIPTQRDRPVAVSVSLKFINILEVNEITNEVDVVFWQQTTWSDRTLAWNSSHSPDQVSVPISSLWVPDLAAYNAISKPEVLTPQLARVVSDGEVLYMPSIRQRFSCDVSGVDTESGATCRIKIGSWTHHSREISVDPTTENSDDSEYFSQYSRFEILDVTQKKNSVTYSCCPEAYEDVEVSLNFRKKGRSEIL 8P1F,8P1E,8P11,7NDV,7NDP,4ALX,3WIP,7N43,5T90,4NZB,3ZDH,3ZDG,3U8N,3U8M,3U8L,3U8K,3U8J,1YI5,1UV6,5J5I,5J5H,5J5G,5J5F,5BP0,4ZRU,4ZR6,4ZK1,4ZJT,4QAC,4QAB,4QAA,9QM8 Acetylcholine-binding protein ACHP_LYMST P58154 201534 CC(=O)OCC[N+](C)(C)C InChI=1S/C7H16NO2/c1-7(9)10-6-5-8(2,3)4/h5-6H2,1-4H3/q+1 OIPILFWXSMYKGL-UHFFFAOYSA-N 10759 2-acetoxyethyl(trimethyl)ammonium;perchlorate::2-acetoxyethyl(trimethyl)ammonium;bromide::acetylcholine chloride::cid_6060::CHEMBL667::[2-(acetyloxy)ethyl]trimethylazanium::acetylcholine::US10667515, Compound ACh Acetylcholine-binding protein Lymnaea stagnalis 3850 7.4000 25.00 C Curated from the literature by BindingDB 10.1021/bi1006354 10.7270/Q2TB15HP 20701394 aid1799850 Geitmann, M; Retra, K; de Kloe, GE; Homan, E; Smit, AB; de Esch, IJ; Danielson, UH 9/21/2010 3/4/2013 Beactica http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10759 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5104&target=Acetylcholine-binding+protein&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10759&enzyme=Acetylcholine-binding+protein&column=ki&startPg=0&Increment=50&submit=Search ACH 9AVU,7T8X,8ZMS,3Q5S,2XZ5,7T90,7T96,7T94,3WIP,8ST3,8ST2,8ST1,8ST0,8ST4,7TRS,8SSZ,2RIN,2ACE,7PRR,2HA4,6V1R,2J0H,9AWJ,3RQW 187 172097188 CHEMBL667 DB03128 C01996 1 MRRNIFCLACLWIVQACLSLDRADILYNIRQTSRPDVIPTQRDRPVAVSVSLKFINILEVNEITNEVDVVFWQQTTWSDRTLAWNSSHSPDQVSVPISSLWVPDLAAYNAISKPEVLTPQLARVVSDGEVLYMPSIRQRFSCDVSGVDTESGATCRIKIGSWTHHSREISVDPTTENSDDSEYFSQYSRFEILDVTQKKNSVTYSCCPEAYEDVEVSLNFRKKGRSEIL 8P1F,8P1E,8P11,7NDV,7NDP,4ALX,3WIP,7N43,5T90,4NZB,3ZDH,3ZDG,3U8N,3U8M,3U8L,3U8K,3U8J,1YI5,1UV6,5J5I,5J5H,5J5G,5J5F,5BP0,4ZRU,4ZR6,4ZK1,4ZJT,4QAC,4QAB,4QAA,9QM8 Acetylcholine-binding protein ACHP_LYMST P58154 51009747 CC(=O)OCC[N+](C)(C)C InChI=1S/C7H16NO2/c1-7(9)10-6-5-8(2,3)4/h5-6H2,1-4H3/q+1 OIPILFWXSMYKGL-UHFFFAOYSA-N 10759 2-acetoxyethyl(trimethyl)ammonium;perchlorate::2-acetoxyethyl(trimethyl)ammonium;bromide::acetylcholine chloride::cid_6060::CHEMBL667::[2-(acetyloxy)ethyl]trimethylazanium::acetylcholine::US10667515, Compound ACh Acetylcholine-binding protein Lymnaea stagnalis 3162.28 ChEMBL 10.1021/jm801400g 10.7270/Q2NK3DXK 19331415 Ulens, C; Akdemir, A; Jongejan, A; van Elk, R; Bertrand, S; Perrakis, A; Leurs, R; Smit, AB; Sixma, TK; Bertrand, D; de Esch, IJ 4/16/2009 1/11/2010 Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10759 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5104&target=Acetylcholine-binding+protein&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10759&enzyme=Acetylcholine-binding+protein&column=ki&startPg=0&Increment=50&submit=Search ACH 2ACE,2HA4,2J0H,2RIN,2XZ5,3Q5S,3RQW,3WIP,6V1R,7PRR,7T8X,7T90,7T94,7T96,7TRS,8SSZ,8ST0,8ST1,8ST2,8ST3,8ST4,8XTW,8ZMS,9AVU,9AWJ,9DMH,9DMQ,9E3E,9E3G,9EJZ,9GU2,9GU3 187 172097188 CHEMBL667 DB03128 C01996 1 MRRNIFCLACLWIVQACLSLDRADILYNIRQTSRPDVIPTQRDRPVAVSVSLKFINILEVNEITNEVDVVFWQQTTWSDRTLAWNSSHSPDQVSVPISSLWVPDLAAYNAISKPEVLTPQLARVVSDGEVLYMPSIRQRFSCDVSGVDTESGATCRIKIGSWTHHSREISVDPTTENSDDSEYFSQYSRFEILDVTQKKNSVTYSCCPEAYEDVEVSLNFRKKGRSEIL 8P1F,8P1E,8P11,7NDV,7NDP,4ALX,3WIP,7N43,5T90,4NZB,3ZDH,3ZDG,3U8N,3U8M,3U8L,3U8K,3U8J,1YI5,1UV6,5J5I,5J5H,5J5G,5J5F,5BP0,4ZRU,4ZR6,4ZK1,4ZJT,4QAC,4QAB,4QAA,9SG3 Acetylcholine-binding protein ACHP_LYMST P58154 51023574 CC(=O)OCC[N+](C)(C)C InChI=1S/C7H16NO2/c1-7(9)10-6-5-8(2,3)4/h5-6H2,1-4H3/q+1 OIPILFWXSMYKGL-UHFFFAOYSA-N 10759 2-acetoxyethyl(trimethyl)ammonium;perchlorate::2-acetoxyethyl(trimethyl)ammonium;bromide::acetylcholine chloride::cid_6060::CHEMBL667::[2-(acetyloxy)ethyl]trimethylazanium::acetylcholine::US10667515, Compound ACh Acetylcholine-binding protein Lymnaea stagnalis 6309.57 ChEMBL 10.1016/j.bmc.2011.08.028 10.7270/Q2SN09BH 21920761 Akdemir, A; Rucktooa, P; Jongejan, A; Elk, R; Bertrand, S; Sixma, TK; Bertrand, D; Smit, AB; Leurs, R; de Graaf, C; de Esch, IJ 9/29/2011 3/24/2012 Vu University Amsterdam http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10759 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=5104&target=Acetylcholine-binding+protein&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10759&enzyme=Acetylcholine-binding+protein&column=ki&startPg=0&Increment=50&submit=Search ACH 2ACE,2HA4,2J0H,2RIN,2XZ5,3Q5S,3RQW,3WIP,6V1R,7PRR,7T8X,7T90,7T94,7T96,7TRS,8SSZ,8ST0,8ST1,8ST2,8ST3,8ST4,8XTW,8ZMS,9AVU,9AWJ,9DMH,9DMQ,9E3E,9E3G,9EJZ,9GU2,9GU3 187 172097188 CHEMBL667 DB03128 C01996 1 MRRNIFCLACLWIVQACLSLDRADILYNIRQTSRPDVIPTQRDRPVAVSVSLKFINILEVNEITNEVDVVFWQQTTWSDRTLAWNSSHSPDQVSVPISSLWVPDLAAYNAISKPEVLTPQLARVVSDGEVLYMPSIRQRFSCDVSGVDTESGATCRIKIGSWTHHSREISVDPTTENSDDSEYFSQYSRFEILDVTQKKNSVTYSCCPEAYEDVEVSLNFRKKGRSEIL 8P1F,8P1E,8P11,7NDV,7NDP,4ALX,3WIP,7N43,5T90,4NZB,3ZDH,3ZDG,3U8N,3U8M,3U8L,3U8K,3U8J,1YI5,1UV6,5J5I,5J5H,5J5G,5J5F,5BP0,4ZRU,4ZR6,4ZK1,4ZJT,4QAC,4QAB,4QAA,9SG3 Acetylcholine-binding protein ACHP_LYMST P58154 50788798 CN(C)CCNC(=S)Nc1ccccc1OC InChI=1S/C12H19N3OS/c1-15(2)9-8-13-12(17)14-10-6-4-5-7-11(10)16-3/h4-7H,8-9H2,1-3H3,(H2,13,14,17) WGGARZSAXKSVFS-UHFFFAOYSA-N 50252256 CHEMBL4064806 Acetylcholinesterase Homo sapiens 120000 ChEMBL 10.1016/j.ejmech.2017.03.050 10.7270/Q23X893Z 28433681 Knutsson, S; Kindahl, T; Engdahl, C; Nikjoo, D; Forsgren, N; Kitur, S; Ekström, F; Kamau, L; Linusson, A 7/7/2017 12/1/2019 Ume£ http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50252256 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50252256&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search VY8 8ORC 895655 401962961 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 15300 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 40 8.0000 25.00 C Curated from the literature by BindingDB 10.1021/jm049510k 10.7270/Q27P8WMJ 15771436 aid1796269 Campiani, G; Fattorusso, C; Butini, S; Gaeta, A; Agnusdei, M; Gemma, S; Persico, M; Catalanotti, B; Savini, L; Nacci, V; Novellino, E; Holloway, HW; Greig, NH; Belinskaya, T; Fedorko, JM; Saxena, A 3/24/2005 5/2/2006 Universita Di Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 15341 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Rattus norvegicus 223 8.0000 25.00 C Curated from the literature by BindingDB 10.1016/j.bmcl.2004.07.005 10.7270/Q23X84VR 15324879 aid1796271 Shao, D; Zou, C; Luo, C; Tang, X; Li, Y 9/20/2004 5/2/2006 Shanghai Institute of Materia Medica http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 15348 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 250 8.0000 37.00 C Curated from the literature by BindingDB 10.1021/jm990971t 10.7270/Q2057D4R 10821713 aid1796272 Recanatini, M; Cavalli, A; Belluti, F; Piazzi, L; Rampa, A; Bisi, A; Gobbi, S; Valenti, P; Andrisano, V; Bartolini, M; Cavrini, V 5/18/2000 5/2/2006 University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 15384 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Bos taurus 40 8.0000 30.00 C Curated from the literature by BindingDB 10.1021/jm050746d 10.7270/Q2VD6WN2 16420031 aid1796273 Rodriguez-Franco, MI; Fernandez-Bachiller, MI; Perez, C; Hernandez-Ledesma, B; Bartolome, B 1/26/2006 5/8/2006 Instituto De Quimica Medica (Csic) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 15408 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 350 Curated from the literature by BindingDB 10.1021/jm050746d 10.7270/Q2VD6WN2 16420031 aid1796273 Rodriguez-Franco, MI; Fernandez-Bachiller, MI; Perez, C; Hernandez-Ledesma, B; Bartolome, B 1/26/2006 5/8/2006 Instituto De Quimica Medica (Csic) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 15441 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Bos taurus 167 8.0000 30.00 C Curated from the literature by BindingDB 10.1021/jm0503289 10.7270/Q2QN64Z5 16279781 aid1796276 Munoz-Ruiz, P; Rubio, L; Garcia-Palomero, E; Dorronsoro, I; del Monte-Millan, M; Valenzuela, R; Usan, P; de Austria, C; Bartolini, M; Andrisano, V; Bidon-Chanal, A; Orozco, M; Luque, FJ; Medina, M; Martinez, A 11/17/2005 5/8/2006 Neuropharma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 15517 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Bos taurus 167 8.0000 30.00 C Curated from the literature by BindingDB 10.1016/j.bmc.2005.09.029 10.7270/Q2G73BW9 16230018 aid1796282 Alonso, D; Dorronsoro, I; Rubio, L; Munoz, P; Garcia-Palomero, E; Del Monte, M; Bidon-Chanal, A; Orozco, M; Luque, FJ; Castro, A; Medina, M; Martinez, A 12/15/2005 5/8/2006 Neuropharma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 15557 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 151 250 Curated from the literature by BindingDB 10.1016/s0968-0896(99)00306-5 10.7270/Q2BG2M6F 10732965 aid1796284 Rampa, A; Bisi, A; Belluti, F; Gobbi, S; Valenti, P; Andrisano, V; Cavrini, V; Cavalli, A; Recanatini, M 3/28/2000 5/9/2006 University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 15920 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Rattus norvegicus 319 Curated from the literature by BindingDB 10.1021/jm00128a024 10.7270/Q24Q7S6Z 2754707 aid1796315 Shutske, GM; Pierrat, FA; Kapples, KJ; Cornfeldt, ML; Szewczak, MR; Huger, FP; Bores, GM; Haroutunian, V; Davis, KL 8/28/1989 5/23/2006 Hoechst-Roussel Pharmaceuticals http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 15961 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Rattus norvegicus 223 7.4000 37.00 C Curated from the literature by BindingDB 10.1021/jm990224w 10.7270/Q2W957CH 10514292 aid1796323 Carlier, PR; Chow, ES; Han, Y; Liu, J; El Yazal, J; Pang, YP 10/7/1999 5/25/2006 Hong Kong University of Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 17440 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Rattus norvegicus 590 7.4000 37.00 C Curated from the literature by BindingDB 10.1074/jbc.271.39.23646 10.7270/Q2XW4H0P 8798583 aid1796459 Pang, YP; Quiram, P; Jelacic, T; Hong, F; Brimijoin, S 9/27/1996 7/31/2006 Mayo Foundation http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 17461 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Rattus norvegicus 223 7.4000 37.00 C Curated from the literature by BindingDB 10.1016/s0968-0896(98)00213-2 10.7270/Q2T43R9Q 10218828 aid1796461 Carlier, PR; Han, YF; Chow, ES; Li, CP; Wang, H; Lieu, TX; Wong, HS; Pang, YP 2/28/1999 8/1/2006 Hong Kong University of Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 17501 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 424 8.0000 37.00 C Curated from the literature by BindingDB 10.1021/jm049112h 10.7270/Q2JQ0Z7J 15658850 aid1796463 Rosini, M; Andrisano, V; Bartolini, M; Bolognesi, ML; Hrelia, P; Minarini, A; Tarozzi, A; Melchiorre, C 1/27/2005 8/1/2006 University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 17514 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 40 8.0000 25.00 C Curated from the literature by BindingDB 10.1016/s0960-894x(01)00294-3 10.7270/Q2DZ06JN 11425559 aid1796464 Savini, L; Campiani, G; Gaeta, A; Pellerano, C; Fattorusso, C; Chiasserini, L; Fedorko, JM; Saxena, A 7/9/2001 8/1/2006 Universita Degli Studi Di Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 17693 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 205 8.0000 25.00 C Curated from the literature by BindingDB 10.1021/jm0496741 10.7270/Q21N7ZB6 15771413 aid1796478 Camps, P; Formosa, X; Munoz-Torrero, D; Petrignet, J; Badia, A; Clos, MV 3/24/2005 8/8/2006 Universitat De Barcelona http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 17711 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 137 8.0000 25.00 C Curated from the literature by BindingDB 10.1021/jm060257t 10.7270/Q2WW7FWB 16722663 aid1796481 Gemma, S; Gabellieri, E; Huleatt, P; Fattorusso, C; Borriello, M; Catalanotti, B; Butini, S; De Angelis, M; Novellino, E; Nacci, V; Belinskaya, T; Saxena, A; Campiani, G 6/1/2006 8/5/2006 Universita Di Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 17742 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 190 Curated from the literature by BindingDB 10.1021/jm050578p 10.7270/Q2S75DJ6 16570913 aid1796482 Luo, W; Yu, QS; Kulkarni, SS; Parrish, DA; Holloway, HW; Tweedie, D; Shafferman, A; Lahiri, DK; Brossi, A; Greig, NH 4/6/2006 8/13/2006 National Institutes of Health http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 18675 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 190 8.0000 37.00 C Curated from the literature by BindingDB 10.1021/jm010491d 10.7270/Q22J6933 12166941 aid1796572 Yu, QS; Zhu, X; Holloway, HW; Whittaker, NF; Brossi, A; Greig, NH 8/15/2002 9/12/2006 National Institutes of Health http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 34157 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Bos taurus 446 Curated from the literature by BindingDB 10.1021/jm070536w 10.7270/Q22B8W82 17902635 aid1797820 Sauvaître, T; Barlier, M; Herlem, D; Gresh, N; Chiaroni, A; Guenard, D; Guillou, C 11/1/2007 11/15/2007 Cnrs http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 34167 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 1030 Curated from the literature by BindingDB 10.1021/jm070536w 10.7270/Q22B8W82 17902635 aid1797820 Sauvaître, T; Barlier, M; Herlem, D; Gresh, N; Chiaroni, A; Guenard, D; Guillou, C 11/1/2007 11/15/2007 Cnrs http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 44782 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 6.9 7.4000 22.00 C Curated from the literature by BindingDB 10.1016/s1074-5521(03)00071-1 10.7270/Q2N014T9 12725862 aid1798465 Bencharit, S; Morton, CL; Hyatt, JL; Kuhn, P; Danks, MK; Potter, PM; Redinbo, MR 4/28/2003 9/29/2008 University of North Carolina at Chapel Hill http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 53556 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 147 7.2000 22.00 C Curated from the literature by BindingDB 10.1021/jm801292b 10.7270/Q2C827NZ 19374444 aid1798999 Marco-Contelles, J; León, R; de los Ríos, C; Samadi, A; Bartolini, M; Andrisano, V; Huertas, O; Barril, X; Luque, FJ; Rodríguez-Franco, MI; López, B; López, MG; García, AG; Carreiras Mdo, C; Villarroya, M 5/14/2009 6/9/2009 Csic http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 248238 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Mus musculus 18 7.0000 25.00 C Curated from the literature by BindingDB 10.1021/bi401043w 10.7270/Q24X56GT 24040835 aid1800423 Beri, V; Wildman, SA; Shiomi, K; Al-Rashid, ZF; Cheung, J; Rosenberry, TL 10/22/2013 10/6/2014 Mayo Clinic http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 293113 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 7.64 7.53 8.0000 Curated from the literature by BindingDB 10.1016/j.bioorg.2015.04.006 10.7270/Q2930RW6 25956827 aid1801049 Öztaskin, N; Çetinkaya, Y; Taslimi, P; Göksu, S; Gülçin, Ä° 6/28/2015 9/3/2015 Ataturk University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 293168 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 56 8.0000 25.00 C Curated from the literature by BindingDB 10.1016/j.bioorg.2015.05.005 10.7270/Q2WS8S05 26042530 aid1801052 Kanhed, AM; Sinha, A; Machhi, J; Tripathi, A; Parikh, ZS; Pillai, PP; Giridhar, R; Yadav, MR 8/28/2015 9/8/2015 The M. S. University of Baroda http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 354299 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 1.6e+2 8.0000 25.00 C Curated from the literature by BindingDB 10.1111/cbdd.12800 10.7270/Q26D5RSX 27282589 aid1802080 Osman, W; Mohamed, T; Sit, VM; Vasefi, MS; Beazely, MA; Rao, PP 11/28/2016 11/4/2016 University of Waterloo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50005889 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Mus musculus 81 ChEMBL 10.1021/jm00102a005 10.7270/Q25M64P8 1469686 Sugimoto, H; Tsuchiya, Y; Sugumi, H; Higurashi, K; Karibe, N; Iimura, Y; Sasaki, A; Araki, S; Yamanishi, Y; Yamatsu, K 1/25/1993 11/10/2009 Eisai http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 50006607 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 180 ChEMBL 10.1021/jm00095a008 10.7270/Q200012X 1507203 Valli, MJ; Tang, Y; Kosh, JW; Chapman, JM; Sowell, JW 9/22/1992 11/10/2009 University of South Carolina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50012867 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 52 ChEMBL 10.1021/jm00081a022 10.7270/Q20G3J3J 1738151 Cardozo, MG; Iimura, Y; Sugimoto, H; Yamanishi, Y; Hopfinger, AJ 3/17/1992 11/10/2009 University of Illinois http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50035644 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Rattus norvegicus 310 ChEMBL 10.1021/jm00402a002 10.7270/Q25D8QTS 3385720 Shutske, GM; Pierrat, FA; Cornfeldt, ML; Szewczak, MR; Huger, FP; Bores, GM; Haroutunian, V; Davis, KL 8/5/1988 11/10/2009 Hoechst-Roussel Pharmaceuticals http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50043118 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 75 ChEMBL 10.1021/jm9602266 10.7270/Q20V8BVM 8709135 Pool, WF; Woolf, TF; Reily, MD; Caprathe, BW; Emmerling, MR; Jaen, JC 9/6/1996 11/10/2009 Warner-Lambert http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50048808 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 170 ChEMBL 10.1021/jm00015a002 10.7270/Q2Q52NN0 7636841 Villalobos, A; Butler, TW; Chapin, DS; Chen, YL; DeMattos, SB; Ives, JL; Jones, SB; Liston, DR; Nagel, AA; Nason, DM 9/12/1995 11/10/2009 Pfizer http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50049175 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Rattus norvegicus 63 ChEMBL 10.1021/jm00015a020 10.7270/Q22B8X2S 7636858 Vidaluc, JL; Calmel, F; Bigg, DC; Carilla, E; Briley, M 9/12/1995 11/10/2009 Centre De Recherche Pierre Fabre http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50054652 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 219 ChEMBL 10.1021/jm9810452 10.7270/Q2HH6KRM 9784091 Melchiorre, C; Andrisano, V; Bolognesi, ML; Budriesi, R; Cavalli, A; Cavrini, V; Rosini, M; Tumiatti, V; Recanatini, M 11/23/1998 11/8/2012 University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50061529 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Rattus norvegicus 270.9 ChEMBL 10.1021/jm00041a007 10.7270/Q2SX6C8G 8057278 Ishihara, Y; Hirai, K; Miyamoto, M; Goto, G 9/12/1994 11/10/2009 Takeda Chemical Industries http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50062444 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 270 ChEMBL 10.1021/jm00043a012 10.7270/Q2VT1R4X 8064800 Villalobos, A; Blake, JF; Biggers, CK; Butler, TW; Chapin, DS; Chen, YL; Ives, JL; Jones, SB; Liston, DR; Nagel, AA 9/22/1994 11/10/2009 Pfizer http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50064862 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Rattus norvegicus 110 ChEMBL 10.1021/jm00031a019 10.7270/Q2N29W0C 8126709 Vidaluc, JL; Calmel, F; Bigg, D; Carilla, E; Stenger, A; Chopin, P; Briley, M 4/12/1994 11/10/2009 Centre De Recherche Pierre Fabre MéDicament http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50077029 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 285 ChEMBL 10.1016/j.bmcl.2013.10.034 10.7270/Q2WQ058K 24220172 Mao, F; Chen, J; Zhou, Q; Luo, Z; Huang, L; Li, X 12/2/2013 7/25/2014 Sun Yat-Sen University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50078494 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Rattus norvegicus 320 ChEMBL 10.1021/jm9506433 10.7270/Q2BR8R7K 8558529 Klein, JT; Davis, L; Olsen, GE; Wong, GS; Huger, FP; Smith, CP; Petko, WW; Cornfeldt, M; Wilker, JC; Blitzer, RD; Landau, E; Haroutunian, V; Martin, LL; Effland, RC 2/28/1996 11/10/2009 Hoechst-Roussel Pharmaceuticals http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50082019 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 250 ChEMBL 10.1016/j.ejmech.2014.03.042 10.7270/Q2K075SX 24681980 Belluti, F; De Simone, A; Tarozzi, A; Bartolini, M; Djemil, A; Bisi, A; Gobbi, S; Montanari, S; Cavalli, A; Andrisano, V; Bottegoni, G; Rampa, A 4/14/2014 2/7/2015 University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50082746 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 200 ChEMBL 10.1016/j.ejmech.2014.03.044 10.7270/Q2RJ4M0X 24704618 Kliachyna, M; Santoni, G; Nussbaum, V; Renou, J; Sanson, B; Colletier, JP; Arboléas, M; Loiodice, M; Weik, M; Jean, L; Renard, PY; Nachon, F; Baati, R 4/14/2014 2/7/2015 University of Strasburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50086285 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 78 ChEMBL 10.1021/jm9602266 10.7270/Q20V8BVM 8709135 Pool, WF; Woolf, TF; Reily, MD; Caprathe, BW; Emmerling, MR; Jaen, JC 9/6/1996 11/10/2009 Warner-Lambert http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50086293 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Rattus norvegicus 46 ChEMBL 10.1021/jm9602266 10.7270/Q20V8BVM 8709135 Pool, WF; Woolf, TF; Reily, MD; Caprathe, BW; Emmerling, MR; Jaen, JC 9/6/1996 11/10/2009 Warner-Lambert http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50086295 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Mus musculus 143 ChEMBL 10.1021/jm9602266 10.7270/Q20V8BVM 8709135 Pool, WF; Woolf, TF; Reily, MD; Caprathe, BW; Emmerling, MR; Jaen, JC 9/6/1996 11/10/2009 Warner-Lambert http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 50094636 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 230 ChEMBL 10.1021/jm5000613 10.7270/Q2HX1F61 24738476 López-Iglesias, B; Pérez, C; Morales-García, JA; Alonso-Gil, S; Pérez-Castillo, A; Romero, A; López, MG; Villarroya, M; Conde, S; Rodríguez-Franco, MI 5/8/2014 2/9/2015 IQM-CSIC http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50102054 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Rattus norvegicus 78 ChEMBL 10.1021/jm970150t 10.7270/Q25H7FC9 9357518 McKenna, MT; Proctor, GR; Young, LC; Harvey, AL 12/11/1997 11/10/2009 University of Strathclyde http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50192970 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 180 ChEMBL 10.1021/jm0109356 10.7270/Q298869Q 11689088 Andreani, A; Cavalli, A; Granaiola, M; Guardigli, M; Leoni, A; Locatelli, A; Morigi, R; Rambaldi, M; Recanatini, M; Roda, A 11/5/2001 11/10/2009 Università http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50225821 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 151 ChEMBL 10.1021/jm021055+ 10.7270/Q2RF5TD4 12620072 Tumiatti, V; Rosini, M; Bartolini, M; Cavalli, A; Marucci, G; Andrisano, V; Angeli, P; Banzi, R; Minarini, A; Recanatini, M; Melchiorre, C 3/6/2003 11/10/2009 University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50228172 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Rattus norvegicus 160 ChEMBL 10.1021/jm020391n 10.7270/Q26972X5 12646025 Barreiro, EJ; Camara, CA; Verli, H; Brazil-Mas, L; Castro, NG; Cintra, WM; Aracava, Y; Rodrigues, CR; Fraga, CA 3/20/2003 11/10/2009 Universidade Federal Do Rio De Janeiro http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50237044 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Mus musculus 106 ChEMBL 10.1021/jm501195e 10.7270/Q22V2HQ7 25226236 Brus, B; Košak, U; Turk, S; Pišlar, A; Coquelle, N; Kos, J; Stojan, J; Colletier, JP; Gobec, S 10/9/2014 3/8/2016 University of Ljubljana http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 50237048 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 190 ChEMBL 10.1021/jm501195e 10.7270/Q22V2HQ7 25226236 Brus, B; Košak, U; Turk, S; Pišlar, A; Coquelle, N; Kos, J; Stojan, J; Colletier, JP; Gobec, S 10/9/2014 3/8/2016 University of Ljubljana http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50240362 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 500 ChEMBL 10.1021/jm5010804 10.7270/Q25H7HVD 25259726 Nepovimova, E; Uliassi, E; Korabecny, J; Peña-Altamira, LE; Samez, S; Pesaresi, A; Garcia, GE; Bartolini, M; Andrisano, V; Bergamini, C; Fato, R; Lamba, D; Roberti, M; Kuca, K; Monti, B; Bolognesi, ML 10/23/2014 3/9/2016 Alma Mater Studiorum-University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50269729 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 300 ChEMBL 10.1016/j.bmc.2014.05.032 10.7270/Q2RF5WN3 24934993 Sandhu, S; Bansal, Y; Silakari, O; Bansal, G 7/28/2014 3/23/2016 Punjabi University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50283122 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 72 ChEMBL 10.1016/j.bmc.2014.06.045 10.7270/Q25X2BK0 25047936 Darras, FH; Wehle, S; Huang, G; Sotriffer, CA; Decker, M 8/29/2014 3/28/2016 Universit£T Regensburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50283136 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 72 ChEMBL 10.1016/j.bmc.2014.06.045 10.7270/Q25X2BK0 25047936 Darras, FH; Wehle, S; Huang, G; Sotriffer, CA; Decker, M 8/29/2014 3/28/2016 Universit£T Regensburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50286983 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 36 ChEMBL 10.1016/j.bmc.2014.06.057 10.7270/Q27M09KB 25088549 Sun, Q; Peng, DY; Yang, SG; Zhu, XL; Yang, WC; Yang, GF 8/29/2014 3/31/2016 Central China Normal University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50287083 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 500 ChEMBL 10.1021/jm5008648 10.7270/Q23T9JWH 25089370 Hamulakova, S; Janovec, L; Hrabinova, M; Spilovska, K; Korabecny, J; Kristian, P; Kuca, K; Imrich, J 8/28/2014 3/31/2016 P. J. Safarik University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50287099 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 225 ChEMBL 10.1021/jm5008648 10.7270/Q23T9JWH 25089370 Hamulakova, S; Janovec, L; Hrabinova, M; Spilovska, K; Korabecny, J; Kristian, P; Kuca, K; Imrich, J 8/28/2014 3/31/2016 P. J. Safarik University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50287106 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 101 ChEMBL 10.1021/jm5008648 10.7270/Q23T9JWH 25089370 Hamulakova, S; Janovec, L; Hrabinova, M; Spilovska, K; Korabecny, J; Kristian, P; Kuca, K; Imrich, J 8/28/2014 3/31/2016 P. J. Safarik University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50289974 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 90 ChEMBL 10.1016/j.bmcl.2004.10.067 10.7270/Q2CN73CD 15603953 Yoo, ID; Cho, KM; Lee, CK; Kim, WG 12/17/2004 11/10/2009 Korea Research Institute of Bioscience and Biotechnology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50294105 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 484 ChEMBL 10.1016/j.bmcl.2014.12.071 10.7270/Q22B90QH 25597004 Decroocq, C; Stauffert, F; Pamlard, O; Oulaïdi, F; Gallienne, E; Martin, OR; Guillou, C; Compain, P 2/4/2015 4/3/2016 University of Strasburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50301299 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 131 ChEMBL 10.1016/j.bmc.2015.01.045 10.7270/Q2PN979Q 25707322 Guzior, N; Bajda, M; Rakoczy, J; Brus, B; Gobec, S; Malawska, B 3/17/2015 4/9/2016 Jagiellonian University Medical College http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50307863 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 200 ChEMBL 10.1016/j.bmcl.2005.04.005 10.7270/Q2SJ1K4G 15878275 Bianchi, DA; Hirschmann, GS; Theoduloz, C; Bracca, AB; Kaufman, TS 5/24/2005 11/10/2009 Universidad Nacional De Rosario http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50314708 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 435 ChEMBL 10.1016/j.ejmech.2015.01.058 10.7270/Q2154JRN 25656088 Xie, SS; Lan, JS; Wang, XB; Jiang, N; Dong, G; Li, ZR; Wang, KD; Guo, PP; Kong, LY 3/13/2015 4/22/2016 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50318268 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 131 ChEMBL 10.1016/j.ejmech.2015.01.027 10.7270/Q23T9JXZ 25621991 Guzior, N; Bajda, M; Skrok, M; Kurpiewska, K; Lewinski, K; Brus, B; Pišlar, A; Kos, J; Gobec, S; Malawska, B 2/20/2015 4/24/2016 Jagiellonian University Medical College http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50325873 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 420 ChEMBL 10.1016/j.ejmech.2015.03.040 10.7270/Q20R9R4H 25812965 Xie, SS; Wang, X; Jiang, N; Yu, W; Wang, KD; Lan, JS; Li, ZR; Kong, LY 4/20/2015 4/28/2016 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50358479 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Mus musculus 106 ChEMBL 10.1016/j.bmc.2015.06.010 10.7270/Q2W097PZ 26116179 Knez, D; Brus, B; Coquelle, N; Sosic, I; Šink, R; Brazzolotto, X; Mravljak, J; Colletier, JP; Gobec, S 7/27/2015 10/18/2016 University of Ljubljana http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 50358543 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Rattus norvegicus 223 ChEMBL 10.1021/jm060164b 10.7270/Q2154GPX 16942022 Rydberg, EH; Brumshtein, B; Greenblatt, HM; Wong, DM; Shaya, D; Williams, LD; Carlier, PR; Pang, YP; Silman, I; Sussman, JL 8/31/2006 11/10/2009 Institute of Science http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50367854 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 467 ChEMBL 10.1016/j.bmc.2014.08.035 10.7270/Q2M61N1Z 25282654 Lan, JS; Xie, SS; Li, SY; Pan, LF; Wang, XB; Kong, LY 12/2/2014 10/27/2016 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50368525 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 147 ChEMBL 10.1021/jm061047j 10.7270/Q26T0M97 17181144 Marco-Contelles, J; Leon, R; de Los Rios, C; Guglietta, A; Terencio, J; Lopez, MG; Garcia, AG; Villarroya, M 12/21/2006 11/10/2009 Laboratorio De Radicales Libres (Iqog, Csic) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50381329 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 300 ChEMBL 10.1016/j.bmcl.2015.05.002 10.7270/Q2TB18P5 26003339 Rampa, A; Mancini, F; De Simone, A; Falchi, F; Belluti, F; Di Martino, RM; Gobbi, S; Andrisano, V; Tarozzi, A; Bartolini, M; Cavalli, A; Bisi, A 6/8/2015 11/10/2016 University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50393650 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Rattus norvegicus 200 ChEMBL 10.1016/j.ejmech.2007.04.018 10.7270/Q2TH8MG0 17624631 Andreani, A; Burnelli, S; Granaiola, M; Guardigli, M; Leoni, A; Locatelli, A; Morigi, R; Rambaldi, M; Rizzoli, M; Varoli, L; Roda, A 3/10/2008 1/11/2010 Università http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50400948 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 501 ChEMBL 10.1016/j.bmc.2015.07.029 10.7270/Q25T3N9G 26242241 Bajda, M; Jonczyk, J; Malawska, B; Czarnecka, K; Girek, M; Olszewska, P; Sikora, J; Mikiciuk-Olasik, E; Skibinski, R; Gumieniczek, A; Szymanski, P 8/31/2015 11/23/2016 Jagiellonian University Medical College http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50407186 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 424 ChEMBL 10.1021/jm701225u 10.7270/Q2FN15Z6 18047264 Bolognesi, ML; Cavalli, A; Valgimigli, L; Bartolini, M; Rosini, M; Andrisano, V; Recanatini, M; Melchiorre, C 12/20/2007 11/11/2009 Bologna University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50420947 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Bos taurus 134 ChEMBL 10.1016/j.bmc.2008.06.022 10.7270/Q2NC611F 18585045 Leonetti, F; Catto, M; Nicolotti, O; Pisani, L; Cappa, A; Stefanachi, A; Carotti, A 8/11/2008 1/11/2010 Università http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 50422508 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 424 ChEMBL 10.1021/jm800577j 10.7270/Q21G0M23 18605718 Rosini, M; Simoni, E; Bartolini, M; Cavalli, A; Ceccarini, L; Pascu, N; McClymont, DW; Tarozzi, A; Bolognesi, ML; Minarini, A; Tumiatti, V; Andrisano, V; Mellor, IR; Melchiorre, C 8/7/2008 1/11/2010 University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50431874 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 36 ChEMBL 10.1016/j.bmcl.2008.08.076 10.7270/Q29W0F9S 18786825 Butini, S; Guarino, E; Campiani, G; Brindisi, M; Coccone, SS; Fiorini, I; Novellino, E; Belinskaya, T; Saxena, A; Gemma, S 9/23/2008 1/11/2010 European Research Centre For Drug Discovery and Development (Natsyndrugs) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50433266 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 200 ChEMBL 10.1016/j.bmcl.2015.06.047 10.7270/Q2668G1T 26159481 Al-Rashid, ZF; Hsung, RP 10/14/2015 12/17/2016 Alchemical Research http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50439102 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 320 ChEMBL 10.1021/acs.jmedchem.5b01325 10.7270/Q29P33GZ 26503905 Nepovimova, E; Korabecny, J; Dolezal, R; Babkova, K; Ondrejicek, A; Jun, D; Sepsova, V; Horova, A; Hrabinova, M; Soukup, O; Bukum, N; Jost, P; Muckova, L; Kassa, J; Malinak, D; Andrs, M; Kuca, K 11/25/2015 12/22/2016 University Hospital Hradec Kralove http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50452568 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 424 ChEMBL 10.1021/acs.jmedchem.5b01119 10.7270/Q2S75J5X 26632651 Zha, X; Lamba, D; Zhang, L; Lou, Y; Xu, C; Kang, D; Chen, L; Xu, Y; Zhang, L; De Simone, A; Samez, S; Pesaresi, A; Stojan, J; Lopez, MG; Egea, J; Andrisano, V; Bartolini, M 1/14/2016 5/31/2017 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50462852 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 143 ChEMBL 10.1016/S0960-894X(00)80267-X 10.7270/Q2G73DN0 Desai, MC; Thadeio, PF; Lipinski, CA; Liston, DR; Spencer, RW; Williams, IH 12/28/1991 8/17/2010 TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50464313 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 34 ChEMBL 10.1016/S0960-894X(00)80545-4 10.7270/Q29886XS Gregor, VE; Emmerling, MR; Lee, C; Moore, CJ 12/28/1992 8/17/2010 TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50464340 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Rattus norvegicus 230 ChEMBL 10.1016/S0960-894X(00)80546-6 10.7270/Q25H7G51 Shutske, GM; Bores, GM; Bradshaw, KC; Huger, FP; Kapples, KJ; Larsen, RD; Rush, DK; Tomer, JD 12/28/1992 8/17/2010 TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50464371 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Rattus norvegicus 81 ChEMBL 10.1016/S0960-894X(00)80547-8 10.7270/Q21R6QDV Sugimoto, H; Iimura, Y; Yamanishi, Y; Yamatsu, K 12/28/1992 8/17/2010 TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50476825 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Bos taurus 550 ChEMBL 10.1016/0960-894X(95)00562-8 10.7270/Q27W6C5T Holan, G; Virgona, CT; Watson, KG; Finkelstein, BL 12/28/1996 8/20/2010 TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 50484775 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Rattus norvegicus 200 ChEMBL 10.1016/S0960-894X(97)10025-7 10.7270/Q2KW5G10 Valenti, P; Rampa, A; Bisi, A; Andrisano, V; Cavrini, V; Fin, L; Buriani, A; Giusti, P 12/28/1997 8/22/2010 TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50484779 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 254 ChEMBL 10.1016/S0960-894X(97)10025-7 10.7270/Q2KW5G10 Valenti, P; Rampa, A; Bisi, A; Andrisano, V; Cavrini, V; Fin, L; Buriani, A; Giusti, P 12/28/1997 8/22/2010 TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50489464 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 7.6 ChEMBL 10.1016/j.bmc.2016.04.002 10.7270/Q2930W3J 27068142 Özgeris, B; Göksu, S; Polat Köse, L; Gülçin, I; Salmas, RE; Durdagi, S; Tümer, F; Supuran, CT 4/23/2016 8/5/2017 Erzurum Technical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50489504 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 7.5 ChEMBL 10.1016/j.bmc.2016.04.002 10.7270/Q2930W3J 27068142 Özgeris, B; Göksu, S; Polat Köse, L; Gülçin, I; Salmas, RE; Durdagi, S; Tümer, F; Supuran, CT 4/23/2016 8/5/2017 Erzurum Technical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50508689 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 450 ChEMBL 10.1016/j.bmc.2016.07.025 10.7270/Q2DV1MV0 27460699 Wang, J; Wang, ZM; Li, XM; Li, F; Wu, JJ; Kong, LY; Wang, XB 8/22/2016 10/6/2017 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50513633 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 200 ChEMBL 10.1021/np9001515 10.7270/Q22807ND 19422203 Wang, YH; Long, CL; Yang, FM; Wang, X; Sun, QY; Wang, HS; Shi, YN; Tang, GH 6/26/2009 8/27/2010 Chinese Academy of Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50520400 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Rattus norvegicus 114 ChEMBL 10.1016/j.ejmech.2016.06.025 10.7270/Q2X92D8D 27392529 Ceschi, MA; da Costa, JS; Lopes, JPB; Câmara, VS; Campo, LF; Borges, ACA; Gonçalves, CAS; de Souza, DF; Konrath, EL; Karl, ALM; Guedes, IA; Dardenne, LE 10/4/2016 7/4/2018 Universidade Federal Do Rio Grande Do Sul http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50534610 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Rattus norvegicus 8.8E1 ChEMBL 10.1016/j.ejmech.2009.10.039 10.7270/Q27W6C85 19954865 dos Santos Pisoni, D; Sobieski da Costa, J; Gamba, D; Petzhold, CL; de Amorim Borges, AC; Ceschi, MA; Lunardi, P; Saraiva Goncalves, CA 2/1/2010 8/29/2010 Universidade Federal Do Rio Grande Do Sul http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50534830 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 459 ChEMBL 10.1016/j.ejmech.2016.07.052 10.7270/Q2ZW1NW5 27484514 Wang, ZM; Cai, P; Liu, QH; Xu, DQ; Yang, XL; Wu, JJ; Kong, LY; Wang, XB 11/10/2016 8/17/2018 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50540047 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Mus musculus 115 ChEMBL 10.1016/j.bmc.2016.11.032 10.7270/Q2HH6N2G 27908752 Košak, U; Knez, D; Coquelle, N; Brus, B; Pišlar, A; Nachon, F; Brazzolotto, X; Kos, J; Colletier, JP; Gobec, S 1/15/2017 8/24/2018 University of Ljubljana http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 50543772 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 131 ChEMBL 10.1016/j.ejmech.2016.08.016 10.7270/Q2PZ5BT8 27560283 Wieckowska, A; Kolaczkowski, M; Bucki, A; Godyn, J; Marcinkowska, M; Wieckowski, K; Zareba, P; Siwek, A; Kazek, G; Gluch-Lutwin, M; Mierzejewski, P; Bienkowski, P; Sienkiewicz-Jarosz, H; Knez, D; Wichur, T; Gobec, S; Malawska, B 11/29/2016 8/31/2018 Jagiellonian University Collegium Medicum http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50544891 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 128 ChEMBL 10.1016/j.bmc.2009.08.017 10.7270/Q2J966GQ 19726199 Yan, J; Sun, L; Wu, G; Yi, P; Yang, F; Zhou, L; Zhang, X; Li, Z; Yang, X; Luo, H; Qiu, M 9/16/2009 8/31/2010 The Chinese Academy of Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50561687 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Bos taurus 40 ChEMBL 10.1021/jm900628z 10.7270/Q2668DB1 19856923 Arce, MP; Rodriguez-Franco, MI; Gonzalez-Munoz, GC; Perez, C; Lopez, B; Villarroya, M; Lopez, MG; Garcia, AG; Conde, S 11/20/2009 11/17/2010 Instituto De Quimica Medica (Csic) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 50561705 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 350 ChEMBL 10.1021/jm900628z 10.7270/Q2668DB1 19856923 Arce, MP; Rodriguez-Franco, MI; Gonzalez-Munoz, GC; Perez, C; Lopez, B; Villarroya, M; Lopez, MG; Garcia, AG; Conde, S 11/20/2009 11/17/2010 Instituto De Quimica Medica (Csic) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50578129 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 223 ChEMBL 10.1016/j.ejmech.2009.12.038 10.7270/Q25H7GFM 20053484 Lv, W; Xue, Y 2/17/2010 11/20/2010 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50586380 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 350 ChEMBL 10.1021/jm100329q 10.7270/Q22Z15QR 20545360 Fernandez-Bachiller, MI; Perez, C; Gonzalez-Munoz, GC; Conde, S; Lopez, MG; Villarroya, M; Garcia, AG; Rodriguez-Franco, MI 7/1/2010 11/21/2010 Instituto De Quimica Medica http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50586404 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Bos taurus 40 ChEMBL 10.1021/jm100329q 10.7270/Q22Z15QR 20545360 Fernandez-Bachiller, MI; Perez, C; Gonzalez-Munoz, GC; Conde, S; Lopez, MG; Villarroya, M; Garcia, AG; Rodriguez-Franco, MI 7/1/2010 11/21/2010 Instituto De Quimica Medica http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 50597952 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 800 ChEMBL 10.1021/jm100573q 10.7270/Q23R0T3D 20684567 Chaudhaery, SS; Roy, KK; Shakya, N; Saxena, G; Sammi, SR; Nazir, A; Nath, C; Saxena, AK 9/2/2010 6/11/2011 Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50601922 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 500 ChEMBL 10.1016/j.bmcl.2010.08.044 10.7270/Q2K937RW 20817518 Korabecny, J; Musilek, K; Holas, O; Binder, J; Zemek, F; Marek, J; Pohanka, M; Opletalova, V; Dohnal, V; Kuca, K 9/20/2010 6/12/2011 Charles University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50613086 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Bos taurus 40 ChEMBL 10.1016/j.ejmech.2010.09.039 10.7270/Q2KW5G84 20926162 Gonzalez-Munoz, GC; Arce, MP; Lopez, B; Perez, C; Villarroya, M; Lopez, MG; Garcia, AG; Conde, S; Rodriguez-Franco, MI 11/24/2010 8/20/2011 IQM-CSIC http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 50614018 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Bos taurus 109 ChEMBL 10.1016/j.bmc.2010.11.040 10.7270/Q22R3RX5 21163662 Samadi, A; Valderas, C; de los Rios, C; Bastida, A; Chioua, M; Gonzalez-Lafuente, L; Colmena, I; Gandia, L; Romero, A; Del Barrio, L; Martin-de-Saavedra, MD; Lopez, MG; Villarroya, M; Marco-Contelles, J 1/3/2011 8/21/2011 Laboratorio De Radicales Libres Y Qu�Mica Computacional (Iqog, Csic) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 50635768 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 93 ChEMBL 10.1016/j.bmc.2011.02.030 10.7270/Q2Q240JH 21429752 Mohamed, T; Zhao, X; Habib, LK; Yang, J; Rao, PP 3/29/2011 12/3/2011 University of Waterloo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50636570 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 200 ChEMBL 10.1016/j.bmcl.2010.12.041 10.7270/Q27W6CH9 21216144 Al-Rashid, ZF; Hsung, RP 4/25/2011 12/3/2011 Alchemical Research http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50637196 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 110 ChEMBL 10.1021/jm101299d 10.7270/Q2SQ90QT 21417225 Conejo-Garcia, A; Pisani, L; Nunez, Mdel C; Catto, M; Nicolotti, O; Leonetti, F; Campos, JM; Gallo, MA; Espinosa, A; Carotti, A 4/21/2011 12/4/2011 Universidad De Granada http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50645273 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 484 ChEMBL 10.1016/j.ejmech.2011.02.073 10.7270/Q2VM4CMQ 21435752 Rouleau, J; Iorga, BI; Guillou, C 5/2/2011 12/6/2011 Cnrs http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50645448 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 190 ChEMBL 10.1016/j.ejmech.2011.02.071 10.7270/Q2BK1CPG 21459491 Tasso, B; Catto, M; Nicolotti, O; Novelli, F; Tonelli, M; Giangreco, I; Pisani, L; Sparatore, A; Boido, V; Carotti, A; Sparatore, F 5/2/2011 12/6/2011 University of Genoa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50645456 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 190 ChEMBL 10.1016/j.ejmech.2011.02.071 10.7270/Q2BK1CPG 21459491 Tasso, B; Catto, M; Nicolotti, O; Novelli, F; Tonelli, M; Giangreco, I; Pisani, L; Sparatore, A; Boido, V; Carotti, A; Sparatore, F 5/2/2011 12/6/2011 University of Genoa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50645464 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 47 ChEMBL 10.1016/j.ejmech.2011.02.071 10.7270/Q2BK1CPG 21459491 Tasso, B; Catto, M; Nicolotti, O; Novelli, F; Tonelli, M; Giangreco, I; Pisani, L; Sparatore, A; Boido, V; Carotti, A; Sparatore, F 5/2/2011 12/6/2011 University of Genoa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50645474 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 47 ChEMBL 10.1016/j.ejmech.2011.02.071 10.7270/Q2BK1CPG 21459491 Tasso, B; Catto, M; Nicolotti, O; Novelli, F; Tonelli, M; Giangreco, I; Pisani, L; Sparatore, A; Boido, V; Carotti, A; Sparatore, F 5/2/2011 12/6/2011 University of Genoa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50653060 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 3.16 ChEMBL 10.1016/j.ejmech.2011.04.038 10.7270/Q2J67H9J 21570751 Szymanski, P; Karpinski, A; Mikiciuk-Olasik, E 6/13/2011 3/23/2012 Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50655752 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 250 ChEMBL 10.1016/j.ejmech.2011.07.004 10.7270/Q2NP24TK 21798635 Rizzo, S; Bisi, A; Bartolini, M; Mancini, F; Belluti, F; Gobbi, S; Andrisano, V; Rampa, A 8/31/2011 3/23/2012 Institut F£R Molekulare Physiologie http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50664188 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 77 ChEMBL 10.1016/j.bmcl.2011.07.091 10.7270/Q2C829P7 21873056 Mohamed, T; Yeung, JC; Rao, PP 9/12/2011 3/24/2012 University of Waterloo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50665710 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 1026 ChEMBL 10.1021/np200308j 10.7270/Q2XW4K5R 21939219 Liu, J; Dumontet, V; Simonin, AL; Iorga, BI; Guerineau, V; Litaudon, M; Nguyen, VH; Gueritte, F 10/28/2011 3/24/2012 Guangzhou University of Chinese Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50700691 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 500 ChEMBL 10.1016/j.bmcl.2011.08.042 10.7270/Q2HD7W2Q 21920739 Korabecny, J; Musilek, K; Zemek, F; Horova, A; Holas, O; Nepovimova, E; Opletalova, V; Hroudova, J; Fisar, Z; Jung, YS; Kuca, K 10/10/2011 7/21/2012 Charles University In Prague http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50706636 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 122 ChEMBL 10.1021/jm200853t 10.7270/Q20P10G5 22023459 Bolea, I; Juarez-Jimenez, J; de Los Rios, C; Chioua, M; Pouplana, R; Luque, FJ; Unzeta, M; Marco-Contelles, J; Samadi, A 12/15/2011 7/21/2012 Universitat Aut£Noma De Barcelona http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50711454 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Bos taurus 40 ChEMBL 10.1016/j.ejmech.2011.03.003 10.7270/Q2X34XWC 21420206 Gonzalez-Munoz, GC; Arce, MP; Lopez, B; Perez, C; Romero, A; del Barrio, L; Martin-de-Saavedra, MD; Egea, J; Leon, R; Villarroya, M; Lopez, MG; Garcia, AG; Conde, S; Rodriguez-Franco, MI 5/2/2011 7/22/2012 IQM-CSIC http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 50712743 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 130 ChEMBL 10.1016/j.ejmech.2016.11.050 10.7270/Q21R6SR5 27918993 Dgachi, Y; Sokolov, O; Luzet, V; Godyn, J; Panek, D; Bonet, A; Martin, H; Iriepa, I; Moraleda, I; García-Iriepa, C; Janockova, J; Richert, L; Soukup, O; Malawska, B; Chabchoub, F; Marco-Contelles, J; Ismaili, L 1/27/2017 6/18/2019 University of Sfax http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50715679 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 160 ChEMBL 10.1016/j.ejmech.2016.12.005 10.7270/Q2D220WF 27951490 Mohamed, T; Rao, PPN 1/27/2017 6/19/2019 University of Waterloo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50726050 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Rattus norvegicus 200 ChEMBL 10.1016/0960-894X(96)00102-3 10.7270/Q2736RDK Jaen, JC; Gregor, VE; Lee, C; Davis, R; Emmerling, M 12/28/1996 9/27/2012 TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50726056 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 30 ChEMBL 10.1016/0960-894X(96)00102-3 10.7270/Q2736RDK Jaen, JC; Gregor, VE; Lee, C; Davis, R; Emmerling, M 12/28/1996 9/27/2012 TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50729413 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Rattus norvegicus 223 ChEMBL 10.1016/s0960-894x(99)00396-0 10.7270/Q2PK0GPF 10476864 Carlier, PR; Du, DM; Han, Y; Liu, J; Pang, YP 10/14/1999 9/30/2012 Hong Kong University of Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50763305 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 180 ChEMBL 10.1021/jm00084a015 10.7270/Q28K79QR 1552502 Sowell, JW; Tang, Y; Valli, MJ; Chapman, JM; Usher, LA; Vaughan, CM; Kosh, JW 4/28/1992 10/24/2012 University of South Carolina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50764487 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 19 ChEMBL 10.1021/acs.jmedchem.7b01760 10.7270/Q2RJ4MWK 29400965 Dolles, D; Hoffmann, M; Gunesch, S; Marinelli, O; Möller, J; Santoni, G; Chatonnet, A; Lohse, MJ; Wittmann, HJ; Strasser, A; Nabissi, M; Maurice, T; Decker, M 2/22/2018 10/21/2019 Julius Maximilian University of W£Rzburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50764510 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 20 ChEMBL 10.1021/acs.jmedchem.7b01760 10.7270/Q2RJ4MWK 29400965 Dolles, D; Hoffmann, M; Gunesch, S; Marinelli, O; Möller, J; Santoni, G; Chatonnet, A; Lohse, MJ; Wittmann, HJ; Strasser, A; Nabissi, M; Maurice, T; Decker, M 2/22/2018 10/21/2019 Julius Maximilian University of W£Rzburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50774395 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Mus musculus 80 ChEMBL 10.1021/jm00024a009 10.7270/Q2QC045T 7490731 Sugimoto, H; Iimura, Y; Yamanishi, Y; Yamatsu, K 1/2/1996 10/31/2012 Eisai http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 50774929 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 267 ChEMBL 10.1021/jm00007a005 10.7270/Q21N81S7 7707311 Nagel, AA; Liston, DR; Jung, S; Mahar, M; Vincent, LA; Chapin, D; Chen, YL; Hubbard, S; Ives, JL; Jones, SB 5/11/1995 10/31/2012 Pfizer http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50779123 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 76.0 ChEMBL 10.1021/jm950771r 10.7270/Q2PZ59GC 8978837 Cho, SJ; Garsia, ML; Bier, J; Tropsha, A 1/24/1997 11/3/2012 University of North Carolina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50790418 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Bos taurus 130 ChEMBL 10.1021/jm980620z 10.7270/Q2H70GH6 10464010 Camps, P; El Achab, R; Gorbig, DM; Morral, J; Munoz-Torrero, D; Badia, A; Eladi Banos, J; Vivas, NM; Barril, X; Orozco, M; Luque, FJ 9/20/1999 11/12/2012 Universitat De Barcelona http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 50793121 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 95 ChEMBL 10.1021/jm981101z 10.7270/Q26M37JW 10052979 Contreras, JM; Rival, YM; Chayer, S; Bourguignon, JJ; Wermuth, CG 3/16/1999 11/13/2012 Louis Pasteur University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50798513 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Bos taurus 130 ChEMBL 10.1021/jm000980y 10.7270/Q2Q52Q9B 11101357 Camps, P; El Achab R, na; Morral, J; Munoz-Torrero, D; Badia, A; Banos, JE; Vivas, NM; Barril, X; Orozco, M; Luque, FJ 8/13/2001 11/25/2012 Universitat De Barcelona http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 50798526 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 205 ChEMBL 10.1021/jm000980y 10.7270/Q2Q52Q9B 11101357 Camps, P; El Achab R, na; Morral, J; Munoz-Torrero, D; Badia, A; Banos, JE; Vivas, NM; Barril, X; Orozco, M; Luque, FJ 8/13/2001 11/25/2012 Universitat De Barcelona http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50802109 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 95 ChEMBL 10.1021/jm001088u 10.7270/Q2222VG9 11495583 Contreras, JM; Parrot, I; Sippl, W; Rival, YM; Wermuth, CG 8/9/2001 11/25/2012 Louis Pasteur University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50803461 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Bos taurus 130 ChEMBL 10.1021/jm010949b 10.7270/Q2SF2WWD 11741490 Camps, P; Gomez, E; Munoz-Torrero, D; Badia, A; Vivas, NM; Barril, X; Orozco, M; Luque, FJ 12/19/2001 11/26/2012 Universitat De Barcelona http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 50803463 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 205 ChEMBL 10.1021/jm010949b 10.7270/Q2SF2WWD 11741490 Camps, P; Gomez, E; Munoz-Torrero, D; Badia, A; Vivas, NM; Barril, X; Orozco, M; Luque, FJ 12/19/2001 11/26/2012 Universitat De Barcelona http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50811187 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Bos taurus 40 ChEMBL 10.1021/jm0255668 10.7270/Q2GF0V7X 12502352 Savini, L; Gaeta, A; Fattorusso, C; Catalanotti, B; Campiani, G; Chiasserini, L; Pellerano, C; Novellino, E; McKissic, D; Saxena, A 12/27/2002 11/27/2012 University of Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 50819208 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Rattus norvegicus 590 ChEMBL 10.1021/jm040031v 10.7270/Q2NC61ZJ 15214773 Erlanson, DA; McDowell, RS; O'Brien, T 6/24/2004 11/30/2012 Sunesis Pharmaceuticals http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50819245 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Mus musculus 18 ChEMBL 10.1021/jm040031v 10.7270/Q2NC61ZJ 15214773 Erlanson, DA; McDowell, RS; O'Brien, T 6/24/2004 11/30/2012 Sunesis Pharmaceuticals http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 50828047 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 424 ChEMBL 10.1021/jm049156q 10.7270/Q2P84CPM 15633997 Bolognesi, ML; Andrisano, V; Bartolini, M; Banzi, R; Melchiorre, C 1/6/2005 12/3/2012 University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50828054 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 151 ChEMBL 10.1021/jm049156q 10.7270/Q2P84CPM 15633997 Bolognesi, ML; Andrisano, V; Bartolini, M; Banzi, R; Melchiorre, C 1/6/2005 12/3/2012 University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50828391 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 267 ChEMBL 10.1021/jm0493461 10.7270/Q2HH6KTH 15887964 Cappelli, A; Gallelli, A; Manini, M; Anzini, M; Mennuni, L; Makovec, F; Menziani, MC; Alcaro, S; Ortuso, F; Vomero, S 5/12/2005 12/3/2012 University of Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50830756 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 190 ChEMBL 10.1021/jm049309+ 10.7270/Q2TM7BWQ 15715468 Luo, W; Yu, QS; Zhan, M; Parrish, D; Deschamps, JR; Kulkarni, SS; Holloway, HW; Alley, GM; Lahiri, DK; Brossi, A; Greig, NH 2/17/2005 12/3/2012 National Institute On Aging http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50840687 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 205 ChEMBL 10.1021/jm060945c 10.7270/Q29K4C1S 17154513 Camps, P; Gomez, E; Munoz-Torrero, D; Badia, A; Clos, MV; Curutchet, C; Munoz-Muriedas, J; Luque, FJ 12/12/2006 12/8/2012 Universitat De Barcelona http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50840701 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Bos taurus 130 ChEMBL 10.1021/jm060945c 10.7270/Q29K4C1S 17154513 Camps, P; Gomez, E; Munoz-Torrero, D; Badia, A; Clos, MV; Curutchet, C; Munoz-Muriedas, J; Luque, FJ 12/12/2006 12/8/2012 Universitat De Barcelona http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 50848522 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 424 ChEMBL 10.1021/jm070559a 10.7270/Q218379R 17850125 Bolognesi, ML; Banzi, R; Bartolini, M; Cavalli, A; Tarozzi, A; Andrisano, V; Minarini, A; Rosini, M; Tumiatti, V; Bergamini, C; Fato, R; Lenaz, G; Hrelia, P; Cattaneo, A; Recanatini, M; Melchiorre, C 9/27/2007 12/11/2012 University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50849608 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 136 ChEMBL 10.1021/jm070859s 10.7270/Q2NS0VRN 17944454 Elsinghorst, PW; Cieslik, JS; Mohr, K; Trankle, C; Gutschow, M 11/8/2007 12/12/2012 University of Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50849620 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 926 ChEMBL 10.1021/jm070859s 10.7270/Q2NS0VRN 17944454 Elsinghorst, PW; Cieslik, JS; Mohr, K; Trankle, C; Gutschow, M 11/8/2007 12/12/2012 University of Bonn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50852143 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 200 ChEMBL 10.1021/np0702077 10.7270/Q2MK6DQQ 17822295 Wang, YH; Zhang, ZK; Yang, FM; Sun, QY; He, HP; Di, YT; Mu, SZ; Lu, Y; Chang, Y; Zheng, QT; Ding, M; Dong, JH; Hao, XJ 10/1/2007 12/14/2012 Chinese Academy of Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50852951 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 600 ChEMBL 10.1016/j.bmc.2017.09.028 10.7270/Q2FT8PHZ 28986116 Makhaeva, GF; Lushchekina, SV; Boltneva, NP; Serebryakova, OG; Rudakova, EV; Ustyugov, AA; Bachurin, SO; Shchepochkin, AV; Chupakhin, ON; Charushin, VN; Richardson, RJ 11/1/2017 1/26/2020 Institute of Physiologically Active Compounds Russian Academy of Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50853579 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 420 ChEMBL 10.1021/jm7009364 10.7270/Q25B039W 18181565 Cavalli, A; Bolognesi, ML; Minarini, A; Rosini, M; Tumiatti, V; Recanatini, M; Melchiorre, C 2/7/2008 12/14/2012 University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50854739 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 45.1 ChEMBL 10.1021/jm701491k 10.7270/Q2XP75SX 18232655 Fang, L; Appenroth, D; Decker, M; Kiehntopf, M; Roegler, C; Deufel, T; Fleck, C; Peng, S; Zhang, Y; Lehmann, J 2/21/2008 12/14/2012 TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50871611 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 36.0 ChEMBL 10.1021/jm701253t 10.7270/Q22Z16D4 18479118 Butini, S; Campiani, G; Borriello, M; Gemma, S; Panico, A; Persico, M; Catalanotti, B; Ros, S; Brindisi, M; Agnusdei, M; Fiorini, I; Nacci, V; Novellino, E; Belinskaya, T; Saxena, A; Fattorusso, C 6/5/2008 12/16/2012 University of Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50871660 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Bos taurus 445 ChEMBL 10.1021/jm701253t 10.7270/Q22Z16D4 18479118 Butini, S; Campiani, G; Borriello, M; Gemma, S; Panico, A; Persico, M; Catalanotti, B; Ros, S; Brindisi, M; Agnusdei, M; Fiorini, I; Nacci, V; Novellino, E; Belinskaya, T; Saxena, A; Fattorusso, C 6/5/2008 12/16/2012 University of Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 50871838 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Bos taurus 130 ChEMBL 10.1021/jm8001313 10.7270/Q2F76DGK 18517184 Camps, P; Formosa, X; Galdeano, C; Gomez, T; Munoz-Torrero, D; Scarpellini, M; Viayna, E; Badia, A; Clos, MV; Camins, A; Pallas, M; Bartolini, M; Mancini, F; Andrisano, V; Estelrich, J; Lizondo, M; Bidon-Chanal, A; Luque, FJ 6/19/2008 12/16/2012 Laboratori De Qu�Mica Farmac�Utica (Unitat Associada Al Csic) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 50871848 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 205 ChEMBL 10.1021/jm8001313 10.7270/Q2F76DGK 18517184 Camps, P; Formosa, X; Galdeano, C; Gomez, T; Munoz-Torrero, D; Scarpellini, M; Viayna, E; Badia, A; Clos, MV; Camins, A; Pallas, M; Bartolini, M; Mancini, F; Andrisano, V; Estelrich, J; Lizondo, M; Bidon-Chanal, A; Luque, FJ 6/19/2008 12/16/2012 Laboratori De Qu�Mica Farmac�Utica (Unitat Associada Al Csic) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50871870 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Rattus norvegicus 223 ChEMBL 10.1021/jm8001313 10.7270/Q2F76DGK 18517184 Camps, P; Formosa, X; Galdeano, C; Gomez, T; Munoz-Torrero, D; Scarpellini, M; Viayna, E; Badia, A; Clos, MV; Camins, A; Pallas, M; Bartolini, M; Mancini, F; Andrisano, V; Estelrich, J; Lizondo, M; Bidon-Chanal, A; Luque, FJ 6/19/2008 12/16/2012 Laboratori De Qu�Mica Farmac�Utica (Unitat Associada Al Csic) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50871874 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Bos taurus 167 ChEMBL 10.1021/jm8001313 10.7270/Q2F76DGK 18517184 Camps, P; Formosa, X; Galdeano, C; Gomez, T; Munoz-Torrero, D; Scarpellini, M; Viayna, E; Badia, A; Clos, MV; Camins, A; Pallas, M; Bartolini, M; Mancini, F; Andrisano, V; Estelrich, J; Lizondo, M; Bidon-Chanal, A; Luque, FJ 6/19/2008 12/16/2012 Laboratori De Qu�Mica Farmac�Utica (Unitat Associada Al Csic) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 50873536 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 150 ChEMBL 10.1016/j.bmc.2008.07.005 10.7270/Q2DZ096D 18640842 Leon, R; de los Rios, C; Marco-Contelles, J; Huertas, O; Barril, X; Luque, FJ; Lopez, MG; Garcia, AG; Villarroya, M 8/18/2008 12/17/2012 Laboratorio De Radicales Libres (Iqog, Csic) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50881003 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 300 ChEMBL 10.1016/j.ejmech.2017.02.042 10.7270/Q2P55R0J 28242549 Xia, CL; Wang, N; Guo, QL; Liu, ZQ; Wu, JQ; Huang, SL; Ou, TM; Tan, JH; Wang, HG; Li, D; Huang, ZS 4/21/2017 2/5/2020 Sun Yat-Sen University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50888820 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 600 ChEMBL 10.1016/j.bmc.2017.05.045 10.7270/Q2F76G21 28578994 Shchegol'kov, EV; Makhaeva, GF; Boltneva, NP; Lushchekina, SV; Serebryakova, OG; Rudakova, EV; Kovaleva, NV; Burgart, YV; Saloutin, VI; Chupakhin, ON; Bachurin, SO; Richardson, RJ 8/1/2017 3/2/2020 Urals Branch of Russian Academy of Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50901812 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 270 ChEMBL 10.1021/acs.jnatprod.6b01178 10.7270/Q2WS8WR8 28445039 Guo, Y; Zhang, N; Chen, C; Huang, J; Li, XN; Liu, J; Zhu, H; Tong, Q; Zhang, J; Luo, Z; Xue, Y; Zhang, Y 5/26/2017 4/19/2020 Chinese Academy of Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50908506 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Bos taurus 710 ChEMBL 10.1016/j.bmc.2010.01.074 10.7270/Q2R78G5X 20176490 Geissler, T; Brandt, W; Porzel, A; Schlenzig, D; Kehlen, A; Wessjohann, L; Arnold, N 3/10/2010 12/28/2012 Institute of Plant Biochemistry http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 50913393 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 100 ChEMBL 10.1021/jm901902w 10.7270/Q25T3MFV 20575555 de Los Rios, C; Egea, J; Marco-Contelles, J; Leon, R; Samadi, A; Iriepa, I; Moraleda, I; Galvez, E; Garcia, AG; Lopez, MG; Villarroya, M; Romero, A 7/29/2010 12/31/2012 Universidad Autonoma De Madrid http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50913399 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Bos taurus 27 ChEMBL 10.1021/jm901902w 10.7270/Q25T3MFV 20575555 de Los Rios, C; Egea, J; Marco-Contelles, J; Leon, R; Samadi, A; Iriepa, I; Moraleda, I; Galvez, E; Garcia, AG; Lopez, MG; Villarroya, M; Romero, A 7/29/2010 12/31/2012 Universidad Autonoma De Madrid http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 50925057 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 317 ChEMBL 10.1021/jm200840c 10.7270/Q26974KH 22185619 Galdeano, C; Viayna, E; Sola, I; Formosa, X; Camps, P; Badia, A; Clos, MV; Relat, J; Ratia, M; Bartolini, M; Mancini, F; Andrisano, V; Salmona, M; Minguillon, C; Gonzalez-Munoz, GC; Rodriguez-Franco, MI; Bidon-Chanal, A; Luque, FJ; Munoz-Torrero, D 1/26/2012 2/7/2013 Universitat De Barcelona http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50928265 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 350 ChEMBL 10.1021/jm201460y 10.7270/Q2M32WS2 22243648 Fernandez-Bachiller, MI; Perez, C; Monjas, L; Rademann, J; Rodriguez-Franco, MI 2/9/2012 2/7/2013 IQM-CSIC http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50928270 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Bos taurus 40 ChEMBL 10.1021/jm201460y 10.7270/Q2M32WS2 22243648 Fernandez-Bachiller, MI; Perez, C; Monjas, L; Rademann, J; Rodriguez-Franco, MI 2/9/2012 2/7/2013 IQM-CSIC http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 50931107 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 420 ChEMBL 10.1016/j.ejmech.2012.03.022 10.7270/Q25H7H97 22503231 Samadi, A; de los Rios, C; Bolea, I; Chioua, M; Iriepa, I; Moraleda, I; Bartolini, M; Andrisano, V; Galvez, E; Valderas, C; Unzeta, M; Marco-Contelles, J 4/30/2012 2/7/2013 Laboratorio De Radicales Libres Y Qu�Mica Computacional (Iqog, Csic) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50931207 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Rattus norvegicus 130 ChEMBL 10.1016/j.bmc.2018.04.037 10.7270/Q28P631Z 29729987 Liu, W; Wang, H; Li, X; Xu, Y; Zhang, J; Wang, W; Gong, Q; Qiu, X; Zhu, J; Mao, F; Zhang, H; Li, J 7/23/2018 5/3/2020 East China University of Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50949134 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 101 ChEMBL 10.1016/j.ejmech.2012.06.051 10.7270/Q2HH6M4Z 22818849 Hamulakova, S; Janovec, L; Hrabinova, M; Kristian, P; Kuca, K; Banasova, M; Imrich, J 9/3/2012 2/8/2013 P. J. Safarik University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50949142 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 225 ChEMBL 10.1016/j.ejmech.2012.06.051 10.7270/Q2HH6M4Z 22818849 Hamulakova, S; Janovec, L; Hrabinova, M; Kristian, P; Kuca, K; Banasova, M; Imrich, J 9/3/2012 2/8/2013 P. J. Safarik University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50949158 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 500 ChEMBL 10.1016/j.ejmech.2012.06.051 10.7270/Q2HH6M4Z 22818849 Hamulakova, S; Janovec, L; Hrabinova, M; Kristian, P; Kuca, K; Banasova, M; Imrich, J 9/3/2012 2/8/2013 P. J. Safarik University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50961223 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Mus musculus 130 ChEMBL 10.1016/j.bmc.2012.09.005 10.7270/Q2HT2QFT 23026084 Roy, KK; Tota, S; Tripathi, T; Chander, S; Nath, C; Saxena, AK 10/15/2012 5/17/2013 Csir-Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 50961481 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 32 ChEMBL 10.1016/j.bmc.2012.09.016 10.7270/Q2ZW1N1Z 23041347 Peng, DY; Sun, Q; Zhu, XL; Lin, HY; Chen, Q; Yu, NX; Yang, WC; Yang, GF 10/23/2012 5/17/2013 Central China Normal University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50978634 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 350 ChEMBL 10.1016/j.ejmech.2012.06.038 10.7270/Q2R78GCM 22795665 Maalej, E; Chabchoub, F; Oset-Gasque, MJ; Esquivias-Perez, M; Gonzalez, MP; Monjas, L; Perez, C; de los Rios, C; Rodriguez-Franco, MI; Iriepa, I; Moraleda, I; Chioua, M; Romero, A; Marco-Contelles, J; Samadi, A 7/30/2012 5/17/2013 University of Sfax http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50984020 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 230 ChEMBL 10.1016/j.ejmech.2017.08.051 10.7270/Q2XS5XWN 28863358 Chierrito, TPC; Pedersoli-Mantoani, S; Roca, C; Requena, C; Sebastian-Perez, V; Castillo, WO; Moreira, NCS; Pérez, C; Sakamoto-Hojo, ET; Takahashi, CS; Jiménez-Barbero, J; Cañada, FJ; Campillo, NE; Martinez, A; Carvalho, I 10/20/2017 6/3/2020 University of S£O Paulo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50986001 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 424 ChEMBL 10.1016/j.ejmech.2017.09.022 10.7270/Q27083ZM 29031067 Pandolfi, F; De Vita, D; Bortolami, M; Coluccia, A; Di Santo, R; Costi, R; Andrisano, V; Alabiso, F; Bergamini, C; Fato, R; Bartolini, M; Scipione, L 12/1/2017 6/12/2020 Sapienza University of Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50994358 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 269.77 ChEMBL 10.1021/jm950704x 10.7270/Q25D8T1Q 8558505 Tong, W; Collantes, ER; Chen, Y; Welsh, WJ 2/28/1996 5/20/2013 University of Missouri St. Louis http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50995286 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 76.03 ChEMBL 10.1021/jm970488n 10.7270/Q2BZ6784 9435905 So, SS; Karplus, M 2/13/1998 5/20/2013 Harvard University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51030320 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 430 ChEMBL 10.1016/j.ejmech.2018.01.055 10.7270/Q2M61NST 29407958 Jiang, N; Huang, Q; Liu, J; Liang, N; Li, Q; Li, Q; Xie, SS 2/25/2018 8/6/2020 Jiangxi University of Traditional Chinese Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51033647 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 34 ChEMBL 10.1021/jm049877p 10.7270/Q26974WJ 15317459 Martin-Santamaria, S; Munoz-Muriedas, J; Luque, FJ; Gago, F 8/19/2004 9/23/2013 Universitat De Barcelona http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51033673 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 251 ChEMBL 10.1021/jm049877p 10.7270/Q26974WJ 15317459 Martin-Santamaria, S; Munoz-Muriedas, J; Luque, FJ; Gago, F 8/19/2004 9/23/2013 Universitat De Barcelona http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51038565 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 117 ChEMBL 10.1016/j.ejmech.2018.01.028 10.7270/Q2CF9SQV 29466774 Li, G; Hong, G; Li, X; Zhang, Y; Xu, Z; Mao, L; Feng, X; Liu, T 3/25/2018 8/16/2020 Peking Union Medical College http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51039208 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 100 ChEMBL 10.1016/j.bmc.2012.10.045 10.7270/Q2QV3NTH 23199476 Catto, M; Pisani, L; Leonetti, F; Nicolotti, O; Pesce, P; Stefanachi, A; Cellamare, S; Carotti, A 12/18/2012 9/24/2013 University of Bari Aldo Moro http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51046183 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Rattus norvegicus 249 ChEMBL 10.1016/j.bmc.2012.11.044 10.7270/Q20C4X3F 23273608 Hu, Y; Zhang, J; Chandrashankra, O; Ip, FC; Ip, NY 1/15/2013 9/24/2013 The Hong Kong University of Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 51054065 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Rattus norvegicus 230 ChEMBL 10.1016/j.bmc.2013.01.015 10.7270/Q2GB25C5 23380475 Shi, DH; Huang, W; Li, C; Wang, LT; Wang, SF 2/15/2013 9/24/2013 Hainan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 51057687 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 320 ChEMBL 10.1016/j.ejmech.2018.02.083 10.7270/Q2W95CT0 29533874 Hepnarova, V; Korabecny, J; Matouskova, L; Jost, P; Muckova, L; Hrabinova, M; Vykoukalova, N; Kerhartova, M; Kucera, T; Dolezal, R; Nepovimova, E; Spilovska, K; Mezeiova, E; Pham, NL; Jun, D; Staud, F; Kaping, D; Kuca, K; Soukup, O 4/25/2018 8/16/2020 University of Defence http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51102567 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 374 ChEMBL 10.1016/j.ejmech.2018.06.044 10.7270/Q2WQ06BW 29958119 Chioua, M; Buzzi, E; Moraleda, I; Iriepa, I; Maj, M; Wnorowski, A; Giovannini, C; Tramarin, A; Portali, F; Ismaili, L; López-Alvarado, P; Bolognesi, ML; Jóźwiak, K; Menéndez, JC; Marco-Contelles, J; Bartolini, M 7/15/2018 8/15/2020 Laboratory of Medicinal Chemistry (Iqog, Csic) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51118351 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 77 ChEMBL 10.1016/j.ejmech.2017.09.008 10.7270/Q2VT1VQS 28923380 Ma, F; Du, H 11/10/2017 8/16/2020 Xinyang Normal University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51130787 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 600 ChEMBL 10.1016/j.bmc.2018.08.010 10.7270/Q2RR21X9 30104121 Makhaeva, GF; Boltneva, NP; Lushchekina, SV; Rudakova, EV; Serebryakova, OG; Kulikova, LN; Beloglazkin, AA; Borisov, RS; Richardson, RJ 9/1/2018 8/17/2020 Institute of Physiologically Active Compounds Russian Academy of Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51134350 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 230 ChEMBL 10.1021/acsmedchemlett.7b00463 10.7270/Q2MG7S5F 29541355 Jiang, XY; Chen, TK; Zhou, JT; He, SY; Yang, HY; Chen, Y; Qu, W; Feng, F; Sun, HP 3/8/2018 8/18/2020 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51140794 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 230 ChEMBL 10.1016/j.ejmech.2018.07.056 10.7270/Q2F192DM 30245401 Reis, J; Cagide, F; Valencia, ME; Teixeira, J; Bagetta, D; Pérez, C; Uriarte, E; Oliveira, PJ; Ortuso, F; Alcaro, S; Rodríguez-Franco, MI; Borges, F 10/5/2018 8/18/2020 University of Porto http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51141567 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Mus musculus 34 ChEMBL 10.1016/j.bmc.2018.10.003 10.7270/Q2B56NFD 30340901 Lopes, JPB; Silva, L; da Costa Franarin, G; Antonio Ceschi, M; Seibert Lüdtke, D; Ferreira Dantas, R; de Salles, CMC; Paes Silva-Jr, F; Roberto Senger, M; Alvim Guedes, I; Emmanuel Dardenne, L 11/1/2018 8/18/2020 Universidade Federal Do Rio Grande Do Sul http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 51144121 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 115 ChEMBL 10.1016/j.ejmech.2018.07.033 10.7270/Q27W6FW2 30031971 Knez, D; Coquelle, N; Pišlar, A; Žakelj, S; Jukič, M; Sova, M; Mravljak, J; Nachon, F; Brazzolotto, X; Kos, J; Colletier, JP; Gobec, S 8/5/2018 8/18/2020 University of Ljubljana http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51183384 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 140 ChEMBL 10.1007/s00044-011-9695-0 10.7270/Q2DV1NSH n/a 12/28/2012 8/30/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51195839 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 268 ChEMBL 10.1016/j.bmc.2013.05.001 10.7270/Q2NC645G 23719283 Zhu, J; Wu, CF; Li, X; Wu, GS; Xie, S; Hu, QN; Deng, Z; Zhu, MX; Luo, HR; Hong, X 7/15/2013 9/1/2020 Key Laboratory of Combinatorial Biosynthesis and Drug Discovery (Wuhan University) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51196253 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 160 ChEMBL 10.1016/j.bmcl.2013.05.092 10.7270/Q2JD50Q1 23791077 Mohamed, T; Osman, W; Tin, G; Rao, PP 8/1/2013 9/1/2020 University of Waterloo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51201815 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 383 ChEMBL 10.1016/j.bmcl.2013.09.091 10.7270/Q22F7RDV 24140444 Prati, F; Bartolini, M; Simoni, E; De Simone, A; Pinto, A; Andrisano, V; Bolognesi, ML 12/1/2013 9/1/2020 Alma Mater Studiorum University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51210455 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 285 ChEMBL 10.1016/j.ejmech.2014.09.081 10.7270/Q2CF9T2R 25282266 Huang, L; Miao, H; Sun, Y; Meng, F; Li, X 11/24/2014 9/3/2020 Sun Yat-Sen University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51218669 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 79 ChEMBL 10.1016/j.bmc.2016.01.031 10.7270/Q2B85C4Q 26827140 Makhaeva, GF; Boltneva, NP; Lushchekina, SV; Serebryakova, OG; Stupina, TS; Terentiev, AA; Serkov, IV; Proshin, AN; Bachurin, SO; Richardson, RJ 3/1/2016 9/4/2020 Institute of Physiologically Active Compounds Russian Academy of Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51218781 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 330 ChEMBL 10.1021/acs.jnatprod.5b00830 10.7270/Q2T72MFH 26583263 Zhang, JJ; Yang, XW; Liu, X; Ma, JZ; Liao, Y; Xu, G 12/24/2015 9/4/2020 Chinese Academy of Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51227575 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 300 ChEMBL 10.1016/j.bmc.2018.12.023 10.7270/Q2SF30F6 30579802 Feng, L; Zhang, Y; Liu, YC; Liu, Y; Luo, SH; Huang, CS; Li, SH 1/15/2019 2/18/2021 Chinese Academy of Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51245811 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 412 ChEMBL 10.1016/j.ejmech.2019.02.012 10.7270/Q2V69NVX 30771604 AlFadly, ED; Elzahhar, PA; Tramarin, A; Elkazaz, S; Shaltout, H; Abu-Serie, MM; Janockova, J; Soukup, O; Ghareeb, DA; El-Yazbi, AF; Rafeh, RW; Bakkar, NZ; Kobeissy, F; Iriepa, I; Moraleda, I; Saudi, MNS; Bartolini, M; Belal, ASF 4/1/2019 2/20/2021 Alexandria University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51247193 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 400 ChEMBL 10.1016/j.ejmech.2019.02.008 10.7270/Q2B27ZK8 30771601 Fang, Y; Zhou, H; Gu, Q; Xu, J 4/1/2019 2/20/2021 Sun Yat-Sen University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51248654 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 30 ChEMBL 10.1016/j.bmc.2019.01.025 10.7270/Q2N87F3N 30744931 Mishra, P; Kumar, A; Panda, G 3/15/2019 2/20/2021 Csir-Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51248658 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Rattus norvegicus 590 ChEMBL 10.1016/j.bmc.2019.01.025 10.7270/Q2N87F3N 30744931 Mishra, P; Kumar, A; Panda, G 3/15/2019 2/20/2021 Csir-Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 51248770 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 500 ChEMBL 10.1016/j.bmc.2019.01.025 10.7270/Q2N87F3N 30744931 Mishra, P; Kumar, A; Panda, G 3/15/2019 2/20/2021 Csir-Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51248801 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Rattus norvegicus 131 ChEMBL 10.1016/j.bmc.2019.01.025 10.7270/Q2N87F3N 30744931 Mishra, P; Kumar, A; Panda, G 3/15/2019 2/20/2021 Csir-Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 51257176 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 426 ChEMBL 10.1016/j.bmc.2019.07.050 10.7270/Q28W3HMG 31401008 Sangshetti, J; Pathan, SK; Patil, R; Akber Ansari, S; Chhajed, S; Arote, R; Shinde, DB 9/15/2019 2/21/2021 Y. B. Chavan College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51257752 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 158 ChEMBL 10.1021/acs.jmedchem.9b00623 10.7270/Q20G3PHK 31609608 Scheiner, M; Dolles, D; Gunesch, S; Hoffmann, M; Nabissi, M; Marinelli, O; Naldi, M; Bartolini, M; Petralla, S; Poeta, E; Monti, B; Falkeis, C; Vieth, M; Hübner, H; Gmeiner, P; Maitra, R; Maurice, T; Decker, M 10/24/2019 2/21/2021 Julius Maximilian University of W£Rzburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51257787 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 13 ChEMBL 10.1021/acs.jmedchem.9b00623 10.7270/Q20G3PHK 31609608 Scheiner, M; Dolles, D; Gunesch, S; Hoffmann, M; Nabissi, M; Marinelli, O; Naldi, M; Bartolini, M; Petralla, S; Poeta, E; Monti, B; Falkeis, C; Vieth, M; Hübner, H; Gmeiner, P; Maitra, R; Maurice, T; Decker, M 10/24/2019 2/21/2021 Julius Maximilian University of W£Rzburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51261701 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 412 ChEMBL 10.1016/j.ejmech.2019.07.053 10.7270/Q23R0X60 31376562 Roldán-Peña, JM; Romero-Real, V; Hicke, J; Maya, I; Franconetti, A; Lagunes, I; Padrón, JM; Petralla, S; Poeta, E; Naldi, M; Bartolini, M; Monti, B; Bolognesi, ML; López, Ó; Fernández-Bolaños, JG 11/1/2019 2/21/2021 Universidad De Sevilla http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51271843 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 131 ChEMBL 10.1016/j.ejmech.2019.111785 10.7270/Q2Q81HF9 31669851 Bajda, M; Łażewska, D; Godyń, J; Zaręba, P; Kuder, K; Hagenow, S; Łątka, K; Stawarska, E; Stark, H; Kieć-Kononowicz, K; Malawska, B 1/1/2020 2/23/2021 Jagiellonian University Medical College http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51282972 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 424 ChEMBL 10.1016/j.ejmech.2018.12.063 10.7270/Q2J969S0 30798053 Oukoloff, K; Coquelle, N; Bartolini, M; Naldi, M; Le Guevel, R; Bach, S; Josselin, B; Ruchaud, S; Catto, M; Pisani, L; Denora, N; Iacobazzi, RM; Silman, I; Sussman, JL; Buron, F; Colletier, JP; Jean, L; Routier, S; Renard, PY 4/15/2019 2/24/2021 Cnrs http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51283288 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 320 ChEMBL 10.1016/j.ejmech.2019.02.021 10.7270/Q2RV0S3X 30851693 Chalupova, K; Korabecny, J; Bartolini, M; Monti, B; Lamba, D; Caliandro, R; Pesaresi, A; Brazzolotto, X; Gastellier, AJ; Nachon, F; Pejchal, J; Jarosova, M; Hepnarova, V; Jun, D; Hrabinova, M; Dolezal, R; Zdarova Karasova, J; Mzik, M; Kristofikova, Z; Misik, J; Muckova, L; Jost, P; Soukup, O; Benkova, M; Setnicka, V; Habartova, L; Chvojkova, M; Kleteckova, L; Vales, K; Mezeiova, E; Uliassi, E; Valis, M; Nepovimova, E; Bolognesi, ML; Kuca, K 4/15/2019 2/24/2021 University of Hradec Kralove http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51297462 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 55 ChEMBL 10.1016/j.ejmech.2019.111651 10.7270/Q2ZP49K2 31479975 Mahmoud, WR; Nissan, YM; Elsawah, MM; Refaey, RH; Ragab, MF; Amin, KM 11/15/2019 2/25/2021 Cairo University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51298839 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 79 ChEMBL 10.1016/j.bmcl.2019.126754 10.7270/Q2K93C0P 31708262 Williams, A; Zhou, S; Zhan, CG 12/15/2019 2/25/2021 University of Kentucky http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51324252 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 50 ChEMBL 10.1021/acs.jmedchem.6b00426 10.7270/Q2SJ1Q44 27253679 Shidore, M; Machhi, J; Shingala, K; Murumkar, P; Sharma, MK; Agrawal, N; Tripathi, A; Parikh, Z; Pillai, P; Yadav, MR 6/23/2016 2/28/2021 The Maharaja Sayajirao University of Baroda http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51334438 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Bos taurus 180 ChEMBL 10.1016/j.ejmech.2019.02.005 10.7270/Q23N26XF 30739821 de Los Ríos, C; Marco-Contelles, J 3/15/2019 8/12/2021 Hospital Universitario De La Princesa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 51348084 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 100 ChEMBL 10.1016/j.bmcl.2020.127075 10.7270/Q22V2KQ2 32165042 Joubert, J; Kapp, E 5/1/2020 8/14/2021 University of The Western Cape http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51350551 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Rattus norvegicus 600 ChEMBL 10.1021/acs.jmedchem.0c00242 10.7270/Q2KD22HB 32539387 Bancet, A; Raingeval, C; Lomberget, T; Le Borgne, M; Guichou, JF; Krimm, I 10/22/2020 3/21/2022 University of Lyon http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 51356864 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 480 ChEMBL 10.1016/j.bmc.2020.115820 10.7270/Q2WW7N96 33120080 Lin, SX; Curtis, MA; Sperry, J 12/15/2020 3/22/2022 University of Auckland http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51356979 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Rattus norvegicus 93 ChEMBL 10.1016/j.bmc.2020.115820 10.7270/Q2WW7N96 33120080 Lin, SX; Curtis, MA; Sperry, J 12/15/2020 3/22/2022 University of Auckland http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 51361358 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 420 ChEMBL 10.1021/acs.jmedchem.6b01178 10.7270/Q2WH2TMM 27736061 Benchekroun, M; Romero, A; Egea, J; León, R; Michalska, P; Buendía, I; Jimeno, ML; Jun, D; Janockova, J; Sepsova, V; Soukup, O; Bautista-Aguilera, OM; Refouvelet, B; Ouari, O; Marco-Contelles, J; Ismaili, L 11/10/2016 3/23/2022 UBFC http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51366749 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 190 ChEMBL 10.1016/j.bmc.2020.115940 10.7270/Q20K2D6W 33340937 Jiang, X; Wang, Y; Liu, C; Xing, C; Wang, Y; Lyu, W; Wang, S; Li, Q; Chen, T; Chen, Y; Feng, F; Liu, W; Sun, H 1/15/2021 3/24/2022 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51368949 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Rattus norvegicus 170 ChEMBL 10.1016/j.bmcl.2020.127498 10.7270/Q2K35Z9F 32818604 Marco, JL 11/1/2020 3/25/2022 Csic http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 51370997 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 84 ChEMBL 10.1016/j.bmcl.2020.127609 10.7270/Q23R0XH1 33039562 Miles, JA; Kapure, JS; Deora, GS; Courageux, C; Igert, A; Dias, J; McGeary, RP; Brazzolotto, X; Ross, BP 12/15/2020 3/25/2022 The University of Queensland http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51371626 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 72 ChEMBL 10.1016/j.bmcl.2020.127659 10.7270/Q28919H1 33137375 Du, H; Jiang, X; Ma, M; Xu, H; Liu, S; Ma, F 12/15/2020 3/25/2022 Xinyang Normal University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51375492 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 131 ChEMBL 10.1016/j.ejmech.2020.112743 10.7270/Q2P272S9 32882609 Łażewska, D; Bajda, M; Kaleta, M; Zaręba, P; Doroz-Płonka, A; Siwek, A; Alachkar, A; Mogilski, S; Saad, A; Kuder, K; Olejarz-Maciej, A; Godyń, J; Stary, D; Sudoł, S; Więcek, M; Latacz, G; Walczak, M; Handzlik, J; Sadek, B; Malawska, B; Kieć-Kononowicz, K 12/1/2020 3/26/2022 Jagiellonian University Medical College http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51376179 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 172 ChEMBL 10.1016/j.ejmech.2020.112751 10.7270/Q2TQ656B 32950908 Jiang, X; Zhou, J; Wang, Y; Chen, L; Duan, Y; Huang, J; Liu, C; Chen, Y; Liu, W; Sun, H; Feng, F; Qu, W 12/1/2020 3/26/2022 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51386448 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 320 ChEMBL 10.1021/acs.jmedchem.0c00528 10.7270/Q23N2733 32706255 Pérez-Areales, FJ; Garrido, M; Aso, E; Bartolini, M; De Simone, A; Espargaró, A; Ginex, T; Sabate, R; Pérez, B; Andrisano, V; Puigoriol-Illamola, D; Pallàs, M; Luque, FJ; Loza, MI; Brea, J; Ferrer, I; Ciruela, F; Messeguer, A; Muñoz-Torrero, D 9/10/2020 3/28/2022 University of Barcelona (Ub) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51398105 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 250 ChEMBL 10.1016/j.ejmech.2020.112415 10.7270/Q27P9344 32454229 Zhou, B; Li, H; Cui, Z; Li, D; Geng, H; Gao, J; Zhou, L 8/15/2020 3/29/2022 Northwest A&F University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51410368 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 320 ChEMBL 10.1016/j.ejmech.2021.113434 10.7270/Q2PC365G 33892271 Gorecki, L; Misiachna, A; Damborsky, J; Dolezal, R; Korabecny, J; Cejkova, L; Hakenova, K; Chvojkova, M; Karasova, JZ; Prchal, L; Novak, M; Kolcheva, M; Kortus, S; Vales, K; Horak, M; Soukup, O 7/5/2021 8/20/2022 University Hospital Hradec Kralove http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51414161 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 320 ChEMBL 10.1016/j.bmcl.2021.128100 10.7270/Q2WD44BG 33984470 Mezeiova, E; Hrabinova, M; Hepnarova, V; Jun, D; Janockova, J; Muckova, L; Prchal, L; Kristofikova, Z; Kucera, T; Gorecki, L; Chalupova, K; Kunes, J; Hroudova, J; Soukup, O; Korabecny, J 7/1/2021 8/20/2022 University Hospital Hradec Kralove http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51436909 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Mus musculus 200 ChEMBL 10.1021/acs.jmedchem.1c00160 10.7270/Q2FR01GX 34024109 Yao, H; Uras, G; Zhang, P; Xu, S; Yin, Y; Liu, J; Qin, S; Li, X; Allen, S; Bai, R; Gong, Q; Zhang, H; Zhu, Z; Xu, J 6/10/2021 3/5/2023 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 51437535 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 111 ChEMBL 10.1021/acs.jmedchem.1c00534 10.7270/Q29027NK 34152756 Scheiner, M; Hoffmann, M; He, F; Poeta, E; Chatonnet, A; Monti, B; Maurice, T; Decker, M 7/8/2021 3/5/2023 Julius Maximilian University of W£Rzburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51437536 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 110 ChEMBL 10.1021/acs.jmedchem.1c00534 10.7270/Q29027NK 34152756 Scheiner, M; Hoffmann, M; He, F; Poeta, E; Chatonnet, A; Monti, B; Maurice, T; Decker, M 7/8/2021 3/5/2023 Julius Maximilian University of W£Rzburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51440963 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Rattus norvegicus 237 ChEMBL 10.1016/j.ejmech.2021.113827 10.7270/Q2222ZP7 34530383 Ip, FCF; Fu, G; Yang, F; Kang, F; Sun, P; Ling, CY; Cheung, K; Xie, F; Hu, Y; Fu, L; Ip, NY 12/15/2021 3/5/2023 The Hong Kong University of Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 51454048 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 230 ChEMBL 10.1021/acs.jmedchem.1c00048 10.7270/Q24F1VNK 33829779 Rossi, M; Freschi, M; de Camargo Nascente, L; Salerno, A; de Melo Viana Teixeira, S; Nachon, F; Chantegreil, F; Soukup, O; Prchal, L; Malaguti, M; Bergamini, C; Bartolini, M; Angeloni, C; Hrelia, S; Soares Romeiro, LA; Bolognesi, ML 4/22/2021 3/7/2023 Alma Mater Studiorum - University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51455607 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 230 ChEMBL 10.7270/Q2CF9V25 33346659 De Simone, A; Tumiatti, V; Andrisano, V; Milelli, A 1/14/2021 6/18/2023 University of Turin http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51460756 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 93 ChEMBL 10.7270/Q2BV7MK2 35923722 Paolino, M; Rullo, M; Maramai, S; de Candia, M; Pisani, L; Catto, M; Mugnaini, C; Brizzi, A; Cappelli, A; Olivucci, M; Corelli, F; Altomare, CD 7/20/2022 6/18/2023 Universit� http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51462464 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 178 ChEMBL 10.7270/Q2J67MWD 36561075 Machado, V; Cenci, AR; Teixeira, KF; Sens, L; Tizziani, T; Nunes, RJ; Ferreira, LLG; Yunes, RA; Sandjo, LP; Andricopulo, AD; de Oliveira, AS 12/14/2022 6/19/2023 Federal University of Santa Catarina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51464275 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 188 ChEMBL 10.7270/Q2W66QRK 36092149 Spatz, P; Zimmermann, T; Steinmüller, S; Hofmann, J; Maurice, T; Decker, M 8/17/2022 6/19/2023 Julius Maximilian University of W�Rzburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51464282 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 200 ChEMBL 10.7270/Q2W66QRK 36092149 Spatz, P; Zimmermann, T; Steinmüller, S; Hofmann, J; Maurice, T; Decker, M 8/17/2022 6/19/2023 Julius Maximilian University of W�Rzburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51472940 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 270 ChEMBL 10.7270/Q2XW4PTH 35658485 Li, C; Shao, Y; Li, W; Yin, T; Li, H; Yan, H; Guo, X; Liu, B; He, B 6/24/2022 6/21/2023 Kunming Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51475822 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 110 ChEMBL 10.7270/Q2445RHZ 35276424 Fantacuzzi, M; Amoroso, R; Carradori, S; De Filippis, B 4/5/2022 6/21/2023 "G. D'Annunzio" University of Chieti-Pescara http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51483470 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 32 ChEMBL 10.7270/Q2BP06TV 34743062 Sheng, K; Song, Y; Lei, F; Zhao, W; Fan, L; Wu, L; Liu, Y; Wu, S; Zhang, Y 1/5/2022 6/22/2023 Northwest University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51489513 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 117000 ChEMBL 10.7270/Q2N58RF6 35395370 İmamoğlu, R; Koç, E; Kısa, D 6/1/2022 6/23/2023 Bartin University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51493982 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 412 ChEMBL 10.7270/Q2TB1BZK 34619465 Li, Y; Sang, S; Ren, W; Pei, Y; Bian, Y; Chen, Y; Sun, H 12/15/2021 6/24/2023 Nanjing University of Chinese Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51497995 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 99 ChEMBL 10.7270/Q2445RKV 35101650 Waly, OM; Saad, KM; El-Subbagh, HI; Bayomi, SM; Ghaly, MA 3/5/2022 6/24/2023 Mansoura University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51506728 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 1180 ChEMBL 10.7270/Q241724G 36179486 Hitge, R; Petzer, A; Petzer, JP 11/1/2022 6/26/2023 North-West University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51510855 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Mus musculus 34 ChEMBL 10.7270/Q2XS60M8 35028560 Lopes, JPB; Silva, L; Lüdtke, DS 12/15/2021 4/19/2024 Universidade Federal Do Rio Grande Do Sul Av. Bento http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 51521398 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 148 ChEMBL 10.7270/Q2BP071Z 36223681 Wang, Y; Xiong, B; Lin, H; Li, Q; Yang, H; Qiao, Y; Li, Q; Xu, Z; Lyu, W; Qu, W; Liu, W; Chen, Y; Feng, F; Sun, H 12/15/2022 4/21/2024 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51530446 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 43 ChEMBL 10.7270/Q2T72NQH 32795767 Nehra, B; Rulhania, S; Jaswal, S; Kumar, B; Singh, G; Monga, V 11/1/2020 4/23/2024 Isf College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51530455 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 23 ChEMBL 10.7270/Q2T72NQH 32795767 Nehra, B; Rulhania, S; Jaswal, S; Kumar, B; Singh, G; Monga, V 11/1/2020 4/23/2024 Isf College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51530503 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 283 ChEMBL 10.7270/Q2T72NQH 32795767 Nehra, B; Rulhania, S; Jaswal, S; Kumar, B; Singh, G; Monga, V 11/1/2020 4/23/2024 Isf College of Pharmacy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51538801 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 415 ChEMBL 10.7270/Q2SN0FB5 37487339 Uliassi, E; Bergamini, C; Rizzardi, N; Naldi, M; Cores, Á; Bartolini, M; Carlos Menéndez, J; Bolognesi, ML 8/15/2023 12/14/2024 Alma Mater Studiorum - University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51546069 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 152 ChEMBL 10.7270/Q2G44VP5 37127287 Spatz, P; Steinmüller, SAM; Tutov, A; Poeta, E; Morilleau, A; Carles, A; Deventer, MH; Hofmann, J; Stove, CP; Monti, B; Maurice, T; Decker, M 5/11/2023 12/16/2024 Julius Maximilian University Wuerzburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51548105 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 170 ChEMBL 10.7270/Q20R9TSV 35987018 Guo, J; Cheng, M; Liu, P; Cao, D; Luo, J; Wan, Y; Fang, Y; Jin, Y; Xie, SS; Liu, J 11/15/2022 12/17/2024 Jiangxi University of Chinese Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51597708 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 320 ChEMBL 10.7270/Q2FJ2NFM 38218127 Misiachna, A; Svobodova, B; Netolicky, J; Chvojkova, M; Kleteckova, L; Prchal, L; Novak, M; Hrabinova, M; Kucera, T; Muckova, L; Moravcova, Z; Karasova, JZ; Pejchal, J; Blazek, F; Malinak, D; Hakenova, K; Krausova, BH; Kolcheva, M; Ladislav, M; Korabecny, J; Pahnke, J; Vales, K; Horak, M; Soukup, O //0 10/12/2025 Charles University in Prague http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51604078 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 160 ChEMBL 10.7270/Q24172RJ 38852337 Sun, T; Zhen, T; Harakandi, CH; Wang, L; Guo, H; Chen, Y; Sun, H //0 10/12/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51605713 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 8961 CHEMBL95::Cognex::cid_1935::CHEMBL1337960::1,2,3,4-tetrahydroacridin-9-amine::Tracine::tacrine.HCl::9-THA::1,2,3,4-tetrahydro-9-acridinamine::9-amino-1,2,3,4-tetrahydroacridine (THA)::Tacrine::US8999994, Tacrine Acetylcholinesterase Homo sapiens 412 ChEMBL 10.7270/Q2NP2937 39283654 Nocentini, A; Costa, A; Bonardi, A; Ammara, A; Giovannuzzi, S; Petreni, A; Bartolucci, G; Rani, B; Leri, M; Bucciantini, M; Fernández-Bolaños, JG; López, Ó; Passani, MB; Provensi, G; Gratteri, P; Supuran, CT //0 10/12/2025 University of Florence http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8961 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8961&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46509736 CHEMBL1337960CHEMBL95 DB00382 C01453 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51590693 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 10591 tacrine.HCl Acetylcholinesterase Homo sapiens 306 ChEMBL 10.7270/Q28W3JZC 38157596 Liu, Y; Ma, C; Li, Y; Li, M; Cui, T; Zhao, X; Li, Z; Jia, H; Wang, H; Xiu, X; Hu, D; Zhang, R; Wang, N; Liu, P; Yang, H; Cheng, M //0 10/11/2025 Shenyang Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10591 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10591&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46511194 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51600981 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 10591 tacrine.HCl Acetylcholinesterase Homo sapiens 109 ChEMBL 10.7270/Q23N2822 38820854 La Spada, G; Miniero, DV; Rullo, M; Cipolloni, M; Delre, P; Colliva, C; Colella, M; Leonetti, F; Liuzzi, GM; Mangiatordi, GF; Giacchè, N; Pisani, L //0 10/12/2025 University of Bari Aldo Moro http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10591 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10591&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 46511194 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51577264 c1ccc2c(c1)c(c3c(n2)CCCC3)N InChI=1S/C13H14N2/c14-13-9-5-1-3-7-11(9)15-12-8-4-2-6-10(12)13/h1,3,5,7H,2,4,6,8H2,(H2,14,15) YLJREFDVOIBQDA-UHFFFAOYSA-N 50433314 [14C]-Tacrine Monohydrate Monohydrochloride::CHEMBL1337960 Acetylcholinesterase Homo sapiens 90 ChEMBL 10.7270/Q2NZ8D79 38579622 Samarelli, F; Purgatorio, R; Lopopolo, G; Deruvo, C; Catto, M; Andresini, M; Carrieri, A; Nicolotti, O; De Palma, A; Miniero, DV; de Candia, M; Altomare, CD //0 10/11/2025 University of Bari Aldo Moro http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50433314 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50433314&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search THA 1ACJ,1MX1,2AOW,2AOX,4BDS,7XN1,8T5G 1935 175445631 CHEMBL1337960 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51451288 CC1=C(C(=O)Oc2c1ccc(c2)OCC3CCN(CC3)Cc4ccccc4)C InChI=1S/C24H27NO3/c1-17-18(2)24(26)28-23-14-21(8-9-22(17)23)27-16-20-10-12-25(13-11-20)15-19-6-4-3-5-7-19/h3-9,14,20H,10-13,15-16H2,1-2H3 MWFBGTXYOJLQIW-UHFFFAOYSA-N 50585931 CHEMBL4598256 Acetylcholinesterase Homo sapiens 380 ChEMBL 10.1021/acs.jmedchem.1c01784 10.7270/Q2BG2SWG 35195417 Rullo, M; Cipolloni, M; Catto, M; Colliva, C; Miniero, DV; Latronico, T; de Candia, M; Benicchi, T; Linusson, A; Giacchè, N; Altomare, CD; Pisani, L 3/10/2022 3/7/2023 University of Bari "Aldo Moro http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50585931 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50585931&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search AJ9 7QB4 155535905 476022018 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51451283 CN(Cc1ccccc1)Cc2ccc(cc2)COc3ccc4c(c3)OC(=O)C=C4CO InChI=1S/C26H25NO4/c1-27(15-19-5-3-2-4-6-19)16-20-7-9-21(10-8-20)18-30-23-11-12-24-22(17-28)13-26(29)31-25(24)14-23/h2-14,28H,15-18H2,1H3 RTJRBYKZQSYWCM-UHFFFAOYSA-N 50585930 CHEMBL3586771 Acetylcholinesterase Homo sapiens 120 ChEMBL 10.1021/acs.jmedchem.1c01784 10.7270/Q2BG2SWG 35195417 Rullo, M; Cipolloni, M; Catto, M; Colliva, C; Miniero, DV; Latronico, T; de Candia, M; Benicchi, T; Linusson, A; Giacchè, N; Altomare, CD; Pisani, L 3/10/2022 3/7/2023 University of Bari "Aldo Moro http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50585930 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50585930&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search 5IK 7P4F,7QAK 122180463 476022017 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51600967 CN(Cc1ccccc1)Cc2ccc(cc2)COc3ccc4c(c3)OC(=O)C=C4CO InChI=1S/C26H25NO4/c1-27(15-19-5-3-2-4-6-19)16-20-7-9-21(10-8-20)18-30-23-11-12-24-22(17-28)13-26(29)31-25(24)14-23/h2-14,28H,15-18H2,1H3 RTJRBYKZQSYWCM-UHFFFAOYSA-N 50585930 CHEMBL3586771 Acetylcholinesterase Homo sapiens 120 ChEMBL 10.7270/Q23N2822 38820854 La Spada, G; Miniero, DV; Rullo, M; Cipolloni, M; Delre, P; Colliva, C; Colella, M; Leonetti, F; Liuzzi, GM; Mangiatordi, GF; Giacchè, N; Pisani, L //0 10/12/2025 University of Bari Aldo Moro http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50585930 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50585930&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search 5IK 7P4F,7QAK 122180463 476022017 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 15299 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 2.9 8.0000 25.00 C Curated from the literature by BindingDB 10.1021/jm049510k 10.7270/Q27P8WMJ 15771436 aid1796269 Campiani, G; Fattorusso, C; Butini, S; Gaeta, A; Agnusdei, M; Gemma, S; Persico, M; Catalanotti, B; Savini, L; Nacci, V; Novellino, E; Holloway, HW; Greig, NH; Belinskaya, T; Fedorko, JM; Saxena, A 3/24/2005 5/2/2006 Universita Di Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 15518 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Bos taurus 19 8.0000 30.00 C Curated from the literature by BindingDB 10.1016/j.bmc.2005.09.029 10.7270/Q2G73BW9 16230018 aid1796282 Alonso, D; Dorronsoro, I; Rubio, L; Munoz, P; Garcia-Palomero, E; Del Monte, M; Bidon-Chanal, A; Orozco, M; Luque, FJ; Castro, A; Medina, M; Martinez, A 12/15/2005 5/8/2006 Neuropharma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 17743 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 22 Curated from the literature by BindingDB 10.1021/jm050578p 10.7270/Q2S75DJ6 16570913 aid1796482 Luo, W; Yu, QS; Kulkarni, SS; Parrish, DA; Holloway, HW; Tweedie, D; Shafferman, A; Lahiri, DK; Brossi, A; Greig, NH 4/6/2006 8/13/2006 National Institutes of Health http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 18638 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 20.5 23.1 8.0000 37.00 C Curated from the literature by BindingDB 10.1021/jm0340602 10.7270/Q29Z9332 12773032 aid1796570 Piazzi, L; Rampa, A; Bisi, A; Gobbi, S; Belluti, F; Cavalli, A; Bartolini, M; Andrisano, V; Valenti, P; Recanatini, M 6/5/2003 9/12/2006 University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 18676 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 22 8.0000 37.00 C Curated from the literature by BindingDB 10.1021/jm010491d 10.7270/Q22J6933 12166941 aid1796572 Yu, QS; Zhu, X; Holloway, HW; Whittaker, NF; Brossi, A; Greig, NH 8/15/2002 9/12/2006 National Institutes of Health http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 200777 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 26 Curated from the literature by BindingDB 10.1111/j.1747-0285.2012.01435.x 10.7270/Q28P5Z3T 22726458 aid1799797 Raza, R; Saeed, A; Arif, M; Mahmood, S; Muddassar, M; Raza, A; Iqbal, J 10/28/2012 10/29/2012 Comsats Institute of Information Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 293169 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 23 8.0000 25.00 C Curated from the literature by BindingDB 10.1016/j.bioorg.2015.05.005 10.7270/Q2WS8S05 26042530 aid1801052 Kanhed, AM; Sinha, A; Machhi, J; Tripathi, A; Parikh, ZS; Pillai, PP; Giridhar, R; Yadav, MR 8/28/2015 9/8/2015 The M. S. University of Baroda http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 344013 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 1e+1 8.0000 25.00 C Curated from the literature by BindingDB 10.1016/j.bioorg.2016.05.002 10.7270/Q2P849PS 27231830 aid1801892 Chigurupati, S; Selvaraj, M; Mani, V; Selvarajan, KK; Mohammad, JI; Kaveti, B; Bera, H; Palanimuthu, VR; Teh, LK; Salleh, MZ 8/28/2016 9/8/2016 Aimst University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 354300 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 4e+1 8.0000 25.00 C Curated from the literature by BindingDB 10.1111/cbdd.12800 10.7270/Q26D5RSX 27282589 aid1802080 Osman, W; Mohamed, T; Sit, VM; Vasefi, MS; Beazely, MA; Rao, PP 11/28/2016 11/4/2016 University of Waterloo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 393850 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 6.16 8.0000 25.00 C Curated from the literature by BindingDB 10.7270/Q2JM28HK aid1802741 Ozadali-Sari, K; Küçükkilinç, TT; Ayazgok, B; Balkan, A; Unsal-Tan, O 5/2/2017 5/9/2017 Hacettepe University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 404157 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Mus musculus 94 US Patent 10.7270/Q2WD3ZFC aid1802876 US9346818 Bai, H; Zhao, X; Zhong, J; Gong, Y; Zhu, Q; Liu, X; Zheng, X; Liu, L 5/24/2016 6/5/2017 Zhejiang Hisun Pharmaceutical http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 560596 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 8.00 US Patent 10.7270/Q24Q7X1C aid1795926 US9586925 Gulcan, HO; Unlu, S; Esiringu, I; Sahin, Y; Ercetin, T; Oz, D; Sahin, F 3/7/2017 3/2/2019 Nobel IlaÇ http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 643512 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 11.0 US Patent 10.7270/Q23J3G2W aid1796792 US9663465 Dallemagne, P; Rochais, C; Lecoutey, C; Boulouard, M; Freret, T 5/30/2017 6/3/2019 Universite De Caen http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50008786 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Bos taurus 8 ChEMBL 10.1016/s0960-894x(98)00076-6 10.7270/Q2S181N2 9871563 Perola, E; Cellai, L; Brufani, M 1/26/1999 11/10/2009 Istituto Di Strutturistica Chimica G. Giacomello http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 50008802 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Bos taurus 6 ChEMBL 10.1016/s0960-894x(98)00076-6 10.7270/Q2S181N2 9871563 Perola, E; Cellai, L; Brufani, M 1/26/1999 11/10/2009 Istituto Di Strutturistica Chimica G. Giacomello http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 50017164 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 18 ChEMBL 10.1016/s0960-894x(02)00482-1 10.7270/Q2CZ37Q4 12182861 Clark, JK; Cowley, P; Muir, AW; Palin, R; Pow, E; Prosser, AB; Taylor, R; Zhang, MQ 8/16/2002 10/5/2012 Organon Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50049157 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 1.7 ChEMBL 10.1021/jm00015a020 10.7270/Q22B8X2S 7636858 Vidaluc, JL; Calmel, F; Bigg, DC; Carilla, E; Briley, M 9/12/1995 11/10/2009 Centre De Recherche Pierre Fabre http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50062419 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 8 ChEMBL 10.1021/jm00043a012 10.7270/Q2VT1R4X 8064800 Villalobos, A; Blake, JF; Biggers, CK; Butler, TW; Chapin, DS; Chen, YL; Ives, JL; Jones, SB; Liston, DR; Nagel, AA 9/22/1994 11/10/2009 Pfizer http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50109206 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 62 ChEMBL 10.1016/j.ejmech.2014.06.034 10.7270/Q2862J10 24980117 Bukhari, SN; Jantan, I; Masand, VH; Mahajan, DT; Sher, M; Naeem-ul-Hassan, M; Amjad, MW 7/28/2014 2/12/2015 Universiti Kebangsaan Malaysia http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50119526 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 8 ChEMBL 10.1016/s0960-894x(98)00076-6 10.7270/Q2S181N2 9871563 Perola, E; Cellai, L; Brufani, M 1/26/1999 11/10/2009 Istituto Di Strutturistica Chimica G. Giacomello http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50147135 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 20 ChEMBL 10.1016/s0960-894x(99)00597-1 10.7270/Q2ZP45B8 10612585 Zeng, F; Jiang, H; Zhai, Y; Zhang, H; Chen, K; Ji, R 1/13/2000 11/10/2009 Institute of Materia Medica http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50164264 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 21 ChEMBL 10.1021/jm100293f 10.7270/Q2B56JXF 20420456 Melchiorre, C; Bolognesi, ML; Minarini, A; Rosini, M; Tumiatti, V 8/19/2010 3/19/2011 University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50192953 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 40 ChEMBL 10.1021/jm0109356 10.7270/Q298869Q 11689088 Andreani, A; Cavalli, A; Granaiola, M; Guardigli, M; Leoni, A; Locatelli, A; Morigi, R; Rambaldi, M; Recanatini, M; Roda, A 11/5/2001 11/10/2009 Università http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50233737 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 8.0 ChEMBL 10.1016/j.bmc.2014.08.016 10.7270/Q2WH2RKB 25189690 Gulcan, HO; Unlu, S; Esiringu, I; Ercetin, T; Sahin, Y; Oz, D; Sahin, MF 9/22/2014 3/6/2016 Eastern Mediterranean University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50253247 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 20 ChEMBL 10.1021/np500558b 10.7270/Q2Z32183 25455147 Kim, H; Yang, I; Patil, RS; Kang, S; Lee, J; Choi, H; Kim, MS; Nam, SJ; Kang, H 12/26/2014 3/15/2016 Seoul National University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50289511 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 20.5 ChEMBL 10.1021/jm0494366 10.7270/Q2JD4W91 15588084 Tumiatti, V; Andrisano, V; Banzi, R; Bartolini, M; Minarini, A; Rosini, M; Melchiorre, C 12/13/2004 11/10/2009 University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50301298 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 6.0 ChEMBL 10.1016/j.bmc.2015.01.045 10.7270/Q2PN979Q 25707322 Guzior, N; Bajda, M; Rakoczy, J; Brus, B; Gobec, S; Malawska, B 3/17/2015 4/9/2016 Jagiellonian University Medical College http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50309213 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 16 ChEMBL 10.1021/jm501501a 10.7270/Q2WS8VX3 25418133 Bautista-Aguilera, OM; Samadi, A; Chioua, M; Nikolic, K; Filipic, S; Agbaba, D; Soriano, E; de Andrés, L; Rodríguez-Franco, MI; Alcaro, S; Ramsay, RR; Ortuso, F; Yañez, M; Marco-Contelles, J 12/29/2014 4/15/2016 Laboratorio De Quimica Medica (Iqog, Csic) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50318267 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 6.0 ChEMBL 10.1016/j.ejmech.2015.01.027 10.7270/Q23T9JXZ 25621991 Guzior, N; Bajda, M; Skrok, M; Kurpiewska, K; Lewinski, K; Brus, B; Pišlar, A; Kos, J; Gobec, S; Malawska, B 2/20/2015 4/24/2016 Jagiellonian University Medical College http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50325447 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 6.0 ChEMBL 10.1021/acs.jmedchem.5b00115 10.7270/Q2HQ41MH 25793650 Rochais, C; Lecoutey, C; Gaven, F; Giannoni, P; Hamidouche, K; Hedou, D; Dubost, E; Genest, D; Yahiaoui, S; Freret, T; Bouet, V; Dauphin, F; Sopkova de Oliveira Santos, J; Ballandonne, C; Corvaisier, S; Malzert-Fréon, A; Legay, R; Boulouard, M; Claeysen, S; Dallemagne, P 4/9/2015 4/28/2016 Cermn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50341577 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 15 ChEMBL 10.1016/j.ejmech.2015.02.063 10.7270/Q2GQ70HK 25778991 Sang, Z; Qiang, X; Li, Y; Yuan, W; Liu, Q; Shi, Y; Ang, W; Luo, Y; Tan, Z; Deng, Y 4/6/2015 10/8/2016 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50341700 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 12 ChEMBL 10.1016/j.ejmech.2015.02.063 10.7270/Q2GQ70HK 25778991 Sang, Z; Qiang, X; Li, Y; Yuan, W; Liu, Q; Shi, Y; Ang, W; Luo, Y; Tan, Z; Deng, Y 4/6/2015 10/8/2016 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50351102 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 15 ChEMBL 10.1021/acs.jmedchem.5b00599 10.7270/Q26T0PCZ 26107513 Farina, R; Pisani, L; Catto, M; Nicolotti, O; Gadaleta, D; Denora, N; Soto-Otero, R; Mendez-Alvarez, E; Passos, CS; Muncipinto, G; Altomare, CD; Nurisso, A; Carrupt, PA; Carotti, A 7/23/2015 10/13/2016 University of Bari Aldo Moro http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50368941 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 11 ChEMBL 10.1016/j.bmc.2014.07.009 10.7270/Q22809B6 25082512 Li, Y; Peng, P; Tang, L; Hu, Y; Hu, Y; Sheng, R 8/29/2014 10/28/2016 Zhejiang University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50375186 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 15 ChEMBL 10.1016/j.bmc.2015.01.042 10.7270/Q2BG2QS9 25678013 Liu, Q; Qiang, X; Li, Y; Sang, Z; Li, Y; Tan, Z; Deng, Y 2/23/2015 11/2/2016 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50393651 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 40 ChEMBL 10.1016/j.ejmech.2007.04.018 10.7270/Q2TH8MG0 17624631 Andreani, A; Burnelli, S; Granaiola, M; Guardigli, M; Leoni, A; Locatelli, A; Morigi, R; Rambaldi, M; Rizzoli, M; Varoli, L; Roda, A 3/10/2008 1/11/2010 Università http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50412579 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 20 ChEMBL 10.1016/j.ejmech.2008.02.035 10.7270/Q2833RT4 18396354 Belluti, F; Piazzi, L; Bisi, A; Gobbi, S; Bartolini, M; Cavalli, A; Valenti, P; Rampa, A 3/2/2009 1/11/2010 University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50413409 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 12 ChEMBL 10.1016/j.ejmech.2008.03.003 10.7270/Q29W0F8B 18436348 Sheng, R; Xu, Y; Hu, C; Zhang, J; Lin, X; Li, J; Yang, B; He, Q; Hu, Y 12/31/2008 1/11/2010 Zhejiang University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50425406 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 26.8 ChEMBL 10.1016/j.bmc.2008.07.014 10.7270/Q2RR1Z2W 18662884 Shen, Y; Sheng, R; Zhang, J; He, Q; Yang, B; Hu, Y 8/18/2008 1/11/2010 Zhejiang University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50429023 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 14 ChEMBL 10.1016/j.ejmech.2015.08.052 10.7270/Q21V5GT0 26363866 Luo, XT; Wang, CM; Liu, Y; Huang, ZG 10/9/2015 12/14/2016 1St Affiliated Hospital of Guangxi Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50448170 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 7.9 ChEMBL 10.1016/j.bmc.2008.12.067 10.7270/Q24J0F0R 19162488 Zhu, Y; Xiao, K; Ma, L; Xiong, B; Fu, Y; Yu, H; Wang, W; Wang, X; Hu, D; Peng, H; Li, J; Gong, Q; Chai, Q; Tang, X; Zhang, H; Li, J; Shen, J 2/23/2009 1/11/2010 Chinese Academy of Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50464333 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 2.3 ChEMBL 10.1016/S0960-894X(00)80545-4 10.7270/Q29886XS Gregor, VE; Emmerling, MR; Lee, C; Moore, CJ 12/28/1992 8/17/2010 TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50464359 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 5.7 ChEMBL 10.1016/S0960-894X(00)80547-8 10.7270/Q21R6QDV Sugimoto, H; Iimura, Y; Yamanishi, Y; Yamatsu, K 12/28/1992 8/17/2010 TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50468278 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 10.0 ChEMBL 10.1016/j.bmc.2016.02.023 10.7270/Q2125VHK 26917219 Xie, SS; Lan, JS; Wang, X; Wang, ZM; Jiang, N; Li, F; Wu, JJ; Wang, J; Kong, LY 3/13/2016 6/19/2017 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50498585 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 7.0 ChEMBL 10.1021/acsmedchemlett.6b00099 10.7270/Q2NG4SJJ 27096037 Gunaydin, H; Bartberger, MD 4/20/2016 9/10/2017 Merck http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50502591 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 11 ChEMBL 10.1021/acsmedchemlett.5b00483 10.7270/Q2PN97JV 27190595 Costanzo, P; Cariati, L; Desiderio, D; Sgammato, R; Lamberti, A; Arcone, R; Salerno, R; Nardi, M; Masullo, M; Oliverio, M 5/18/2016 9/26/2017 Magna Graecia University of Catanzaro http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50502623 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 10.0 ChEMBL 10.1021/acsmedchemlett.5b00483 10.7270/Q2PN97JV 27190595 Costanzo, P; Cariati, L; Desiderio, D; Sgammato, R; Lamberti, A; Arcone, R; Salerno, R; Nardi, M; Masullo, M; Oliverio, M 5/18/2016 9/26/2017 Magna Graecia University of Catanzaro http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50508688 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 120 ChEMBL 10.1016/j.bmc.2016.07.025 10.7270/Q2DV1MV0 27460699 Wang, J; Wang, ZM; Li, XM; Li, F; Wu, JJ; Kong, LY; Wang, XB 8/22/2016 10/6/2017 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50521824 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 10.0 ChEMBL 10.1016/j.ejmech.2016.05.055 10.7270/Q2HX1FNV 27267007 Estrada, M; Herrera-Arozamena, C; Pérez, C; Viña, D; Romero, A; Morales-García, JA; Pérez-Castillo, A; Rodríguez-Franco, MI 10/4/2016 7/10/2018 IQM-CSIC http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50523812 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 9.0 ChEMBL 10.1016/j.ejmech.2015.10.001 10.7270/Q2B27X8T 26471320 Wu, MY; Esteban, G; Brogi, S; Shionoya, M; Wang, L; Campiani, G; Unzeta, M; Inokuchi, T; Butini, S; Marco-Contelles, J 10/4/2016 7/17/2018 Okayama University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50531952 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 90 ChEMBL 10.1016/j.bmc.2016.10.016 10.7270/Q2B85B3V 27780618 Mughal, EU; Sadiq, A; Murtaza, S; Rafique, H; Zafar, MN; Riaz, T; Khan, BA; Hameed, A; Khan, KM 1/1/2017 8/13/2018 University of Gujrat http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50534800 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 48 ChEMBL 10.1016/j.ejmech.2016.07.052 10.7270/Q2ZW1NW5 27484514 Wang, ZM; Cai, P; Liu, QH; Xu, DQ; Yang, XL; Wu, JJ; Kong, LY; Wang, XB 11/10/2016 8/17/2018 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50543704 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 6.0 ChEMBL 10.1016/j.ejmech.2016.08.016 10.7270/Q2PZ5BT8 27560283 Wieckowska, A; Kolaczkowski, M; Bucki, A; Godyn, J; Marcinkowska, M; Wieckowski, K; Zareba, P; Siwek, A; Kazek, G; Gluch-Lutwin, M; Mierzejewski, P; Bienkowski, P; Sienkiewicz-Jarosz, H; Knez, D; Wichur, T; Gobec, S; Malawska, B 11/29/2016 8/31/2018 Jagiellonian University Collegium Medicum http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50544743 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 12 ChEMBL 10.1016/j.bmc.2009.07.072 10.7270/Q29S1R4M 19692250 Sheng, R; Lin, X; Zhang, J; Chol, KS; Huang, W; Yang, B; He, Q; Hu, Y 9/2/2009 8/31/2010 Zhejiang University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50553458 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 20 ChEMBL 10.1016/j.bmc.2010.01.071 10.7270/Q2P26Z7H 20171894 Rizzo, S; Bartolini, M; Ceccarini, L; Piazzi, L; Gobbi, S; Cavalli, A; Recanatini, M; Andrisano, V; Rampa, A 3/11/2010 9/2/2010 University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50578102 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 8 ChEMBL 10.1016/j.ejmech.2009.12.038 10.7270/Q25H7GFM 20053484 Lv, W; Xue, Y 2/17/2010 11/20/2010 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50585681 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 43 ChEMBL 10.1016/s0960-894x(02)00482-1 10.7270/Q2CZ37Q4 12182861 Clark, JK; Cowley, P; Muir, AW; Palin, R; Pow, E; Prosser, AB; Taylor, R; Zhang, MQ 8/16/2002 10/5/2012 Organon Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50588924 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens >100000 ChEMBL 10.1021/jm100293f 10.7270/Q2B56JXF 20420456 Melchiorre, C; Bolognesi, ML; Minarini, A; Rosini, M; Tumiatti, V 8/19/2010 3/19/2011 University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50597927 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 90 ChEMBL 10.1021/jm100573q 10.7270/Q23R0T3D 20684567 Chaudhaery, SS; Roy, KK; Shakya, N; Saxena, G; Sammi, SR; Nazir, A; Nath, C; Saxena, AK 9/2/2010 6/11/2011 Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50635765 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 32 ChEMBL 10.1016/j.bmc.2011.02.030 10.7270/Q2Q240JH 21429752 Mohamed, T; Zhao, X; Habib, LK; Yang, J; Rao, PP 3/29/2011 12/3/2011 University of Waterloo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50636569 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 6 ChEMBL 10.1016/j.bmcl.2010.12.041 10.7270/Q27W6CH9 21216144 Al-Rashid, ZF; Hsung, RP 4/25/2011 12/3/2011 Alchemical Research http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50637195 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 18 ChEMBL 10.1021/jm101299d 10.7270/Q2SQ90QT 21417225 Conejo-Garcia, A; Pisani, L; Nunez, Mdel C; Catto, M; Nicolotti, O; Leonetti, F; Campos, JM; Gallo, MA; Espinosa, A; Carotti, A 4/21/2011 12/4/2011 Universidad De Granada http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50638643 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 23 ChEMBL 10.1016/j.ejmech.2011.02.019 10.7270/Q2X92BM2 21397996 Belluti, F; Bartolini, M; Bottegoni, G; Bisi, A; Cavalli, A; Andrisano, V; Rampa, A 3/28/2011 12/4/2011 University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50645452 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 22 ChEMBL 10.1016/j.ejmech.2011.02.071 10.7270/Q2BK1CPG 21459491 Tasso, B; Catto, M; Nicolotti, O; Novelli, F; Tonelli, M; Giangreco, I; Pisani, L; Sparatore, A; Boido, V; Carotti, A; Sparatore, F 5/2/2011 12/6/2011 University of Genoa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50645460 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 22 ChEMBL 10.1016/j.ejmech.2011.02.071 10.7270/Q2BK1CPG 21459491 Tasso, B; Catto, M; Nicolotti, O; Novelli, F; Tonelli, M; Giangreco, I; Pisani, L; Sparatore, A; Boido, V; Carotti, A; Sparatore, F 5/2/2011 12/6/2011 University of Genoa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50645468 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 4150 ChEMBL 10.1016/j.ejmech.2011.02.071 10.7270/Q2BK1CPG 21459491 Tasso, B; Catto, M; Nicolotti, O; Novelli, F; Tonelli, M; Giangreco, I; Pisani, L; Sparatore, A; Boido, V; Carotti, A; Sparatore, F 5/2/2011 12/6/2011 University of Genoa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50645478 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 4150 ChEMBL 10.1016/j.ejmech.2011.02.071 10.7270/Q2BK1CPG 21459491 Tasso, B; Catto, M; Nicolotti, O; Novelli, F; Tonelli, M; Giangreco, I; Pisani, L; Sparatore, A; Boido, V; Carotti, A; Sparatore, F 5/2/2011 12/6/2011 University of Genoa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50664189 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 32 ChEMBL 10.1016/j.bmcl.2011.07.091 10.7270/Q2C829P7 21873056 Mohamed, T; Yeung, JC; Rao, PP 9/12/2011 3/24/2012 University of Waterloo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50706609 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 5 ChEMBL 10.1016/j.bmc.2011.09.061 10.7270/Q24F1R52 22019465 Huang, W; Tang, L; Shi, Y; Huang, S; Xu, L; Sheng, R; Wu, P; Li, J; Zhou, N; Hu, Y 11/9/2011 7/21/2012 Zhejiang University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50714175 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 19 ChEMBL 10.1016/j.ejmech.2016.12.009 10.7270/Q2NG4SW1 27951485 Li, Y; Qiang, X; Luo, L; Yang, X; Xiao, G; Liu, Q; Ai, J; Tan, Z; Deng, Y 1/27/2017 6/19/2019 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50714185 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 36 ChEMBL 10.1016/j.ejmech.2016.12.009 10.7270/Q2NG4SW1 27951485 Li, Y; Qiang, X; Luo, L; Yang, X; Xiao, G; Liu, Q; Ai, J; Tan, Z; Deng, Y 1/27/2017 6/19/2019 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50714970 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 30 ChEMBL 10.1016/j.ejmech.2016.12.005 10.7270/Q2D220WF 27951490 Mohamed, T; Rao, PPN 1/27/2017 6/19/2019 University of Waterloo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50740762 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 11 ChEMBL 10.1016/j.ejmech.2017.02.039 10.7270/Q2F76FVX 28279845 Sang, Z; Pan, W; Wang, K; Ma, Q; Yu, L; Yang, Y; Bai, P; Leng, C; Xu, Q; Li, X; Tan, Z; Liu, W 4/21/2017 8/20/2019 Nanyang Normal University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50740862 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 37 ChEMBL 10.1016/j.ejmech.2017.02.039 10.7270/Q2F76FVX 28279845 Sang, Z; Pan, W; Wang, K; Ma, Q; Yu, L; Yang, Y; Bai, P; Leng, C; Xu, Q; Li, X; Tan, Z; Liu, W 4/21/2017 8/20/2019 Nanyang Normal University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50762714 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 120 ChEMBL 10.1016/j.bmcl.2017.05.050 10.7270/Q2BG2RDS 28552337 Bharkavi, C; Vivek Kumar, S; Ashraf Ali, M; Osman, H; Muthusubramanian, S; Perumal, S 7/15/2017 10/17/2019 Madurai Kamaraj University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50769668 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Mus musculus 5.7 ChEMBL 10.1021/acs.jmedchem.7b01086 10.7270/Q2S75JRJ 29227101 Košak, U; Brus, B; Knez, D; Žakelj, S; Trontelj, J; Pišlar, A; Šink, R; Jukič, M; Živin, M; Podkowa, A; Nachon, F; Brazzolotto, X; Stojan, J; Kos, J; Coquelle, N; Sałat, K; Colletier, JP; Gobec, S 1/11/2018 10/31/2019 University of Ljubljana http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 50774368 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Mus musculus 5.7 ChEMBL 10.1021/jm00024a009 10.7270/Q2QC045T 7490731 Sugimoto, H; Iimura, Y; Yamanishi, Y; Yamatsu, K 1/2/1996 10/31/2012 Eisai http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 50774937 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 8 ChEMBL 10.1021/jm00007a005 10.7270/Q21N81S7 7707311 Nagel, AA; Liston, DR; Jung, S; Mahar, M; Vincent, LA; Chapin, D; Chen, YL; Hubbard, S; Ives, JL; Jones, SB 5/11/1995 10/31/2012 Pfizer http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50787802 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 38 ChEMBL 10.1016/j.ejmech.2017.02.045 10.7270/Q2FB55C0 28388521 Lan, JS; Zhang, T; Liu, Y; Yang, J; Xie, SS; Liu, J; Miao, ZY; Ding, Y 6/16/2017 11/29/2019 Shanghai University of Traditional Chinese Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50790621 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 37 ChEMBL 10.1016/j.bmc.2017.03.070 10.7270/Q2F76G04 28487125 Sang, Z; Pan, W; Wang, K; Ma, Q; Yu, L; Liu, W 6/15/2017 12/3/2019 Nanyang Normal University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50793155 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 16 ChEMBL 10.1021/jm981101z 10.7270/Q26M37JW 10052979 Contreras, JM; Rival, YM; Chayer, S; Bourguignon, JJ; Wermuth, CG 3/16/1999 11/13/2012 Louis Pasteur University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50802100 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 16 ChEMBL 10.1021/jm001088u 10.7270/Q2222VG9 11495583 Contreras, JM; Parrot, I; Sippl, W; Rival, YM; Wermuth, CG 8/9/2001 11/25/2012 Louis Pasteur University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50811176 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Bos taurus 2.9 ChEMBL 10.1021/jm0255668 10.7270/Q2GF0V7X 12502352 Savini, L; Gaeta, A; Fattorusso, C; Catalanotti, B; Campiani, G; Chiasserini, L; Pellerano, C; Novellino, E; McKissic, D; Saxena, A 12/27/2002 11/27/2012 University of Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 50824510 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 16 ChEMBL 10.1016/j.bmcl.2005.05.132 10.7270/Q27H1KBV 15993600 Sheng, R; Lin, X; Li, J; Jiang, Y; Shang, Z; Hu, Y 8/2/2005 12/2/2012 Zhejiang University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50830757 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 22 ChEMBL 10.1021/jm049309+ 10.7270/Q2TM7BWQ 15715468 Luo, W; Yu, QS; Zhan, M; Parrish, D; Deschamps, JR; Kulkarni, SS; Holloway, HW; Alley, GM; Lahiri, DK; Brossi, A; Greig, NH 2/17/2005 12/3/2012 National Institute On Aging http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50848521 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 23 ChEMBL 10.1021/jm070559a 10.7270/Q218379R 17850125 Bolognesi, ML; Banzi, R; Bartolini, M; Cavalli, A; Tarozzi, A; Andrisano, V; Minarini, A; Rosini, M; Tumiatti, V; Bergamini, C; Fato, R; Lenaz, G; Hrelia, P; Cattaneo, A; Recanatini, M; Melchiorre, C 9/27/2007 12/11/2012 University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50853606 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 23 ChEMBL 10.1021/jm7009364 10.7270/Q25B039W 18181565 Cavalli, A; Bolognesi, ML; Minarini, A; Rosini, M; Tumiatti, V; Recanatini, M; Melchiorre, C 2/7/2008 12/14/2012 University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50857406 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 37 ChEMBL 10.1016/j.bmcl.2017.09.055 10.7270/Q22J6F9F 29033232 Sang, Z; Wang, K; Wang, H; Yu, L; Wang, H; Ma, Q; Ye, M; Han, X; Liu, W 11/15/2017 1/26/2020 Nanyang Normal University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50858157 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 19 ChEMBL 10.1016/j.bmcl.2017.09.055 10.7270/Q22J6F9F 29033232 Sang, Z; Wang, K; Wang, H; Yu, L; Wang, H; Ma, Q; Ye, M; Han, X; Liu, W 11/15/2017 1/26/2020 Nanyang Normal University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50864178 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 160 ChEMBL 10.1016/j.bmc.2007.12.048 10.7270/Q27S7PMQ 18249544 Bembenek, SD; Keith, JM; Letavic, MA; Apodaca, R; Barbier, AJ; Dvorak, L; Aluisio, L; Miller, KL; Lovenberg, TW; Carruthers, NI 3/31/2008 12/15/2012 Johnson & Johnson Pharmaceutical Research and Development http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50871835 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Bos taurus 8.12 ChEMBL 10.1021/jm8001313 10.7270/Q2F76DGK 18517184 Camps, P; Formosa, X; Galdeano, C; Gomez, T; Munoz-Torrero, D; Scarpellini, M; Viayna, E; Badia, A; Clos, MV; Camins, A; Pallas, M; Bartolini, M; Mancini, F; Andrisano, V; Estelrich, J; Lizondo, M; Bidon-Chanal, A; Luque, FJ 6/19/2008 12/16/2012 Laboratori De Qu�Mica Farmac�Utica (Unitat Associada Al Csic) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 50871846 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 11.6 ChEMBL 10.1021/jm8001313 10.7270/Q2F76DGK 18517184 Camps, P; Formosa, X; Galdeano, C; Gomez, T; Munoz-Torrero, D; Scarpellini, M; Viayna, E; Badia, A; Clos, MV; Camins, A; Pallas, M; Bartolini, M; Mancini, F; Andrisano, V; Estelrich, J; Lizondo, M; Bidon-Chanal, A; Luque, FJ 6/19/2008 12/16/2012 Laboratori De Qu�Mica Farmac�Utica (Unitat Associada Al Csic) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50871869 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 5.7 ChEMBL 10.1021/jm8001313 10.7270/Q2F76DGK 18517184 Camps, P; Formosa, X; Galdeano, C; Gomez, T; Munoz-Torrero, D; Scarpellini, M; Viayna, E; Badia, A; Clos, MV; Camins, A; Pallas, M; Bartolini, M; Mancini, F; Andrisano, V; Estelrich, J; Lizondo, M; Bidon-Chanal, A; Luque, FJ 6/19/2008 12/16/2012 Laboratori De Qu�Mica Farmac�Utica (Unitat Associada Al Csic) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50871873 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Bos taurus 19 ChEMBL 10.1021/jm8001313 10.7270/Q2F76DGK 18517184 Camps, P; Formosa, X; Galdeano, C; Gomez, T; Munoz-Torrero, D; Scarpellini, M; Viayna, E; Badia, A; Clos, MV; Camins, A; Pallas, M; Bartolini, M; Mancini, F; Andrisano, V; Estelrich, J; Lizondo, M; Bidon-Chanal, A; Luque, FJ 6/19/2008 12/16/2012 Laboratori De Qu�Mica Farmac�Utica (Unitat Associada Al Csic) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 50879191 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 23.1 ChEMBL 10.1021/jm8009684 10.7270/Q2MW2J3W 18954037 Tumiatti, V; Milelli, A; Minarini, A; Rosini, M; Bolognesi, ML; Micco, M; Andrisano, V; Bartolini, M; Mancini, F; Recanatini, M; Cavalli, A; Melchiorre, C 2/20/2009 12/20/2012 University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50881005 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 30 ChEMBL 10.1016/j.ejmech.2017.02.042 10.7270/Q2P55R0J 28242549 Xia, CL; Wang, N; Guo, QL; Liu, ZQ; Wu, JQ; Huang, SL; Ou, TM; Tan, JH; Wang, HG; Li, D; Huang, ZS 4/21/2017 2/5/2020 Sun Yat-Sen University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50881682 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 10.0 ChEMBL 10.1016/j.ejmech.2017.02.034 10.7270/Q2JD5086 28242552 Monjas, L; Arce, MP; León, R; Egea, J; Pérez, C; Villarroya, M; López, MG; Gil, C; Conde, S; Rodríguez-Franco, MI 4/21/2017 2/6/2020 IQM-CSIC http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50888178 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 12 ChEMBL 10.1016/j.ejmech.2017.04.054 10.7270/Q2H41TX2 28458136 Sang, Z; Qiang, X; Li, Y; Xu, R; Cao, Z; Song, Q; Wang, T; Zhang, X; Liu, H; Tan, Z; Deng, Y 7/28/2017 2/26/2020 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50888183 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 15 ChEMBL 10.1016/j.ejmech.2017.04.054 10.7270/Q2H41TX2 28458136 Sang, Z; Qiang, X; Li, Y; Xu, R; Cao, Z; Song, Q; Wang, T; Zhang, X; Liu, H; Tan, Z; Deng, Y 7/28/2017 2/26/2020 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50895443 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 50 ChEMBL 10.1016/j.bmcl.2017.07.013 10.7270/Q20P12G0 28751142 Zhou, LY; Zhu, Y; Jiang, YR; Zhao, XJ; Guo, D 9/1/2017 3/18/2020 Central South University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50913402 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 8.20 ChEMBL 10.1021/jm901902w 10.7270/Q25T3MFV 20575555 de Los Rios, C; Egea, J; Marco-Contelles, J; Leon, R; Samadi, A; Iriepa, I; Moraleda, I; Galvez, E; Garcia, AG; Lopez, MG; Villarroya, M; Romero, A 7/29/2010 12/31/2012 Universidad Autonoma De Madrid http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50919271 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 120 ChEMBL 10.1016/j.bmcl.2010.09.108 10.7270/Q2Q2417W 20951037 Ali, MA; Ismail, R; Choon, TS; Yoon, YK; Wei, AC; Pandian, S; Kumar, RS; Osman, H; Manogaran, E 11/8/2010 1/3/2013 Universiti Sains Malaysia http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50943897 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 32 ChEMBL 10.1016/j.bmcl.2012.05.077 10.7270/Q27S7PSZ 22704921 Mohamed, T; Yeung, JC; Vasefi, MS; Beazely, MA; Rao, PP 7/3/2012 2/8/2013 University of Waterloo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50949799 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 21.5 ChEMBL 10.1016/j.bmc.2011.05.027 10.7270/Q22B903F 22172310 Anand, P; Singh, B 12/30/2011 2/8/2013 Punjabi University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50953151 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 10 ChEMBL 10.1016/j.ejmech.2012.09.030 10.7270/Q2MP54CK 23078965 Samadi, A; Estrada, M; Perez, C; Rodriguez-Franco, MI; Iriepa, I; Moraleda, I; Chioua, M; Marco-Contelles, J 11/26/2012 2/8/2013 Instituto De Qu£Mica Org£Nica General (Csic) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50983315 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 25 ChEMBL 10.7270/Q2ZP4BBB 36067929 Fang, L; Shen, S; Liu, Q; Liu, Z; Zhao, J 11/1/2022 4/18/2024 Southeast University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50984008 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 5.7 ChEMBL 10.1016/j.ejmech.2017.08.051 10.7270/Q2XS5XWN 28863358 Chierrito, TPC; Pedersoli-Mantoani, S; Roca, C; Requena, C; Sebastian-Perez, V; Castillo, WO; Moreira, NCS; Pérez, C; Sakamoto-Hojo, ET; Takahashi, CS; Jiménez-Barbero, J; Cañada, FJ; Campillo, NE; Martinez, A; Carvalho, I 10/20/2017 6/3/2020 University of S£O Paulo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50986019 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 20 ChEMBL 10.1016/j.ejmech.2017.09.022 10.7270/Q27083ZM 29031067 Pandolfi, F; De Vita, D; Bortolami, M; Coluccia, A; Di Santo, R; Costi, R; Andrisano, V; Alabiso, F; Bergamini, C; Fato, R; Bartolini, M; Scipione, L 12/1/2017 6/12/2020 Sapienza University of Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50994371 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 8 ChEMBL 10.1021/jm950704x 10.7270/Q25D8T1Q 8558505 Tong, W; Collantes, ER; Chen, Y; Welsh, WJ 2/28/1996 5/20/2013 University of Missouri St. Louis http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51007492 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 35.48 ChEMBL 10.1016/j.bmc.2008.10.029 10.7270/Q2FQ9XVP 18976927 Morini, G; Comini, M; Rivara, M; Rivara, S; Bordi, F; Plazzi, PV; Flammini, L; Saccani, F; Bertoni, S; Ballabeni, V; Barocelli, E; Mor, M 11/17/2008 5/21/2013 University of Parma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 51030332 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 41 ChEMBL 10.1016/j.ejmech.2018.01.055 10.7270/Q2M61NST 29407958 Jiang, N; Huang, Q; Liu, J; Liang, N; Li, Q; Li, Q; Xie, SS 2/25/2018 8/6/2020 Jiangxi University of Traditional Chinese Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51031508 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 5.7 ChEMBL 10.1016/j.ejmech.2018.01.066 10.7270/Q2K64MM0 29421570 Dias Viegas, FP; de Freitas Silva, M; Divino da Rocha, M; Castelli, MR; Riquiel, MM; Machado, RP; Vaz, SM; Simões de Lima, LM; Mancini, KC; Marques de Oliveira, PC; Morais, ÉP; Gontijo, VS; da Silva, FMR; D'Alincourt da Fonseca Peçanha, D; Castro, NG; Neves, GA; Giusti-Paiva, A; Vilela, FC; Orlandi, L; Camps, I; Veloso, MP; Leomil Coelho, LF; Ionta, M; Ferreira-Silva, GÁ; Pereira, RM; Dardenne, LE; Guedes, IA; de Oliveira Carneiro Junior, W; Quaglio Bellozi, PM; Pinheiro de Oliveira, AC; Ferreira, FF; Pruccoli, L; Tarozzi, A; Viegas, C 3/10/2018 8/8/2020 Federal University of Alfenas http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51039181 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Bos taurus 4.2 ChEMBL 10.1016/j.bmc.2012.10.045 10.7270/Q2QV3NTH 23199476 Catto, M; Pisani, L; Leonetti, F; Nicolotti, O; Pesce, P; Stefanachi, A; Cellamare, S; Carotti, A 12/18/2012 9/24/2013 University of Bari Aldo Moro http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 51039207 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 2.0 ChEMBL 10.1016/j.bmc.2012.10.045 10.7270/Q2QV3NTH 23199476 Catto, M; Pisani, L; Leonetti, F; Nicolotti, O; Pesce, P; Stefanachi, A; Cellamare, S; Carotti, A 12/18/2012 9/24/2013 University of Bari Aldo Moro http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51042060 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 7.2 ChEMBL 10.1016/j.bmcl.2012.11.100 10.7270/Q2F19118 23276831 Mishra, N; Sasmal, D 1/14/2013 9/24/2013 Birla Institute of Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51046182 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 5.7 ChEMBL 10.1016/j.bmc.2012.11.044 10.7270/Q20C4X3F 23273608 Hu, Y; Zhang, J; Chandrashankra, O; Ip, FC; Ip, NY 1/15/2013 9/24/2013 The Hong Kong University of Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51046185 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 32 ChEMBL 10.1016/j.bmc.2012.11.044 10.7270/Q20C4X3F 23273608 Hu, Y; Zhang, J; Chandrashankra, O; Ip, FC; Ip, NY 1/15/2013 9/24/2013 The Hong Kong University of Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 51107699 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 13 ChEMBL 10.1016/j.bmc.2017.09.012 10.7270/Q22V2JP6 29089261 Singh, M; Kaur, M; Singh, N; Silakari, O 12/15/2017 8/15/2020 Punjabi University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 51108988 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Mus musculus 14550 ChEMBL 10.1016/j.bmc.2017.11.033 10.7270/Q2JQ13MH 29195794 Piplani, P; Jain, A; Devi, D; Anjali, na; Sharma, A; Silakari, P 1/1/2018 8/15/2020 Panjab University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 51116764 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 3.5 ChEMBL 10.1016/j.ejmech.2017.07.006 10.7270/Q2HM5C2T 28728106 Zhao, XJ; Gong, DM; Jiang, YR; Guo, D; Zhu, Y; Deng, YC 9/29/2017 8/16/2020 Central South University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51117364 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 32 ChEMBL 10.1016/j.ejmech.2017.07.055 10.7270/Q2GM89X1 28797883 Lan, JS; Ding, Y; Liu, Y; Kang, P; Hou, JW; Zhang, XY; Xie, SS; Zhang, T 10/20/2017 8/16/2020 Shanghai University of Traditional Chinese Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51117539 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 160 ChEMBL 10.1016/j.ejmech.2017.07.077 10.7270/Q2Q52S78 28800459 Wang, J; Cai, P; Yang, XL; Li, F; Wu, JJ; Kong, LY; Wang, XB 10/20/2017 8/16/2020 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51128796 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 6.9 ChEMBL 10.1016/j.bmcl.2018.07.019 10.7270/Q2R21422 30017317 Gabr, MT; Abdel-Raziq, MS 9/15/2018 8/17/2020 Mansoura University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51133953 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 5.7 ChEMBL 10.1016/j.ejmech.2018.01.007 10.7270/Q2JQ13PD 29335209 Chierrito, TPC; Pedersoli-Mantoani, S; Roca, C; Sebastian-Pérez, V; Martínez-Gonzalez, L; Pérez, DI; Perez, C; Canales, A; Cañada, FJ; Campillo, NE; Carvalho, I; Martinez, A 2/10/2018 8/18/2020 University of S£O Paulo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51140790 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 10.0 ChEMBL 10.1016/j.ejmech.2018.07.056 10.7270/Q2F192DM 30245401 Reis, J; Cagide, F; Valencia, ME; Teixeira, J; Bagetta, D; Pérez, C; Uriarte, E; Oliveira, PJ; Ortuso, F; Alcaro, S; Rodríguez-Franco, MI; Borges, F 10/5/2018 8/18/2020 University of Porto http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51143939 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 10.0 ChEMBL 10.1016/j.ejmech.2018.07.026 10.7270/Q2N300PH 30025348 Estrada Valencia, M; Herrera-Arozamena, C; de Andrés, L; Pérez, C; Morales-García, JA; Pérez-Castillo, A; Ramos, E; Romero, A; Viña, D; Yáñez, M; Laurini, E; Pricl, S; Rodríguez-Franco, MI 8/5/2018 8/18/2020 IQM-CSIC http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51144123 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 22 ChEMBL 10.1016/j.ejmech.2018.07.033 10.7270/Q27W6FW2 30031971 Knez, D; Coquelle, N; Pišlar, A; Žakelj, S; Jukič, M; Sova, M; Mravljak, J; Nachon, F; Brazzolotto, X; Kos, J; Colletier, JP; Gobec, S 8/5/2018 8/18/2020 University of Ljubljana http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51144806 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 48 ChEMBL 10.1016/j.ejmech.2018.08.005 10.7270/Q29P34C1 30096650 Cai, P; Fang, SQ; Yang, HL; Yang, XL; Liu, QH; Kong, LY; Wang, XB 9/5/2018 8/18/2020 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51144819 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 38 ChEMBL 10.1016/j.ejmech.2018.08.005 10.7270/Q29P34C1 30096650 Cai, P; Fang, SQ; Yang, HL; Yang, XL; Liu, QH; Kong, LY; Wang, XB 9/5/2018 8/18/2020 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51188481 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 22 ChEMBL 10.1007/s00044-012-0162-3 10.7270/Q25D8VS0 n/a 12/28/2013 8/31/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 51188786 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 16 ChEMBL 10.1007/s00044-012-0227-3 10.7270/Q24F1TN5 n/a 12/28/2013 8/31/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 51196249 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 40 ChEMBL 10.1016/j.bmcl.2013.05.092 10.7270/Q2JD50Q1 23791077 Mohamed, T; Osman, W; Tin, G; Rao, PP 8/1/2013 9/1/2020 University of Waterloo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51198658 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 10.0 ChEMBL 10.1016/j.ejmech.2013.06.021 10.7270/Q2KW5JZX 23838422 Samadi, A; de la Fuente Revenga, M; Pérez, C; Iriepa, I; Moraleda, I; Rodríguez-Franco, MI; Marco-Contelles, J 9/28/2013 9/1/2020 Instituto De Qu£Mica Org£Nica General (Csic) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51210465 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 12 ChEMBL 10.1016/j.ejmech.2014.09.081 10.7270/Q2CF9T2R 25282266 Huang, L; Miao, H; Sun, Y; Meng, F; Li, X 11/24/2014 9/3/2020 Sun Yat-Sen University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51218670 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 22 ChEMBL 10.1016/j.bmc.2016.01.031 10.7270/Q2B85C4Q 26827140 Makhaeva, GF; Boltneva, NP; Lushchekina, SV; Serebryakova, OG; Stupina, TS; Terentiev, AA; Serkov, IV; Proshin, AN; Bachurin, SO; Richardson, RJ 3/1/2016 9/4/2020 Institute of Physiologically Active Compounds Russian Academy of Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51227518 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Mus musculus 1060 ChEMBL 10.1016/j.bmc.2018.12.007 10.7270/Q21Z47PZ 30578075 Bacalhau, P; Fernandes, L; Rosário Martins, M; Candeias, F; Carreiro, EP; López, Ó; Teresa Caldeira, A; Totobenazara, J; Guedes, RC; Burke, AJ 1/15/2019 2/18/2021 Universidade De £Vora http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 51227524 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Mus musculus 125310 ChEMBL 10.1016/j.bmc.2018.12.007 10.7270/Q21Z47PZ 30578075 Bacalhau, P; Fernandes, L; Rosário Martins, M; Candeias, F; Carreiro, EP; López, Ó; Teresa Caldeira, A; Totobenazara, J; Guedes, RC; Burke, AJ 1/15/2019 2/18/2021 Universidade De £Vora http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 51229230 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 11 ChEMBL 10.1016/j.ejmech.2019.111737 10.7270/Q24J0JCX 31581002 Bai, P; Wang, K; Zhang, P; Shi, J; Cheng, X; Zhang, Q; Zheng, C; Cheng, Y; Yang, J; Lu, X; Sang, Z 12/1/2019 2/18/2021 Chinese Academy of Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51239549 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 6.0 ChEMBL 10.1016/j.ejmech.2018.10.064 10.7270/Q2T72MRJ 30447434 Lalut, J; Santoni, G; Karila, D; Lecoutey, C; Davis, A; Nachon, F; Silman, I; Sussman, J; Weik, M; Maurice, T; Dallemagne, P; Rochais, C 1/15/2019 2/19/2021 Normandie Univ http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51248802 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 5.7 ChEMBL 10.1016/j.bmc.2019.01.025 10.7270/Q2N87F3N 30744931 Mishra, P; Kumar, A; Panda, G 3/15/2019 2/20/2021 Csir-Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51253587 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 40 ChEMBL 10.1016/j.bmc.2019.07.001 10.7270/Q20V8H48 31288978 Srivastava, P; Tripathi, PN; Sharma, P; Shrivastava, SK 8/15/2019 2/20/2021 Indian Institute of Technology (Banaras Hindu University) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51262098 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 12 ChEMBL 10.1016/j.ejmech.2019.111596 10.7270/Q2988BC8 31419776 Lanthier, C; Payan, H; Liparulo, I; Hatat, B; Lecoutey, C; Since, M; Davis, A; Bergamini, C; Claeysen, S; Dallemagne, P; Bolognesi, ML; Rochais, C 11/15/2019 2/21/2021 Normandie Univ http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51271852 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 5.6 ChEMBL 10.1016/j.ejmech.2019.111785 10.7270/Q2Q81HF9 31669851 Bajda, M; Łażewska, D; Godyń, J; Zaręba, P; Kuder, K; Hagenow, S; Łątka, K; Stawarska, E; Stark, H; Kieć-Kononowicz, K; Malawska, B 1/1/2020 2/23/2021 Jagiellonian University Medical College http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51276583 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 15 ChEMBL 10.1016/j.bmc.2018.11.015 10.7270/Q2WD4400 30470598 Song, Q; Li, Y; Cao, Z; Liu, H; Tian, C; Yang, Z; Qiang, X; Tan, Z; Deng, Y 12/15/2018 2/23/2021 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 51284481 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Mus musculus 12 ChEMBL 10.1016/j.bmcl.2019.04.051 10.7270/Q2251NM8 31078410 Huang, L; Ding, L; Li, X; Wang, N; Yan, Y; Yang, M; Cui, W; Benjamin Naman, C; Cheng, K; Zhang, W; Zhang, B; Jin, H; He, S 7/1/2019 2/24/2021 Ningbo University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 51287048 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 16 ChEMBL 10.1016/j.ejmech.2019.05.062 10.7270/Q2RF5ZGP 31158754 Purgatorio, R; de Candia, M; Catto, M; Carrieri, A; Pisani, L; De Palma, A; Toma, M; Ivanova, OA; Voskressensky, LG; Altomare, CD 9/1/2019 2/24/2021 University of Bari Aldo Moro http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51290383 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 10.0 ChEMBL 10.1016/j.ejmech.2019.01.030 10.7270/Q2VQ363K 30685536 González-Naranjo, P; Pérez-Macias, N; Pérez, C; Roca, C; Vaca, G; Girón, R; Sánchez-Robles, E; Martín-Fontelles, MI; de Ceballos, ML; Martin-Requero, A; Campillo, NE; Páez, JA 3/15/2019 2/25/2021 Instituto De Qu£Mica M£Dica (Csic) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51297463 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 59 ChEMBL 10.1016/j.ejmech.2019.111651 10.7270/Q2ZP49K2 31479975 Mahmoud, WR; Nissan, YM; Elsawah, MM; Refaey, RH; Ragab, MF; Amin, KM 11/15/2019 2/25/2021 Cairo University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51311492 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 5.7 ChEMBL 10.1016/j.bmc.2018.12.030 10.7270/Q2XP78D7 30765302 de Andrade, P; Mantoani, SP; Gonçalves Nunes, PS; Magadán, CR; Pérez, C; Xavier, DJ; Hojo, ETS; Campillo, NE; Martínez, A; Carvalho, I 3/15/2019 2/27/2021 University of S£O Paulo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51321365 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Mus musculus 1820 ChEMBL 10.1016/j.bmc.2016.07.061 10.7270/Q2765JT4 27519464 Singla, S; Piplani, P 10/1/2016 2/28/2021 Panjab University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 51322847 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 33 ChEMBL 10.1016/j.ejmech.2019.02.030 10.7270/Q2JD5192 30784883 Sharma, P; Tripathi, A; Tripathi, PN; Prajapati, SK; Seth, A; Tripathi, MK; Srivastava, P; Tiwari, V; Krishnamurthy, S; Shrivastava, SK 4/1/2019 2/28/2021 Indian Institute of Technology (Banaras Hindu University) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51322910 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Mus musculus 84 ChEMBL 10.1016/j.ejmech.2019.02.053 10.7270/Q2DN48JW 30822710 Wang, D; Hu, M; Li, X; Zhang, D; Chen, C; Fu, J; Shao, S; Shi, G; Zhou, Y; Wu, S; Zhang, T 4/15/2019 2/28/2021 Peking Union Medical College http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 51324278 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 10.0 ChEMBL 10.1021/acs.jmedchem.6b00426 10.7270/Q2SJ1Q44 27253679 Shidore, M; Machhi, J; Shingala, K; Murumkar, P; Sharma, MK; Agrawal, N; Tripathi, A; Parikh, Z; Pillai, P; Yadav, MR 6/23/2016 2/28/2021 The Maharaja Sayajirao University of Baroda http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51336042 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 13 ChEMBL 10.1021/acsmedchemlett.9b00656 10.7270/Q2WS8XS4 32435398 Catto, M; Pisani, L; de la Mora, E; Belviso, BD; Mangiatordi, GF; Pinto, A; Palma, A; Denora, N; Caliandro, R; Colletier, JP; Silman, I; Nicolotti, O; Altomare, CD 5/14/2020 8/12/2021 University of Bari Aldo Moro http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51336051 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 16 ChEMBL 10.1021/acsmedchemlett.9b00656 10.7270/Q2WS8XS4 32435398 Catto, M; Pisani, L; de la Mora, E; Belviso, BD; Mangiatordi, GF; Pinto, A; Palma, A; Denora, N; Caliandro, R; Colletier, JP; Silman, I; Nicolotti, O; Altomare, CD 5/14/2020 8/12/2021 University of Bari Aldo Moro http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51350197 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 42 ChEMBL 10.1016/j.ejmech.2019.111707 10.7270/Q2833WM3 31561043 Tripathi, A; Choubey, PK; Sharma, P; Seth, A; Tripathi, PN; Tripathi, MK; Prajapati, SK; Krishnamurthy, S; Shrivastava, SK 12/1/2019 3/21/2022 Indian Institute of Technology (Banaras Hindu University) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51350762 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 120 ChEMBL 10.1016/j.bmcl.2020.127404 10.7270/Q2P55S39 32717612 Le-Nhat-Thuy, G; Nguyen Thi, N; Pham-The, H; Dang Thi, TA; Nguyen Thi, H; Nguyen Thi, TH; Nguyen Hoang, S; Nguyen, TV 9/15/2020 3/21/2022 Viet Nam http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 51354731 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 6.0 ChEMBL 10.1039/d0md00009d 10.7270/Q2C82DXM 33479638 de Souza, MM; Andreolla, MC; Ribeiro, TC; Gonçalves, AE; Medeiros, AR; de Souza, AS; Ferreira, LLG; Andricopulo, AD; Yunes, RA; de Oliveira, AS 2/1/2020 3/22/2022 School of Health Sciences/Graduate Program In Pharmaceutical Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51356978 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 10.0 ChEMBL 10.1016/j.bmc.2020.115820 10.7270/Q2WW7N96 33120080 Lin, SX; Curtis, MA; Sperry, J 12/15/2020 3/22/2022 University of Auckland http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 51366748 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 5.0 ChEMBL 10.1016/j.bmc.2020.115940 10.7270/Q20K2D6W 33340937 Jiang, X; Wang, Y; Liu, C; Xing, C; Wang, Y; Lyu, W; Wang, S; Li, Q; Chen, T; Chen, Y; Feng, F; Liu, W; Sun, H 1/15/2021 3/24/2022 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51368515 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 148 ChEMBL 10.1016/j.bmc.2019.02.031 10.7270/Q2CJ8J40 30795991 Tripathi, PN; Srivastava, P; Sharma, P; Seth, A; Shrivastava, SK 4/1/2019 3/25/2022 Indian Institute of Technology (Banaras Hindu University) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51370619 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 42 ChEMBL 10.1016/j.bmc.2020.115721 10.7270/Q2J106T5 33007563 Choubey, PK; Tripathi, A; Sharma, P; Shrivastava, SK 11/15/2020 3/25/2022 Indian Institute of Technology (Banaras Hindu University) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51371635 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 18 ChEMBL 10.1016/j.bmcl.2020.127659 10.7270/Q28919H1 33137375 Du, H; Jiang, X; Ma, M; Xu, H; Liu, S; Ma, F 12/15/2020 3/25/2022 Xinyang Normal University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51373698 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 15 ChEMBL 10.1016/j.ejmech.2019.111958 10.7270/Q2FR0187 31865014 Sang, Z; Wang, K; Shi, J; Cheng, X; Zhu, G; Wei, R; Ma, Q; Yu, L; Zhao, Y; Tan, Z; Liu, W 2/1/2020 3/26/2022 Nanyang Normal University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 51373718 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 11 ChEMBL 10.1016/j.ejmech.2019.111958 10.7270/Q2FR0187 31865014 Sang, Z; Wang, K; Shi, J; Cheng, X; Zhu, G; Wei, R; Ma, Q; Yu, L; Zhao, Y; Tan, Z; Liu, W 2/1/2020 3/26/2022 Nanyang Normal University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51375493 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 6.0 ChEMBL 10.1016/j.ejmech.2020.112743 10.7270/Q2P272S9 32882609 Łażewska, D; Bajda, M; Kaleta, M; Zaręba, P; Doroz-Płonka, A; Siwek, A; Alachkar, A; Mogilski, S; Saad, A; Kuder, K; Olejarz-Maciej, A; Godyń, J; Stary, D; Sudoł, S; Więcek, M; Latacz, G; Walczak, M; Handzlik, J; Sadek, B; Malawska, B; Kieć-Kononowicz, K 12/1/2020 3/26/2022 Jagiellonian University Medical College http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51377763 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 48 ChEMBL 10.1016/j.ejmech.2020.113124 10.7270/Q2SJ1Q8X 33395623 Erdogan, M; Kilic, B; Sagkan, RI; Aksakal, F; Ercetin, T; Gulcan, HO; Dogruer, DS 2/15/2021 3/26/2022 Gazi University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51378984 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 32 ChEMBL 10.1016/j.bmc.2021.116074 10.7270/Q2HX1HBN 33640707 Cao, Z; Song, Q; Yu, G; Liu, Z; Cong, S; Tan, Z; Deng, Y 4/1/2021 3/26/2022 Guizhou Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51384010 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 9.0 ChEMBL 10.1021/acs.jmedchem.0c01192 10.7270/Q2XD15CH 33111525 Ye, N; Qin, W; Tian, S; Xu, Q; Wold, EA; Zhou, J; Zhen, XC 12/24/2020 3/27/2022 Soochow University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51388190 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 7120 ChEMBL 10.1021/acs.jmedchem.0c00756 10.7270/Q29Z98KD 32787143 Gabr, MT; Brogi, S 9/10/2020 3/28/2022 Stanford University School of Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51392420 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 7.0 ChEMBL 10.1016/j.ejmech.2020.113059 10.7270/Q2KP85V3 33310288 Toublet, FX; Lalut, J; Hatat, B; Lecoutey, C; Davis, A; Since, M; Corvaisier, S; Freret, T; Sopková-de Oliveira Santos, J; Claeysen, S; Boulouard, M; Dallemagne, P; Rochais, C 1/15/2021 3/29/2022 Normandie Univ http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51394068 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 27 ChEMBL 10.1016/j.ejmech.2021.113224 10.7270/Q2HM5D5K 33582578 Manzoor, S; Prajapati, SK; Majumdar, S; Raza, MK; Gabr, MT; Kumar, S; Pal, K; Rashid, H; Kumar, S; Krishnamurthy, S; Hoda, N 4/5/2021 3/29/2022 Jamia Millia Islamia http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51396698 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 14 ChEMBL 10.1016/j.ejmech.2020.112140 10.7270/Q2RV0SGV 32088494 Mozaffarnia, S; Teimuri-Mofrad, R; Rashidi, MR 4/1/2020 3/29/2022 University of Tabriz http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51396775 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 9.0 ChEMBL 10.1016/j.ejmech.2020.112180 10.7270/Q2N301PX 32131034 Sang, Z; Wang, K; Shi, J; Liu, W; Cheng, X; Zhu, G; Wang, Y; Zhao, Y; Qiao, Z; Wu, A; Tan, Z 4/15/2020 3/29/2022 Nanyang Normal University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51397323 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 30 ChEMBL 10.1016/j.ejmech.2020.112257 10.7270/Q2K35ZCB 32375073 Singh, YP; Tej, GNVC; Pandey, A; Priya, K; Pandey, P; Shankar, G; Nayak, PK; Rai, G; Chittiboyina, AG; Doerksen, RJ; Vishwakarma, S; Modi, G 7/15/2020 3/29/2022 Indian Institute of Technology (Banaras Hindu University) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51397661 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 2170 ChEMBL 10.1016/j.ejmech.2020.112368 10.7270/Q2XD15DZ 32388114 Rodríguez-Lavado, J; Gallardo-Garrido, C; Mallea, M; Bustos, V; Osorio, R; Hödar-Salazar, M; Chung, H; Araya-Maturana, R; Lorca, M; Pessoa-Mahana, CD; Mella-Raipán, J; Saitz, C; Jaque, P; Reyes-Parada, M; Iturriaga-Vásquez, P; Pessoa-Mahana, H 7/15/2020 3/29/2022 Universidad De Chile http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51398106 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 30 ChEMBL 10.1016/j.ejmech.2020.112415 10.7270/Q27P9344 32454229 Zhou, B; Li, H; Cui, Z; Li, D; Geng, H; Gao, J; Zhou, L 8/15/2020 3/29/2022 Northwest A&F University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51404156 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 60 ChEMBL 10.1016/j.bmc.2021.116385 10.7270/Q28W3J18 34481338 Singh, YP; Shankar, G; Jahan, S; Singh, G; Kumar, N; Barik, A; Upadhyay, P; Singh, L; Kamble, K; Singh, GK; Tiwari, S; Garg, P; Gupta, S; Modi, G 9/15/2021 8/19/2022 Indian Institute of Technology (Banaras Hindu University) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51408021 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 2.0 ChEMBL 10.1021/acs.jmedchem.0c01863 10.7270/Q2JW8JNQ 33570950 Zhou, Y; Fu, Y; Yin, W; Li, J; Wang, W; Bai, F; Xu, S; Gong, Q; Peng, T; Hong, Y; Zhang, D; Zhang, D; Liu, Q; Xu, Y; Xu, HE; Zhang, H; Jiang, H; Liu, H 2/25/2021 8/19/2022 Chinese Academy of Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 51408047 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 8.0 ChEMBL 10.1021/acs.jmedchem.0c01863 10.7270/Q2JW8JNQ 33570950 Zhou, Y; Fu, Y; Yin, W; Li, J; Wang, W; Bai, F; Xu, S; Gong, Q; Peng, T; Hong, Y; Zhang, D; Zhang, D; Liu, Q; Xu, Y; Xu, HE; Zhang, H; Jiang, H; Liu, H 2/25/2021 8/19/2022 Chinese Academy of Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51408846 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 15 ChEMBL 10.1016/j.ejmech.2021.113310 10.7270/Q28G8QGX 33667847 Sang, Z; Song, Q; Cao, Z; Deng, Y; Tan, Z; Zhang, L 4/15/2021 8/20/2022 Nanyang Normal University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 51417546 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 10.0 ChEMBL 10.1016/j.ejmech.2021.113541 10.7270/Q25D8WNM 34116326 Chowdhury, SR; Gu, J; Hu, Y; Wang, J; Lei, S; Tavallaie, MS; Lam, C; Lu, D; Jiang, F; Fu, L 10/15/2021 8/22/2022 Shanghai Jiao Tong University (Sjtu) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51422165 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 44 ChEMBL 10.1016/j.ejmech.2021.113663 10.7270/Q2222ZKW 34198150 Jiang, X; Liu, C; Zou, M; Xie, H; Lin, T; Lyu, W; Xu, J; Li, Y; Feng, F; Sun, H; Liu, W 11/5/2021 8/23/2022 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51422647 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 18 ChEMBL 10.1016/j.ejmech.2021.113735 10.7270/Q2H41W7X 34371367 Jiang, X; Zhang, Z; Zuo, J; Wu, C; Zha, L; Xu, Y; Wang, S; Shi, J; Liu, XH; Zhang, J; Tang, W 11/5/2021 8/23/2022 Anhui Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51433648 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 27 ChEMBL 10.1016/j.ejmech.2021.113779 10.7270/Q2TB1BQF 34418785 Pont, C; Ginex, T; Griñán-Ferré, C; Scheiner, M; Mattellone, A; Martínez, N; Arce, EM; Soriano-Fernández, Y; Naldi, M; De Simone, A; Barenys, M; Gómez-Catalán, J; Pérez, B; Sabate, R; Andrisano, V; Loza, MI; Brea, J; Bartolini, M; Bolognesi, ML; Decker, M; Pallàs, M; Luque, FJ; Muñoz-Torrero, D 12/5/2021 8/24/2022 University of Barcelona http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51436910 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Mus musculus 6100 ChEMBL 10.1021/acs.jmedchem.1c00160 10.7270/Q2FR01GX 34024109 Yao, H; Uras, G; Zhang, P; Xu, S; Yin, Y; Liu, J; Qin, S; Li, X; Allen, S; Bai, R; Gong, Q; Zhang, H; Zhu, Z; Xu, J 6/10/2021 3/5/2023 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 51440962 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 43 ChEMBL 10.1016/j.ejmech.2021.113827 10.7270/Q2222ZP7 34530383 Ip, FCF; Fu, G; Yang, F; Kang, F; Sun, P; Ling, CY; Cheung, K; Xie, F; Hu, Y; Fu, L; Ip, NY 12/15/2021 3/5/2023 The Hong Kong University of Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 51449752 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Mus musculus 6.2 ChEMBL 10.1016/j.ejmech.2021.114045 10.7270/Q29K4G4C 34922191 Li, X; Li, J; Huang, Y; Gong, Q; Fu, Y; Xu, Y; Huang, J; You, H; Zhang, D; Zhang, D; Mao, F; Zhu, J; Wang, H; Zhang, H; Li, J 2/5/2022 3/7/2023 East China University of Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 51449893 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 7.4 ChEMBL 10.1016/j.ejmech.2021.114045 10.7270/Q29K4G4C 34922191 Li, X; Li, J; Huang, Y; Gong, Q; Fu, Y; Xu, Y; Huang, J; You, H; Zhang, D; Zhang, D; Mao, F; Zhu, J; Wang, H; Zhang, H; Li, J 2/5/2022 3/7/2023 East China University of Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51451290 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 23 ChEMBL 10.1021/acs.jmedchem.1c01784 10.7270/Q2BG2SWG 35195417 Rullo, M; Cipolloni, M; Catto, M; Colliva, C; Miniero, DV; Latronico, T; de Candia, M; Benicchi, T; Linusson, A; Giacchè, N; Altomare, CD; Pisani, L 3/10/2022 3/7/2023 University of Bari "Aldo Moro http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51460755 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 17 ChEMBL 10.7270/Q2BV7MK2 35923722 Paolino, M; Rullo, M; Maramai, S; de Candia, M; Pisani, L; Catto, M; Mugnaini, C; Brizzi, A; Cappelli, A; Olivucci, M; Corelli, F; Altomare, CD 7/20/2022 6/18/2023 Universit� http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51462461 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 87.0 ChEMBL 10.7270/Q2J67MWD 36561075 Machado, V; Cenci, AR; Teixeira, KF; Sens, L; Tizziani, T; Nunes, RJ; Ferreira, LLG; Yunes, RA; Sandjo, LP; Andricopulo, AD; de Oliveira, AS 12/14/2022 6/19/2023 Federal University of Santa Catarina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51470085 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 60 ChEMBL 10.7270/Q2J38XKF 36084304 Turgutalp, B; Bhattarai, P; Ercetin, T; Luise, C; Reis, R; Gurdal, EE; Isaak, A; Biriken, D; Dinter, E; Sipahi, H; Schepmann, D; Junker, A; Wünsch, B; Sippl, W; Gulcan, HO; Kizil, C; Yarim, M 9/22/2022 6/20/2023 Yeditepe University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51471672 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 17 ChEMBL 10.7270/Q2JS9VF3 35462163 Brunetti, L; Leuci, R; Carrieri, A; Catto, M; Occhineri, S; Vinci, G; Gambacorta, L; Baltrukevich, H; Chaves, S; Laghezza, A; Altomare, CD; Tortorella, P; Santos, MA; Loiodice, F; Piemontese, L 7/5/2022 6/21/2023 University of Bari Aldo Moro http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51475772 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 4.0 ChEMBL 10.7270/Q2445RHZ 35276424 Fantacuzzi, M; Amoroso, R; Carradori, S; De Filippis, B 4/5/2022 6/21/2023 "G. D'Annunzio" University of Chieti-Pescara http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51483469 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 59 ChEMBL 10.7270/Q2BP06TV 34743062 Sheng, K; Song, Y; Lei, F; Zhao, W; Fan, L; Wu, L; Liu, Y; Wu, S; Zhang, Y 1/5/2022 6/22/2023 Northwest University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51497993 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 54 ChEMBL 10.7270/Q2445RKV 35101650 Waly, OM; Saad, KM; El-Subbagh, HI; Bayomi, SM; Ghaly, MA 3/5/2022 6/24/2023 Mansoura University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51500709 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Mus musculus 5.4 ChEMBL 10.7270/Q26M3BX2 35339839 Liu, Y; Uras, G; Onuwaje, I; Li, W; Yao, H; Xu, S; Li, X; Li, X; Phillips, J; Allen, S; Gong, Q; Zhang, H; Zhu, Z; Liu, J; Xu, J 5/5/2022 6/25/2023 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 51517021 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 32 ChEMBL 10.7270/Q2F19402 33984802 Ferreira, JPS; Albuquerque, HMT; Cardoso, SM; Silva, AMS; Silva, VLM 10/5/2021 4/21/2024 University of Aveiro http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51521399 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 44 ChEMBL 10.7270/Q2BP071Z 36223681 Wang, Y; Xiong, B; Lin, H; Li, Q; Yang, H; Qiao, Y; Li, Q; Xu, Z; Lyu, W; Qu, W; Liu, W; Chen, Y; Feng, F; Sun, H 12/15/2022 4/21/2024 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51521597 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 198000 ChEMBL 10.7270/Q2SN0F6C 36257284 Li, X; Li, T; Zhang, P; Li, X; Lu, L; Sun, Y; Zhang, B; Allen, S; White, L; Phillips, J; Zhu, Z; Yao, H; Xu, J 12/15/2022 4/21/2024 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51526387 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 16 ChEMBL 10.7270/Q2FR01VV 37003157 Asproni, B; Catto, M; Loriga, G; Murineddu, G; Corona, P; Purgatorio, R; Cichero, E; Fossa, P; Scarano, N; Martínez, AL; Brea, J; Pinna, GA 4/15/2023 4/22/2024 University of Sassari http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51543171 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 17 ChEMBL 10.7270/Q2TT4W9N 36753881 Tonelli, M; Catto, M; Sabaté, R; Francesconi, V; Laurini, E; Pricl, S; Pisani, L; Miniero, DV; Liuzzi, GM; Gatta, E; Relini, A; Gavín, R; Del Rio, JA; Sparatore, F; Carotti, A 3/15/2023 12/15/2024 University of Genoa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51544452 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 3.9 ChEMBL 10.7270/Q2J67N96 38516603 Ţînţaş, ML; Peauger, L; Barré, A; Papamicaël, C; Besson, T; Sopkovà-de Oliveira Santos, J; Gembus, V; Levacher, V 3/20/2024 12/16/2024 University of Rouen Normandy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51548103 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 21 ChEMBL 10.7270/Q20R9TSV 35987018 Guo, J; Cheng, M; Liu, P; Cao, D; Luo, J; Wan, Y; Fang, Y; Jin, Y; Xie, SS; Liu, J 11/15/2022 12/17/2024 Jiangxi University of Chinese Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51555187 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 80 ChEMBL 10.7270/Q24F1W48 38008338 Nguyen, HT; Tuan, AN; Thi, TAD; Van, KT; Le-Nhat-Thuy, G; Thi, PH; Thi, QGN; Thi, CB; Quang, HT; Van Nguyen, T 1/15/2024 12/18/2024 Vietnam Academy of Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51555781 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 79 ChEMBL 10.7270/Q2Q244NH 38283217 Pourtaher, H; Mohammadi, Y; Hasaninejad, A; Iraji, A 1/25/2024 12/18/2024 Persian Gulf University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50252493 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 93000 ChEMBL 10.1016/j.bmcl.2014.10.055 10.7270/Q28G8N9V 25453812 Wei, Z; Liu, YQ; Zhou, XB; Luo, Y; Huang, CQ; Wang, YA; Zheng, ZB; Li, S 12/3/2014 3/15/2016 Institute of Pharmacology and Toxicology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50252498 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 27000 ChEMBL 10.1016/j.bmcl.2014.10.055 10.7270/Q28G8N9V 25453812 Wei, Z; Liu, YQ; Zhou, XB; Luo, Y; Huang, CQ; Wang, YA; Zheng, ZB; Li, S 12/3/2014 3/15/2016 Institute of Pharmacology and Toxicology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50252520 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 1360000 ChEMBL 10.1016/j.bmcl.2014.10.055 10.7270/Q28G8N9V 25453812 Wei, Z; Liu, YQ; Zhou, XB; Luo, Y; Huang, CQ; Wang, YA; Zheng, ZB; Li, S 12/3/2014 3/15/2016 Institute of Pharmacology and Toxicology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50832331 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 15000 ChEMBL 10.1016/j.bmc.2017.06.041 10.7270/Q2SJ1P2T 28684009 Wei, Z; Liu, YQ; Wang, SZ; Yao, L; Nie, HF; Wang, YA; Liu, XY; Zheng, ZB; Li, S 8/15/2017 1/12/2020 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50832338 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 234000 ChEMBL 10.1016/j.bmc.2017.06.041 10.7270/Q2SJ1P2T 28684009 Wei, Z; Liu, YQ; Wang, SZ; Yao, L; Nie, HF; Wang, YA; Liu, XY; Zheng, ZB; Li, S 8/15/2017 1/12/2020 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50832469 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 667800 ChEMBL 10.1016/j.bmc.2017.06.041 10.7270/Q2SJ1P2T 28684009 Wei, Z; Liu, YQ; Wang, SZ; Yao, L; Nie, HF; Wang, YA; Liu, XY; Zheng, ZB; Li, S 8/15/2017 1/12/2020 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51394264 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 636000 ChEMBL 10.1016/j.ejmech.2021.113286 10.7270/Q2ZP49VN 33611189 Wei, Z; Yang, J; Liu, Y; Nie, H; Yao, L; Yang, J; Guo, L; Zheng, Z; Ouyang, Q 4/5/2021 3/29/2022 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51394283 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 60300 ChEMBL 10.1016/j.ejmech.2021.113286 10.7270/Q2ZP49VN 33611189 Wei, Z; Yang, J; Liu, Y; Nie, H; Yao, L; Yang, J; Guo, L; Zheng, Z; Ouyang, Q 4/5/2021 3/29/2022 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51394291 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 29300 ChEMBL 10.1016/j.ejmech.2021.113286 10.7270/Q2ZP49VN 33611189 Wei, Z; Yang, J; Liu, Y; Nie, H; Yao, L; Yang, J; Guo, L; Zheng, Z; Ouyang, Q 4/5/2021 3/29/2022 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50252493 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 93000 ChEMBL 10.1016/j.bmcl.2014.10.055 10.7270/Q28G8N9V 25453812 Wei, Z; Liu, YQ; Zhou, XB; Luo, Y; Huang, CQ; Wang, YA; Zheng, ZB; Li, S 12/3/2014 3/15/2016 Institute of Pharmacology and Toxicology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50252498 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 27000 ChEMBL 10.1016/j.bmcl.2014.10.055 10.7270/Q28G8N9V 25453812 Wei, Z; Liu, YQ; Zhou, XB; Luo, Y; Huang, CQ; Wang, YA; Zheng, ZB; Li, S 12/3/2014 3/15/2016 Institute of Pharmacology and Toxicology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50252520 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 1360000 ChEMBL 10.1016/j.bmcl.2014.10.055 10.7270/Q28G8N9V 25453812 Wei, Z; Liu, YQ; Zhou, XB; Luo, Y; Huang, CQ; Wang, YA; Zheng, ZB; Li, S 12/3/2014 3/15/2016 Institute of Pharmacology and Toxicology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50832331 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 15000 ChEMBL 10.1016/j.bmc.2017.06.041 10.7270/Q2SJ1P2T 28684009 Wei, Z; Liu, YQ; Wang, SZ; Yao, L; Nie, HF; Wang, YA; Liu, XY; Zheng, ZB; Li, S 8/15/2017 1/12/2020 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50832338 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 234000 ChEMBL 10.1016/j.bmc.2017.06.041 10.7270/Q2SJ1P2T 28684009 Wei, Z; Liu, YQ; Wang, SZ; Yao, L; Nie, HF; Wang, YA; Liu, XY; Zheng, ZB; Li, S 8/15/2017 1/12/2020 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50832469 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 667800 ChEMBL 10.1016/j.bmc.2017.06.041 10.7270/Q2SJ1P2T 28684009 Wei, Z; Liu, YQ; Wang, SZ; Yao, L; Nie, HF; Wang, YA; Liu, XY; Zheng, ZB; Li, S 8/15/2017 1/12/2020 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51394264 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 636000 ChEMBL 10.1016/j.ejmech.2021.113286 10.7270/Q2ZP49VN 33611189 Wei, Z; Yang, J; Liu, Y; Nie, H; Yao, L; Yang, J; Guo, L; Zheng, Z; Ouyang, Q 4/5/2021 3/29/2022 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51394283 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 60300 ChEMBL 10.1016/j.ejmech.2021.113286 10.7270/Q2ZP49VN 33611189 Wei, Z; Yang, J; Liu, Y; Nie, H; Yao, L; Yang, J; Guo, L; Zheng, Z; Ouyang, Q 4/5/2021 3/29/2022 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51394291 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 29300 ChEMBL 10.1016/j.ejmech.2021.113286 10.7270/Q2ZP49VN 33611189 Wei, Z; Yang, J; Liu, Y; Nie, H; Yao, L; Yang, J; Guo, L; Zheng, Z; Ouyang, Q 4/5/2021 3/29/2022 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50252493 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 93000 ChEMBL 10.1016/j.bmcl.2014.10.055 10.7270/Q28G8N9V 25453812 Wei, Z; Liu, YQ; Zhou, XB; Luo, Y; Huang, CQ; Wang, YA; Zheng, ZB; Li, S 12/3/2014 3/15/2016 Institute of Pharmacology and Toxicology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50252498 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 27000 ChEMBL 10.1016/j.bmcl.2014.10.055 10.7270/Q28G8N9V 25453812 Wei, Z; Liu, YQ; Zhou, XB; Luo, Y; Huang, CQ; Wang, YA; Zheng, ZB; Li, S 12/3/2014 3/15/2016 Institute of Pharmacology and Toxicology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50252520 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 1360000 ChEMBL 10.1016/j.bmcl.2014.10.055 10.7270/Q28G8N9V 25453812 Wei, Z; Liu, YQ; Zhou, XB; Luo, Y; Huang, CQ; Wang, YA; Zheng, ZB; Li, S 12/3/2014 3/15/2016 Institute of Pharmacology and Toxicology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50832331 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 15000 ChEMBL 10.1016/j.bmc.2017.06.041 10.7270/Q2SJ1P2T 28684009 Wei, Z; Liu, YQ; Wang, SZ; Yao, L; Nie, HF; Wang, YA; Liu, XY; Zheng, ZB; Li, S 8/15/2017 1/12/2020 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50832338 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 234000 ChEMBL 10.1016/j.bmc.2017.06.041 10.7270/Q2SJ1P2T 28684009 Wei, Z; Liu, YQ; Wang, SZ; Yao, L; Nie, HF; Wang, YA; Liu, XY; Zheng, ZB; Li, S 8/15/2017 1/12/2020 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50832469 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 667800 ChEMBL 10.1016/j.bmc.2017.06.041 10.7270/Q2SJ1P2T 28684009 Wei, Z; Liu, YQ; Wang, SZ; Yao, L; Nie, HF; Wang, YA; Liu, XY; Zheng, ZB; Li, S 8/15/2017 1/12/2020 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51394264 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 636000 ChEMBL 10.1016/j.ejmech.2021.113286 10.7270/Q2ZP49VN 33611189 Wei, Z; Yang, J; Liu, Y; Nie, H; Yao, L; Yang, J; Guo, L; Zheng, Z; Ouyang, Q 4/5/2021 3/29/2022 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51394283 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 60300 ChEMBL 10.1016/j.ejmech.2021.113286 10.7270/Q2ZP49VN 33611189 Wei, Z; Yang, J; Liu, Y; Nie, H; Yao, L; Yang, J; Guo, L; Zheng, Z; Ouyang, Q 4/5/2021 3/29/2022 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51394291 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 29300 ChEMBL 10.1016/j.ejmech.2021.113286 10.7270/Q2ZP49VN 33611189 Wei, Z; Yang, J; Liu, Y; Nie, H; Yao, L; Yang, J; Guo, L; Zheng, Z; Ouyang, Q 4/5/2021 3/29/2022 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51083053 CCN(CC)CCNS(=O)(=O)Cc1ccc(cc1)C(F)(F)F InChI=1S/C14H21F3N2O2S/c1-3-19(4-2)10-9-18-22(20,21)11-12-5-7-13(8-6-12)14(15,16)17/h5-8,18H,3-4,9-11H2,1-2H3 UJMFKSSVUDLNIV-UHFFFAOYSA-N 50443029 CHEMBL3087809 Acetylcholinesterase Mus musculus 9200 ChEMBL 10.1021/jm400990p 10.7270/Q24M95Z3 23984975 Andersson, CD; Forsgren, N; Akfur, C; Allgardsson, A; Berg, L; Engdahl, C; Qian, W; Ekstrom, F; Linusson, A 10/10/2013 7/25/2014 Ume£ http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50443029 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50443029&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search N2K 6TD2 72704498 194940925 CHEMBL3087809 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 51083073 CCN(CC)CCNS(=O)(=O)Cc1ccc(cc1)C(F)(F)F InChI=1S/C14H21F3N2O2S/c1-3-19(4-2)10-9-18-22(20,21)11-12-5-7-13(8-6-12)14(15,16)17/h5-8,18H,3-4,9-11H2,1-2H3 UJMFKSSVUDLNIV-UHFFFAOYSA-N 50443029 CHEMBL3087809 Acetylcholinesterase Mus musculus 12000 ChEMBL 10.1021/jm400990p 10.7270/Q24M95Z3 23984975 Andersson, CD; Forsgren, N; Akfur, C; Allgardsson, A; Berg, L; Engdahl, C; Qian, W; Ekstrom, F; Linusson, A 10/10/2013 7/25/2014 Ume£ http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50443029 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50443029&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search N2K 6TD2 72704498 194940925 CHEMBL3087809 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 17749 C[N+](C)(CC=C)c1ccc(cc1)CCC(=O)CCc2ccc(cc2)[N+](C)(C)CC=C InChI=1S/C27H38N2O/c1-7-21-28(3,4)25-15-9-23(10-16-25)13-19-27(30)20-14-24-11-17-26(18-12-24)29(5,6)22-8-2/h7-12,15-18H,1-2,13-14,19-22H2,3-6H3/q+2 ZAEXMNKDGJNLTA-UHFFFAOYSA-N 10624 CHEMBL140020::CHEMBL464538::1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide::4-(5-{4-[dimethyl(prop-2-en-1-yl)aminiumyl]phenyl}-3-oxopentyl)-N,N-dimethyl-N-(prop-2-en-1-yl)anilinium dibromide::BW284c51 Acetylcholinesterase Homo sapiens 18 Curated from the literature by BindingDB 10.1021/jm050578p 10.7270/Q2S75DJ6 16570913 aid1796482 Luo, W; Yu, QS; Kulkarni, SS; Parrish, DA; Holloway, HW; Tweedie, D; Shafferman, A; Lahiri, DK; Brossi, A; Greig, NH 4/6/2006 8/13/2006 National Institutes of Health http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10624&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search EBW 6O52,6O50,1E3Q 1338 46511224 CHEMBL464538CHEMBL140020 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50077034 C[N+](C)(CC=C)c1ccc(cc1)CCC(=O)CCc2ccc(cc2)[N+](C)(C)CC=C InChI=1S/C27H38N2O/c1-7-21-28(3,4)25-15-9-23(10-16-25)13-19-27(30)20-14-24-11-17-26(18-12-24)29(5,6)22-8-2/h7-12,15-18H,1-2,13-14,19-22H2,3-6H3/q+2 ZAEXMNKDGJNLTA-UHFFFAOYSA-N 10624 CHEMBL140020::CHEMBL464538::1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide::4-(5-{4-[dimethyl(prop-2-en-1-yl)aminiumyl]phenyl}-3-oxopentyl)-N,N-dimethyl-N-(prop-2-en-1-yl)anilinium dibromide::BW284c51 Acetylcholinesterase Homo sapiens 800 ChEMBL 10.1016/j.bmcl.2013.10.043 10.7270/Q2ZG6TR6 24220173 Komloova, M; Horova, A; Hrabinova, M; Jun, D; Dolezal, M; Vinsova, J; Kuca, K; Musilek, K 12/2/2013 12/26/2014 Charles University In Prague http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10624&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search EBW 1E3Q,6O50,6O52 1338 46511224 CHEMBL464538CHEMBL140020 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50077039 C[N+](C)(CC=C)c1ccc(cc1)CCC(=O)CCc2ccc(cc2)[N+](C)(C)CC=C InChI=1S/C27H38N2O/c1-7-21-28(3,4)25-15-9-23(10-16-25)13-19-27(30)20-14-24-11-17-26(18-12-24)29(5,6)22-8-2/h7-12,15-18H,1-2,13-14,19-22H2,3-6H3/q+2 ZAEXMNKDGJNLTA-UHFFFAOYSA-N 10624 CHEMBL140020::CHEMBL464538::1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide::4-(5-{4-[dimethyl(prop-2-en-1-yl)aminiumyl]phenyl}-3-oxopentyl)-N,N-dimethyl-N-(prop-2-en-1-yl)anilinium dibromide::BW284c51 Acetylcholinesterase Homo sapiens 50 ChEMBL 10.1016/j.bmcl.2013.10.043 10.7270/Q2ZG6TR6 24220173 Komloova, M; Horova, A; Hrabinova, M; Jun, D; Dolezal, M; Vinsova, J; Kuca, K; Musilek, K 12/2/2013 12/26/2014 Charles University In Prague http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10624&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search EBW 1E3Q,6O50,6O52 1338 46511224 CHEMBL464538CHEMBL140020 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50077066 C[N+](C)(CC=C)c1ccc(cc1)CCC(=O)CCc2ccc(cc2)[N+](C)(C)CC=C InChI=1S/C27H38N2O/c1-7-21-28(3,4)25-15-9-23(10-16-25)13-19-27(30)20-14-24-11-17-26(18-12-24)29(5,6)22-8-2/h7-12,15-18H,1-2,13-14,19-22H2,3-6H3/q+2 ZAEXMNKDGJNLTA-UHFFFAOYSA-N 10624 CHEMBL140020::CHEMBL464538::1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide::4-(5-{4-[dimethyl(prop-2-en-1-yl)aminiumyl]phenyl}-3-oxopentyl)-N,N-dimethyl-N-(prop-2-en-1-yl)anilinium dibromide::BW284c51 Acetylcholinesterase Homo sapiens 30 ChEMBL 10.1016/j.bmcl.2013.10.043 10.7270/Q2ZG6TR6 24220173 Komloova, M; Horova, A; Hrabinova, M; Jun, D; Dolezal, M; Vinsova, J; Kuca, K; Musilek, K 12/2/2013 12/26/2014 Charles University In Prague http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10624&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search EBW 1E3Q,6O50,6O52 1338 46511224 CHEMBL464538CHEMBL140020 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50420945 C[N+](C)(CC=C)c1ccc(cc1)CCC(=O)CCc2ccc(cc2)[N+](C)(C)CC=C InChI=1S/C27H38N2O/c1-7-21-28(3,4)25-15-9-23(10-16-25)13-19-27(30)20-14-24-11-17-26(18-12-24)29(5,6)22-8-2/h7-12,15-18H,1-2,13-14,19-22H2,3-6H3/q+2 ZAEXMNKDGJNLTA-UHFFFAOYSA-N 10624 CHEMBL140020::CHEMBL464538::1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide::4-(5-{4-[dimethyl(prop-2-en-1-yl)aminiumyl]phenyl}-3-oxopentyl)-N,N-dimethyl-N-(prop-2-en-1-yl)anilinium dibromide::BW284c51 Acetylcholinesterase Bos taurus 8 ChEMBL 10.1016/j.bmc.2008.06.022 10.7270/Q2NC611F 18585045 Leonetti, F; Catto, M; Nicolotti, O; Pisani, L; Cappa, A; Stefanachi, A; Carotti, A 8/11/2008 1/11/2010 Università http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10624&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search EBW 1E3Q,6O50,6O52 1338 46511224 CHEMBL464538CHEMBL140020 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 50621497 C[N+](C)(CC=C)c1ccc(cc1)CCC(=O)CCc2ccc(cc2)[N+](C)(C)CC=C InChI=1S/C27H38N2O/c1-7-21-28(3,4)25-15-9-23(10-16-25)13-19-27(30)20-14-24-11-17-26(18-12-24)29(5,6)22-8-2/h7-12,15-18H,1-2,13-14,19-22H2,3-6H3/q+2 ZAEXMNKDGJNLTA-UHFFFAOYSA-N 10624 CHEMBL140020::CHEMBL464538::1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide::4-(5-{4-[dimethyl(prop-2-en-1-yl)aminiumyl]phenyl}-3-oxopentyl)-N,N-dimethyl-N-(prop-2-en-1-yl)anilinium dibromide::BW284c51 Acetylcholinesterase Homo sapiens 30 ChEMBL 10.1016/j.ejmech.2010.12.011 10.7270/Q2PR7W8D 21236521 Musilek, K; Komloova, M; Holas, O; Hrabinova, M; Pohanka, M; Dohnal, V; Nachon, F; Dolezal, M; Kuca, K 1/25/2011 8/23/2011 University of Defence http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10624&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search EBW 1E3Q,6O50,6O52 1338 46511224 CHEMBL464538CHEMBL140020 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50621526 C[N+](C)(CC=C)c1ccc(cc1)CCC(=O)CCc2ccc(cc2)[N+](C)(C)CC=C InChI=1S/C27H38N2O/c1-7-21-28(3,4)25-15-9-23(10-16-25)13-19-27(30)20-14-24-11-17-26(18-12-24)29(5,6)22-8-2/h7-12,15-18H,1-2,13-14,19-22H2,3-6H3/q+2 ZAEXMNKDGJNLTA-UHFFFAOYSA-N 10624 CHEMBL140020::CHEMBL464538::1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide::4-(5-{4-[dimethyl(prop-2-en-1-yl)aminiumyl]phenyl}-3-oxopentyl)-N,N-dimethyl-N-(prop-2-en-1-yl)anilinium dibromide::BW284c51 Acetylcholinesterase Homo sapiens 10 ChEMBL 10.1016/j.ejmech.2010.12.011 10.7270/Q2PR7W8D 21236521 Musilek, K; Komloova, M; Holas, O; Hrabinova, M; Pohanka, M; Dohnal, V; Nachon, F; Dolezal, M; Kuca, K 1/25/2011 8/23/2011 University of Defence http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10624&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search EBW 1E3Q,6O50,6O52 1338 46511224 CHEMBL464538CHEMBL140020 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50621531 C[N+](C)(CC=C)c1ccc(cc1)CCC(=O)CCc2ccc(cc2)[N+](C)(C)CC=C InChI=1S/C27H38N2O/c1-7-21-28(3,4)25-15-9-23(10-16-25)13-19-27(30)20-14-24-11-17-26(18-12-24)29(5,6)22-8-2/h7-12,15-18H,1-2,13-14,19-22H2,3-6H3/q+2 ZAEXMNKDGJNLTA-UHFFFAOYSA-N 10624 CHEMBL140020::CHEMBL464538::1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide::4-(5-{4-[dimethyl(prop-2-en-1-yl)aminiumyl]phenyl}-3-oxopentyl)-N,N-dimethyl-N-(prop-2-en-1-yl)anilinium dibromide::BW284c51 Acetylcholinesterase Homo sapiens 50 ChEMBL 10.1016/j.ejmech.2010.12.011 10.7270/Q2PR7W8D 21236521 Musilek, K; Komloova, M; Holas, O; Hrabinova, M; Pohanka, M; Dohnal, V; Nachon, F; Dolezal, M; Kuca, K 1/25/2011 8/23/2011 University of Defence http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10624&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search EBW 1E3Q,6O50,6O52 1338 46511224 CHEMBL464538CHEMBL140020 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50630030 C[N+](C)(CC=C)c1ccc(cc1)CCC(=O)CCc2ccc(cc2)[N+](C)(C)CC=C InChI=1S/C27H38N2O/c1-7-21-28(3,4)25-15-9-23(10-16-25)13-19-27(30)20-14-24-11-17-26(18-12-24)29(5,6)22-8-2/h7-12,15-18H,1-2,13-14,19-22H2,3-6H3/q+2 ZAEXMNKDGJNLTA-UHFFFAOYSA-N 10624 CHEMBL140020::CHEMBL464538::1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide::4-(5-{4-[dimethyl(prop-2-en-1-yl)aminiumyl]phenyl}-3-oxopentyl)-N,N-dimethyl-N-(prop-2-en-1-yl)anilinium dibromide::BW284c51 Acetylcholinesterase Homo sapiens 10 ChEMBL 10.1016/j.bmcl.2011.02.047 10.7270/Q2JW8F6N 21397501 Komloova, M; Musilek, K; Horova, A; Holas, O; Dohnal, V; Gunn-Moore, F; Kuca, K 4/4/2011 12/2/2011 Charles University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10624&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search EBW 1E3Q,6O50,6O52 1338 46511224 CHEMBL464538CHEMBL140020 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50630036 C[N+](C)(CC=C)c1ccc(cc1)CCC(=O)CCc2ccc(cc2)[N+](C)(C)CC=C InChI=1S/C27H38N2O/c1-7-21-28(3,4)25-15-9-23(10-16-25)13-19-27(30)20-14-24-11-17-26(18-12-24)29(5,6)22-8-2/h7-12,15-18H,1-2,13-14,19-22H2,3-6H3/q+2 ZAEXMNKDGJNLTA-UHFFFAOYSA-N 10624 CHEMBL140020::CHEMBL464538::1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide::4-(5-{4-[dimethyl(prop-2-en-1-yl)aminiumyl]phenyl}-3-oxopentyl)-N,N-dimethyl-N-(prop-2-en-1-yl)anilinium dibromide::BW284c51 Acetylcholinesterase Homo sapiens 50 ChEMBL 10.1016/j.bmcl.2011.02.047 10.7270/Q2JW8F6N 21397501 Komloova, M; Musilek, K; Horova, A; Holas, O; Dohnal, V; Gunn-Moore, F; Kuca, K 4/4/2011 12/2/2011 Charles University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10624&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search EBW 1E3Q,6O50,6O52 1338 46511224 CHEMBL464538CHEMBL140020 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50630057 C[N+](C)(CC=C)c1ccc(cc1)CCC(=O)CCc2ccc(cc2)[N+](C)(C)CC=C InChI=1S/C27H38N2O/c1-7-21-28(3,4)25-15-9-23(10-16-25)13-19-27(30)20-14-24-11-17-26(18-12-24)29(5,6)22-8-2/h7-12,15-18H,1-2,13-14,19-22H2,3-6H3/q+2 ZAEXMNKDGJNLTA-UHFFFAOYSA-N 10624 CHEMBL140020::CHEMBL464538::1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide::4-(5-{4-[dimethyl(prop-2-en-1-yl)aminiumyl]phenyl}-3-oxopentyl)-N,N-dimethyl-N-(prop-2-en-1-yl)anilinium dibromide::BW284c51 Acetylcholinesterase Homo sapiens 30 ChEMBL 10.1016/j.bmcl.2011.02.047 10.7270/Q2JW8F6N 21397501 Komloova, M; Musilek, K; Horova, A; Holas, O; Dohnal, V; Gunn-Moore, F; Kuca, K 4/4/2011 12/2/2011 Charles University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10624&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search EBW 1E3Q,6O50,6O52 1338 46511224 CHEMBL464538CHEMBL140020 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50779141 C[N+](C)(CC=C)c1ccc(cc1)CCC(=O)CCc2ccc(cc2)[N+](C)(C)CC=C InChI=1S/C27H38N2O/c1-7-21-28(3,4)25-15-9-23(10-16-25)13-19-27(30)20-14-24-11-17-26(18-12-24)29(5,6)22-8-2/h7-12,15-18H,1-2,13-14,19-22H2,3-6H3/q+2 ZAEXMNKDGJNLTA-UHFFFAOYSA-N 10624 CHEMBL140020::CHEMBL464538::1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide::4-(5-{4-[dimethyl(prop-2-en-1-yl)aminiumyl]phenyl}-3-oxopentyl)-N,N-dimethyl-N-(prop-2-en-1-yl)anilinium dibromide::BW284c51 Acetylcholinesterase Homo sapiens 8 ChEMBL 10.1021/jm950771r 10.7270/Q2PZ59GC 8978837 Cho, SJ; Garsia, ML; Bier, J; Tropsha, A 1/24/1997 11/3/2012 University of North Carolina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10624&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search EBW 1E3Q,6O50,6O52 1338 46511224 CHEMBL464538CHEMBL140020 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50871593 C[N+](C)(CC=C)c1ccc(cc1)CCC(=O)CCc2ccc(cc2)[N+](C)(C)CC=C InChI=1S/C27H38N2O/c1-7-21-28(3,4)25-15-9-23(10-16-25)13-19-27(30)20-14-24-11-17-26(18-12-24)29(5,6)22-8-2/h7-12,15-18H,1-2,13-14,19-22H2,3-6H3/q+2 ZAEXMNKDGJNLTA-UHFFFAOYSA-N 10624 CHEMBL140020::CHEMBL464538::1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide::4-(5-{4-[dimethyl(prop-2-en-1-yl)aminiumyl]phenyl}-3-oxopentyl)-N,N-dimethyl-N-(prop-2-en-1-yl)anilinium dibromide::BW284c51 Acetylcholinesterase Bos taurus 57 ChEMBL 10.1021/jm701253t 10.7270/Q22Z16D4 18479118 Butini, S; Campiani, G; Borriello, M; Gemma, S; Panico, A; Persico, M; Catalanotti, B; Ros, S; Brindisi, M; Agnusdei, M; Fiorini, I; Nacci, V; Novellino, E; Belinskaya, T; Saxena, A; Fattorusso, C 6/5/2008 12/16/2012 University of Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10624&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search EBW 1E3Q,6O50,6O52 1338 46511224 CHEMBL464538CHEMBL140020 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 50871594 C[N+](C)(CC=C)c1ccc(cc1)CCC(=O)CCc2ccc(cc2)[N+](C)(C)CC=C InChI=1S/C27H38N2O/c1-7-21-28(3,4)25-15-9-23(10-16-25)13-19-27(30)20-14-24-11-17-26(18-12-24)29(5,6)22-8-2/h7-12,15-18H,1-2,13-14,19-22H2,3-6H3/q+2 ZAEXMNKDGJNLTA-UHFFFAOYSA-N 10624 CHEMBL140020::CHEMBL464538::1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide::4-(5-{4-[dimethyl(prop-2-en-1-yl)aminiumyl]phenyl}-3-oxopentyl)-N,N-dimethyl-N-(prop-2-en-1-yl)anilinium dibromide::BW284c51 Acetylcholinesterase Homo sapiens 10 ChEMBL 10.1021/jm701253t 10.7270/Q22Z16D4 18479118 Butini, S; Campiani, G; Borriello, M; Gemma, S; Panico, A; Persico, M; Catalanotti, B; Ros, S; Brindisi, M; Agnusdei, M; Fiorini, I; Nacci, V; Novellino, E; Belinskaya, T; Saxena, A; Fattorusso, C 6/5/2008 12/16/2012 University of Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10624&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search EBW 1E3Q,6O50,6O52 1338 46511224 CHEMBL464538CHEMBL140020 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50919589 C[N+](C)(CC=C)c1ccc(cc1)CCC(=O)CCc2ccc(cc2)[N+](C)(C)CC=C InChI=1S/C27H38N2O/c1-7-21-28(3,4)25-15-9-23(10-16-25)13-19-27(30)20-14-24-11-17-26(18-12-24)29(5,6)22-8-2/h7-12,15-18H,1-2,13-14,19-22H2,3-6H3/q+2 ZAEXMNKDGJNLTA-UHFFFAOYSA-N 10624 CHEMBL140020::CHEMBL464538::1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide::4-(5-{4-[dimethyl(prop-2-en-1-yl)aminiumyl]phenyl}-3-oxopentyl)-N,N-dimethyl-N-(prop-2-en-1-yl)anilinium dibromide::BW284c51 Acetylcholinesterase Homo sapiens 10 ChEMBL 10.1016/j.bmcl.2010.11.051 10.7270/Q2542PK6 21144749 Musilek, K; Roder, J; Komloova, M; Holas, O; Hrabinova, M; Pohanka, M; Dohnal, V; Opletalova, V; Kuca, K; Jung, YS 12/24/2010 1/4/2013 University of Defence http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10624&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search EBW 1E3Q,6O50,6O52 1338 46511224 CHEMBL464538CHEMBL140020 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50919596 C[N+](C)(CC=C)c1ccc(cc1)CCC(=O)CCc2ccc(cc2)[N+](C)(C)CC=C InChI=1S/C27H38N2O/c1-7-21-28(3,4)25-15-9-23(10-16-25)13-19-27(30)20-14-24-11-17-26(18-12-24)29(5,6)22-8-2/h7-12,15-18H,1-2,13-14,19-22H2,3-6H3/q+2 ZAEXMNKDGJNLTA-UHFFFAOYSA-N 10624 CHEMBL140020::CHEMBL464538::1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide::4-(5-{4-[dimethyl(prop-2-en-1-yl)aminiumyl]phenyl}-3-oxopentyl)-N,N-dimethyl-N-(prop-2-en-1-yl)anilinium dibromide::BW284c51 Acetylcholinesterase Homo sapiens 30 ChEMBL 10.1016/j.bmcl.2010.11.051 10.7270/Q2542PK6 21144749 Musilek, K; Roder, J; Komloova, M; Holas, O; Hrabinova, M; Pohanka, M; Dohnal, V; Opletalova, V; Kuca, K; Jung, YS 12/24/2010 1/4/2013 University of Defence http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10624&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search EBW 1E3Q,6O50,6O52 1338 46511224 CHEMBL464538CHEMBL140020 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50995444 C[N+](C)(CC=C)c1ccc(cc1)CCC(=O)CCc2ccc(cc2)[N+](C)(C)CC=C InChI=1S/C27H38N2O/c1-7-21-28(3,4)25-15-9-23(10-16-25)13-19-27(30)20-14-24-11-17-26(18-12-24)29(5,6)22-8-2/h7-12,15-18H,1-2,13-14,19-22H2,3-6H3/q+2 ZAEXMNKDGJNLTA-UHFFFAOYSA-N 10624 CHEMBL140020::CHEMBL464538::1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide::4-(5-{4-[dimethyl(prop-2-en-1-yl)aminiumyl]phenyl}-3-oxopentyl)-N,N-dimethyl-N-(prop-2-en-1-yl)anilinium dibromide::BW284c51 Acetylcholinesterase Homo sapiens 8 ChEMBL 10.1021/jm970488n 10.7270/Q2BZ6784 9435905 So, SS; Karplus, M 2/13/1998 5/20/2013 Harvard University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10624&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search EBW 1E3Q,6O50,6O52 1338 46511224 CHEMBL464538CHEMBL140020 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 17749 C[N+](C)(CC=C)c1ccc(cc1)CCC(=O)CCc2ccc(cc2)[N+](C)(C)CC=C InChI=1S/C27H38N2O/c1-7-21-28(3,4)25-15-9-23(10-16-25)13-19-27(30)20-14-24-11-17-26(18-12-24)29(5,6)22-8-2/h7-12,15-18H,1-2,13-14,19-22H2,3-6H3/q+2 ZAEXMNKDGJNLTA-UHFFFAOYSA-N 10624 CHEMBL140020::CHEMBL464538::1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide::4-(5-{4-[dimethyl(prop-2-en-1-yl)aminiumyl]phenyl}-3-oxopentyl)-N,N-dimethyl-N-(prop-2-en-1-yl)anilinium dibromide::BW284c51 Acetylcholinesterase Homo sapiens 18 Curated from the literature by BindingDB 10.1021/jm050578p 10.7270/Q2S75DJ6 16570913 aid1796482 Luo, W; Yu, QS; Kulkarni, SS; Parrish, DA; Holloway, HW; Tweedie, D; Shafferman, A; Lahiri, DK; Brossi, A; Greig, NH 4/6/2006 8/13/2006 National Institutes of Health http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10624&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search EBW 6O52,6O50,1E3Q 1338 46511224 CHEMBL464538CHEMBL140020 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50077034 C[N+](C)(CC=C)c1ccc(cc1)CCC(=O)CCc2ccc(cc2)[N+](C)(C)CC=C InChI=1S/C27H38N2O/c1-7-21-28(3,4)25-15-9-23(10-16-25)13-19-27(30)20-14-24-11-17-26(18-12-24)29(5,6)22-8-2/h7-12,15-18H,1-2,13-14,19-22H2,3-6H3/q+2 ZAEXMNKDGJNLTA-UHFFFAOYSA-N 10624 CHEMBL140020::CHEMBL464538::1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide::4-(5-{4-[dimethyl(prop-2-en-1-yl)aminiumyl]phenyl}-3-oxopentyl)-N,N-dimethyl-N-(prop-2-en-1-yl)anilinium dibromide::BW284c51 Acetylcholinesterase Homo sapiens 800 ChEMBL 10.1016/j.bmcl.2013.10.043 10.7270/Q2ZG6TR6 24220173 Komloova, M; Horova, A; Hrabinova, M; Jun, D; Dolezal, M; Vinsova, J; Kuca, K; Musilek, K 12/2/2013 12/26/2014 Charles University In Prague http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10624&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search EBW 1E3Q,6O50,6O52 1338 46511224 CHEMBL464538CHEMBL140020 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50077039 C[N+](C)(CC=C)c1ccc(cc1)CCC(=O)CCc2ccc(cc2)[N+](C)(C)CC=C InChI=1S/C27H38N2O/c1-7-21-28(3,4)25-15-9-23(10-16-25)13-19-27(30)20-14-24-11-17-26(18-12-24)29(5,6)22-8-2/h7-12,15-18H,1-2,13-14,19-22H2,3-6H3/q+2 ZAEXMNKDGJNLTA-UHFFFAOYSA-N 10624 CHEMBL140020::CHEMBL464538::1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide::4-(5-{4-[dimethyl(prop-2-en-1-yl)aminiumyl]phenyl}-3-oxopentyl)-N,N-dimethyl-N-(prop-2-en-1-yl)anilinium dibromide::BW284c51 Acetylcholinesterase Homo sapiens 50 ChEMBL 10.1016/j.bmcl.2013.10.043 10.7270/Q2ZG6TR6 24220173 Komloova, M; Horova, A; Hrabinova, M; Jun, D; Dolezal, M; Vinsova, J; Kuca, K; Musilek, K 12/2/2013 12/26/2014 Charles University In Prague http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10624&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search EBW 1E3Q,6O50,6O52 1338 46511224 CHEMBL464538CHEMBL140020 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50077066 C[N+](C)(CC=C)c1ccc(cc1)CCC(=O)CCc2ccc(cc2)[N+](C)(C)CC=C InChI=1S/C27H38N2O/c1-7-21-28(3,4)25-15-9-23(10-16-25)13-19-27(30)20-14-24-11-17-26(18-12-24)29(5,6)22-8-2/h7-12,15-18H,1-2,13-14,19-22H2,3-6H3/q+2 ZAEXMNKDGJNLTA-UHFFFAOYSA-N 10624 CHEMBL140020::CHEMBL464538::1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide::4-(5-{4-[dimethyl(prop-2-en-1-yl)aminiumyl]phenyl}-3-oxopentyl)-N,N-dimethyl-N-(prop-2-en-1-yl)anilinium dibromide::BW284c51 Acetylcholinesterase Homo sapiens 30 ChEMBL 10.1016/j.bmcl.2013.10.043 10.7270/Q2ZG6TR6 24220173 Komloova, M; Horova, A; Hrabinova, M; Jun, D; Dolezal, M; Vinsova, J; Kuca, K; Musilek, K 12/2/2013 12/26/2014 Charles University In Prague http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10624&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search EBW 1E3Q,6O50,6O52 1338 46511224 CHEMBL464538CHEMBL140020 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50420945 C[N+](C)(CC=C)c1ccc(cc1)CCC(=O)CCc2ccc(cc2)[N+](C)(C)CC=C InChI=1S/C27H38N2O/c1-7-21-28(3,4)25-15-9-23(10-16-25)13-19-27(30)20-14-24-11-17-26(18-12-24)29(5,6)22-8-2/h7-12,15-18H,1-2,13-14,19-22H2,3-6H3/q+2 ZAEXMNKDGJNLTA-UHFFFAOYSA-N 10624 CHEMBL140020::CHEMBL464538::1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide::4-(5-{4-[dimethyl(prop-2-en-1-yl)aminiumyl]phenyl}-3-oxopentyl)-N,N-dimethyl-N-(prop-2-en-1-yl)anilinium dibromide::BW284c51 Acetylcholinesterase Bos taurus 8 ChEMBL 10.1016/j.bmc.2008.06.022 10.7270/Q2NC611F 18585045 Leonetti, F; Catto, M; Nicolotti, O; Pisani, L; Cappa, A; Stefanachi, A; Carotti, A 8/11/2008 1/11/2010 Università http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10624&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search EBW 1E3Q,6O50,6O52 1338 46511224 CHEMBL464538CHEMBL140020 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 50621497 C[N+](C)(CC=C)c1ccc(cc1)CCC(=O)CCc2ccc(cc2)[N+](C)(C)CC=C InChI=1S/C27H38N2O/c1-7-21-28(3,4)25-15-9-23(10-16-25)13-19-27(30)20-14-24-11-17-26(18-12-24)29(5,6)22-8-2/h7-12,15-18H,1-2,13-14,19-22H2,3-6H3/q+2 ZAEXMNKDGJNLTA-UHFFFAOYSA-N 10624 CHEMBL140020::CHEMBL464538::1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide::4-(5-{4-[dimethyl(prop-2-en-1-yl)aminiumyl]phenyl}-3-oxopentyl)-N,N-dimethyl-N-(prop-2-en-1-yl)anilinium dibromide::BW284c51 Acetylcholinesterase Homo sapiens 30 ChEMBL 10.1016/j.ejmech.2010.12.011 10.7270/Q2PR7W8D 21236521 Musilek, K; Komloova, M; Holas, O; Hrabinova, M; Pohanka, M; Dohnal, V; Nachon, F; Dolezal, M; Kuca, K 1/25/2011 8/23/2011 University of Defence http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10624&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search EBW 1E3Q,6O50,6O52 1338 46511224 CHEMBL464538CHEMBL140020 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50621526 C[N+](C)(CC=C)c1ccc(cc1)CCC(=O)CCc2ccc(cc2)[N+](C)(C)CC=C InChI=1S/C27H38N2O/c1-7-21-28(3,4)25-15-9-23(10-16-25)13-19-27(30)20-14-24-11-17-26(18-12-24)29(5,6)22-8-2/h7-12,15-18H,1-2,13-14,19-22H2,3-6H3/q+2 ZAEXMNKDGJNLTA-UHFFFAOYSA-N 10624 CHEMBL140020::CHEMBL464538::1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide::4-(5-{4-[dimethyl(prop-2-en-1-yl)aminiumyl]phenyl}-3-oxopentyl)-N,N-dimethyl-N-(prop-2-en-1-yl)anilinium dibromide::BW284c51 Acetylcholinesterase Homo sapiens 10 ChEMBL 10.1016/j.ejmech.2010.12.011 10.7270/Q2PR7W8D 21236521 Musilek, K; Komloova, M; Holas, O; Hrabinova, M; Pohanka, M; Dohnal, V; Nachon, F; Dolezal, M; Kuca, K 1/25/2011 8/23/2011 University of Defence http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10624&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search EBW 1E3Q,6O50,6O52 1338 46511224 CHEMBL464538CHEMBL140020 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50621531 C[N+](C)(CC=C)c1ccc(cc1)CCC(=O)CCc2ccc(cc2)[N+](C)(C)CC=C InChI=1S/C27H38N2O/c1-7-21-28(3,4)25-15-9-23(10-16-25)13-19-27(30)20-14-24-11-17-26(18-12-24)29(5,6)22-8-2/h7-12,15-18H,1-2,13-14,19-22H2,3-6H3/q+2 ZAEXMNKDGJNLTA-UHFFFAOYSA-N 10624 CHEMBL140020::CHEMBL464538::1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide::4-(5-{4-[dimethyl(prop-2-en-1-yl)aminiumyl]phenyl}-3-oxopentyl)-N,N-dimethyl-N-(prop-2-en-1-yl)anilinium dibromide::BW284c51 Acetylcholinesterase Homo sapiens 50 ChEMBL 10.1016/j.ejmech.2010.12.011 10.7270/Q2PR7W8D 21236521 Musilek, K; Komloova, M; Holas, O; Hrabinova, M; Pohanka, M; Dohnal, V; Nachon, F; Dolezal, M; Kuca, K 1/25/2011 8/23/2011 University of Defence http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10624&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search EBW 1E3Q,6O50,6O52 1338 46511224 CHEMBL464538CHEMBL140020 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50630030 C[N+](C)(CC=C)c1ccc(cc1)CCC(=O)CCc2ccc(cc2)[N+](C)(C)CC=C InChI=1S/C27H38N2O/c1-7-21-28(3,4)25-15-9-23(10-16-25)13-19-27(30)20-14-24-11-17-26(18-12-24)29(5,6)22-8-2/h7-12,15-18H,1-2,13-14,19-22H2,3-6H3/q+2 ZAEXMNKDGJNLTA-UHFFFAOYSA-N 10624 CHEMBL140020::CHEMBL464538::1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide::4-(5-{4-[dimethyl(prop-2-en-1-yl)aminiumyl]phenyl}-3-oxopentyl)-N,N-dimethyl-N-(prop-2-en-1-yl)anilinium dibromide::BW284c51 Acetylcholinesterase Homo sapiens 10 ChEMBL 10.1016/j.bmcl.2011.02.047 10.7270/Q2JW8F6N 21397501 Komloova, M; Musilek, K; Horova, A; Holas, O; Dohnal, V; Gunn-Moore, F; Kuca, K 4/4/2011 12/2/2011 Charles University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10624&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search EBW 1E3Q,6O50,6O52 1338 46511224 CHEMBL464538CHEMBL140020 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50630036 C[N+](C)(CC=C)c1ccc(cc1)CCC(=O)CCc2ccc(cc2)[N+](C)(C)CC=C InChI=1S/C27H38N2O/c1-7-21-28(3,4)25-15-9-23(10-16-25)13-19-27(30)20-14-24-11-17-26(18-12-24)29(5,6)22-8-2/h7-12,15-18H,1-2,13-14,19-22H2,3-6H3/q+2 ZAEXMNKDGJNLTA-UHFFFAOYSA-N 10624 CHEMBL140020::CHEMBL464538::1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide::4-(5-{4-[dimethyl(prop-2-en-1-yl)aminiumyl]phenyl}-3-oxopentyl)-N,N-dimethyl-N-(prop-2-en-1-yl)anilinium dibromide::BW284c51 Acetylcholinesterase Homo sapiens 50 ChEMBL 10.1016/j.bmcl.2011.02.047 10.7270/Q2JW8F6N 21397501 Komloova, M; Musilek, K; Horova, A; Holas, O; Dohnal, V; Gunn-Moore, F; Kuca, K 4/4/2011 12/2/2011 Charles University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10624&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search EBW 1E3Q,6O50,6O52 1338 46511224 CHEMBL464538CHEMBL140020 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50630057 C[N+](C)(CC=C)c1ccc(cc1)CCC(=O)CCc2ccc(cc2)[N+](C)(C)CC=C InChI=1S/C27H38N2O/c1-7-21-28(3,4)25-15-9-23(10-16-25)13-19-27(30)20-14-24-11-17-26(18-12-24)29(5,6)22-8-2/h7-12,15-18H,1-2,13-14,19-22H2,3-6H3/q+2 ZAEXMNKDGJNLTA-UHFFFAOYSA-N 10624 CHEMBL140020::CHEMBL464538::1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide::4-(5-{4-[dimethyl(prop-2-en-1-yl)aminiumyl]phenyl}-3-oxopentyl)-N,N-dimethyl-N-(prop-2-en-1-yl)anilinium dibromide::BW284c51 Acetylcholinesterase Homo sapiens 30 ChEMBL 10.1016/j.bmcl.2011.02.047 10.7270/Q2JW8F6N 21397501 Komloova, M; Musilek, K; Horova, A; Holas, O; Dohnal, V; Gunn-Moore, F; Kuca, K 4/4/2011 12/2/2011 Charles University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10624&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search EBW 1E3Q,6O50,6O52 1338 46511224 CHEMBL464538CHEMBL140020 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50779141 C[N+](C)(CC=C)c1ccc(cc1)CCC(=O)CCc2ccc(cc2)[N+](C)(C)CC=C InChI=1S/C27H38N2O/c1-7-21-28(3,4)25-15-9-23(10-16-25)13-19-27(30)20-14-24-11-17-26(18-12-24)29(5,6)22-8-2/h7-12,15-18H,1-2,13-14,19-22H2,3-6H3/q+2 ZAEXMNKDGJNLTA-UHFFFAOYSA-N 10624 CHEMBL140020::CHEMBL464538::1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide::4-(5-{4-[dimethyl(prop-2-en-1-yl)aminiumyl]phenyl}-3-oxopentyl)-N,N-dimethyl-N-(prop-2-en-1-yl)anilinium dibromide::BW284c51 Acetylcholinesterase Homo sapiens 8 ChEMBL 10.1021/jm950771r 10.7270/Q2PZ59GC 8978837 Cho, SJ; Garsia, ML; Bier, J; Tropsha, A 1/24/1997 11/3/2012 University of North Carolina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10624&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search EBW 1E3Q,6O50,6O52 1338 46511224 CHEMBL464538CHEMBL140020 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50871593 C[N+](C)(CC=C)c1ccc(cc1)CCC(=O)CCc2ccc(cc2)[N+](C)(C)CC=C InChI=1S/C27H38N2O/c1-7-21-28(3,4)25-15-9-23(10-16-25)13-19-27(30)20-14-24-11-17-26(18-12-24)29(5,6)22-8-2/h7-12,15-18H,1-2,13-14,19-22H2,3-6H3/q+2 ZAEXMNKDGJNLTA-UHFFFAOYSA-N 10624 CHEMBL140020::CHEMBL464538::1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide::4-(5-{4-[dimethyl(prop-2-en-1-yl)aminiumyl]phenyl}-3-oxopentyl)-N,N-dimethyl-N-(prop-2-en-1-yl)anilinium dibromide::BW284c51 Acetylcholinesterase Bos taurus 57 ChEMBL 10.1021/jm701253t 10.7270/Q22Z16D4 18479118 Butini, S; Campiani, G; Borriello, M; Gemma, S; Panico, A; Persico, M; Catalanotti, B; Ros, S; Brindisi, M; Agnusdei, M; Fiorini, I; Nacci, V; Novellino, E; Belinskaya, T; Saxena, A; Fattorusso, C 6/5/2008 12/16/2012 University of Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10624&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search EBW 1E3Q,6O50,6O52 1338 46511224 CHEMBL464538CHEMBL140020 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 50871594 C[N+](C)(CC=C)c1ccc(cc1)CCC(=O)CCc2ccc(cc2)[N+](C)(C)CC=C InChI=1S/C27H38N2O/c1-7-21-28(3,4)25-15-9-23(10-16-25)13-19-27(30)20-14-24-11-17-26(18-12-24)29(5,6)22-8-2/h7-12,15-18H,1-2,13-14,19-22H2,3-6H3/q+2 ZAEXMNKDGJNLTA-UHFFFAOYSA-N 10624 CHEMBL140020::CHEMBL464538::1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide::4-(5-{4-[dimethyl(prop-2-en-1-yl)aminiumyl]phenyl}-3-oxopentyl)-N,N-dimethyl-N-(prop-2-en-1-yl)anilinium dibromide::BW284c51 Acetylcholinesterase Homo sapiens 10 ChEMBL 10.1021/jm701253t 10.7270/Q22Z16D4 18479118 Butini, S; Campiani, G; Borriello, M; Gemma, S; Panico, A; Persico, M; Catalanotti, B; Ros, S; Brindisi, M; Agnusdei, M; Fiorini, I; Nacci, V; Novellino, E; Belinskaya, T; Saxena, A; Fattorusso, C 6/5/2008 12/16/2012 University of Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10624&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search EBW 1E3Q,6O50,6O52 1338 46511224 CHEMBL464538CHEMBL140020 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50919589 C[N+](C)(CC=C)c1ccc(cc1)CCC(=O)CCc2ccc(cc2)[N+](C)(C)CC=C InChI=1S/C27H38N2O/c1-7-21-28(3,4)25-15-9-23(10-16-25)13-19-27(30)20-14-24-11-17-26(18-12-24)29(5,6)22-8-2/h7-12,15-18H,1-2,13-14,19-22H2,3-6H3/q+2 ZAEXMNKDGJNLTA-UHFFFAOYSA-N 10624 CHEMBL140020::CHEMBL464538::1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide::4-(5-{4-[dimethyl(prop-2-en-1-yl)aminiumyl]phenyl}-3-oxopentyl)-N,N-dimethyl-N-(prop-2-en-1-yl)anilinium dibromide::BW284c51 Acetylcholinesterase Homo sapiens 10 ChEMBL 10.1016/j.bmcl.2010.11.051 10.7270/Q2542PK6 21144749 Musilek, K; Roder, J; Komloova, M; Holas, O; Hrabinova, M; Pohanka, M; Dohnal, V; Opletalova, V; Kuca, K; Jung, YS 12/24/2010 1/4/2013 University of Defence http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10624&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search EBW 1E3Q,6O50,6O52 1338 46511224 CHEMBL464538CHEMBL140020 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50919596 C[N+](C)(CC=C)c1ccc(cc1)CCC(=O)CCc2ccc(cc2)[N+](C)(C)CC=C InChI=1S/C27H38N2O/c1-7-21-28(3,4)25-15-9-23(10-16-25)13-19-27(30)20-14-24-11-17-26(18-12-24)29(5,6)22-8-2/h7-12,15-18H,1-2,13-14,19-22H2,3-6H3/q+2 ZAEXMNKDGJNLTA-UHFFFAOYSA-N 10624 CHEMBL140020::CHEMBL464538::1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide::4-(5-{4-[dimethyl(prop-2-en-1-yl)aminiumyl]phenyl}-3-oxopentyl)-N,N-dimethyl-N-(prop-2-en-1-yl)anilinium dibromide::BW284c51 Acetylcholinesterase Homo sapiens 30 ChEMBL 10.1016/j.bmcl.2010.11.051 10.7270/Q2542PK6 21144749 Musilek, K; Roder, J; Komloova, M; Holas, O; Hrabinova, M; Pohanka, M; Dohnal, V; Opletalova, V; Kuca, K; Jung, YS 12/24/2010 1/4/2013 University of Defence http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10624&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search EBW 1E3Q,6O50,6O52 1338 46511224 CHEMBL464538CHEMBL140020 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50995444 C[N+](C)(CC=C)c1ccc(cc1)CCC(=O)CCc2ccc(cc2)[N+](C)(C)CC=C InChI=1S/C27H38N2O/c1-7-21-28(3,4)25-15-9-23(10-16-25)13-19-27(30)20-14-24-11-17-26(18-12-24)29(5,6)22-8-2/h7-12,15-18H,1-2,13-14,19-22H2,3-6H3/q+2 ZAEXMNKDGJNLTA-UHFFFAOYSA-N 10624 CHEMBL140020::CHEMBL464538::1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide::4-(5-{4-[dimethyl(prop-2-en-1-yl)aminiumyl]phenyl}-3-oxopentyl)-N,N-dimethyl-N-(prop-2-en-1-yl)anilinium dibromide::BW284c51 Acetylcholinesterase Homo sapiens 8 ChEMBL 10.1021/jm970488n 10.7270/Q2BZ6784 9435905 So, SS; Karplus, M 2/13/1998 5/20/2013 Harvard University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10624&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search EBW 1E3Q,6O50,6O52 1338 46511224 CHEMBL464538CHEMBL140020 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 15299 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 2.9 8.0000 25.00 C Curated from the literature by BindingDB 10.1021/jm049510k 10.7270/Q27P8WMJ 15771436 aid1796269 Campiani, G; Fattorusso, C; Butini, S; Gaeta, A; Agnusdei, M; Gemma, S; Persico, M; Catalanotti, B; Savini, L; Nacci, V; Novellino, E; Holloway, HW; Greig, NH; Belinskaya, T; Fedorko, JM; Saxena, A 3/24/2005 5/2/2006 Universita Di Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 15518 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Bos taurus 19 8.0000 30.00 C Curated from the literature by BindingDB 10.1016/j.bmc.2005.09.029 10.7270/Q2G73BW9 16230018 aid1796282 Alonso, D; Dorronsoro, I; Rubio, L; Munoz, P; Garcia-Palomero, E; Del Monte, M; Bidon-Chanal, A; Orozco, M; Luque, FJ; Castro, A; Medina, M; Martinez, A 12/15/2005 5/8/2006 Neuropharma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 17743 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 22 Curated from the literature by BindingDB 10.1021/jm050578p 10.7270/Q2S75DJ6 16570913 aid1796482 Luo, W; Yu, QS; Kulkarni, SS; Parrish, DA; Holloway, HW; Tweedie, D; Shafferman, A; Lahiri, DK; Brossi, A; Greig, NH 4/6/2006 8/13/2006 National Institutes of Health http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 18638 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 20.5 23.1 8.0000 37.00 C Curated from the literature by BindingDB 10.1021/jm0340602 10.7270/Q29Z9332 12773032 aid1796570 Piazzi, L; Rampa, A; Bisi, A; Gobbi, S; Belluti, F; Cavalli, A; Bartolini, M; Andrisano, V; Valenti, P; Recanatini, M 6/5/2003 9/12/2006 University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 18676 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 22 8.0000 37.00 C Curated from the literature by BindingDB 10.1021/jm010491d 10.7270/Q22J6933 12166941 aid1796572 Yu, QS; Zhu, X; Holloway, HW; Whittaker, NF; Brossi, A; Greig, NH 8/15/2002 9/12/2006 National Institutes of Health http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 200777 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 26 Curated from the literature by BindingDB 10.1111/j.1747-0285.2012.01435.x 10.7270/Q28P5Z3T 22726458 aid1799797 Raza, R; Saeed, A; Arif, M; Mahmood, S; Muddassar, M; Raza, A; Iqbal, J 10/28/2012 10/29/2012 Comsats Institute of Information Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 293169 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 23 8.0000 25.00 C Curated from the literature by BindingDB 10.1016/j.bioorg.2015.05.005 10.7270/Q2WS8S05 26042530 aid1801052 Kanhed, AM; Sinha, A; Machhi, J; Tripathi, A; Parikh, ZS; Pillai, PP; Giridhar, R; Yadav, MR 8/28/2015 9/8/2015 The M. S. University of Baroda http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 344013 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 1e+1 8.0000 25.00 C Curated from the literature by BindingDB 10.1016/j.bioorg.2016.05.002 10.7270/Q2P849PS 27231830 aid1801892 Chigurupati, S; Selvaraj, M; Mani, V; Selvarajan, KK; Mohammad, JI; Kaveti, B; Bera, H; Palanimuthu, VR; Teh, LK; Salleh, MZ 8/28/2016 9/8/2016 Aimst University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 354300 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 4e+1 8.0000 25.00 C Curated from the literature by BindingDB 10.1111/cbdd.12800 10.7270/Q26D5RSX 27282589 aid1802080 Osman, W; Mohamed, T; Sit, VM; Vasefi, MS; Beazely, MA; Rao, PP 11/28/2016 11/4/2016 University of Waterloo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 393850 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 6.16 8.0000 25.00 C Curated from the literature by BindingDB 10.7270/Q2JM28HK aid1802741 Ozadali-Sari, K; Küçükkilinç, TT; Ayazgok, B; Balkan, A; Unsal-Tan, O 5/2/2017 5/9/2017 Hacettepe University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 404157 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Mus musculus 94 US Patent 10.7270/Q2WD3ZFC aid1802876 US9346818 Bai, H; Zhao, X; Zhong, J; Gong, Y; Zhu, Q; Liu, X; Zheng, X; Liu, L 5/24/2016 6/5/2017 Zhejiang Hisun Pharmaceutical http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 560596 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 8.00 US Patent 10.7270/Q24Q7X1C aid1795926 US9586925 Gulcan, HO; Unlu, S; Esiringu, I; Sahin, Y; Ercetin, T; Oz, D; Sahin, F 3/7/2017 3/2/2019 Nobel IlaÇ http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 643512 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 11.0 US Patent 10.7270/Q23J3G2W aid1796792 US9663465 Dallemagne, P; Rochais, C; Lecoutey, C; Boulouard, M; Freret, T 5/30/2017 6/3/2019 Universite De Caen http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50008786 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Bos taurus 8 ChEMBL 10.1016/s0960-894x(98)00076-6 10.7270/Q2S181N2 9871563 Perola, E; Cellai, L; Brufani, M 1/26/1999 11/10/2009 Istituto Di Strutturistica Chimica G. Giacomello http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 50008802 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Bos taurus 6 ChEMBL 10.1016/s0960-894x(98)00076-6 10.7270/Q2S181N2 9871563 Perola, E; Cellai, L; Brufani, M 1/26/1999 11/10/2009 Istituto Di Strutturistica Chimica G. Giacomello http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 50017164 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 18 ChEMBL 10.1016/s0960-894x(02)00482-1 10.7270/Q2CZ37Q4 12182861 Clark, JK; Cowley, P; Muir, AW; Palin, R; Pow, E; Prosser, AB; Taylor, R; Zhang, MQ 8/16/2002 10/5/2012 Organon Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50049157 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 1.7 ChEMBL 10.1021/jm00015a020 10.7270/Q22B8X2S 7636858 Vidaluc, JL; Calmel, F; Bigg, DC; Carilla, E; Briley, M 9/12/1995 11/10/2009 Centre De Recherche Pierre Fabre http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50062419 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 8 ChEMBL 10.1021/jm00043a012 10.7270/Q2VT1R4X 8064800 Villalobos, A; Blake, JF; Biggers, CK; Butler, TW; Chapin, DS; Chen, YL; Ives, JL; Jones, SB; Liston, DR; Nagel, AA 9/22/1994 11/10/2009 Pfizer http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50109206 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 62 ChEMBL 10.1016/j.ejmech.2014.06.034 10.7270/Q2862J10 24980117 Bukhari, SN; Jantan, I; Masand, VH; Mahajan, DT; Sher, M; Naeem-ul-Hassan, M; Amjad, MW 7/28/2014 2/12/2015 Universiti Kebangsaan Malaysia http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50119526 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 8 ChEMBL 10.1016/s0960-894x(98)00076-6 10.7270/Q2S181N2 9871563 Perola, E; Cellai, L; Brufani, M 1/26/1999 11/10/2009 Istituto Di Strutturistica Chimica G. Giacomello http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50147135 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 20 ChEMBL 10.1016/s0960-894x(99)00597-1 10.7270/Q2ZP45B8 10612585 Zeng, F; Jiang, H; Zhai, Y; Zhang, H; Chen, K; Ji, R 1/13/2000 11/10/2009 Institute of Materia Medica http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50164264 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 21 ChEMBL 10.1021/jm100293f 10.7270/Q2B56JXF 20420456 Melchiorre, C; Bolognesi, ML; Minarini, A; Rosini, M; Tumiatti, V 8/19/2010 3/19/2011 University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50192953 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 40 ChEMBL 10.1021/jm0109356 10.7270/Q298869Q 11689088 Andreani, A; Cavalli, A; Granaiola, M; Guardigli, M; Leoni, A; Locatelli, A; Morigi, R; Rambaldi, M; Recanatini, M; Roda, A 11/5/2001 11/10/2009 Università http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50233737 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 8.0 ChEMBL 10.1016/j.bmc.2014.08.016 10.7270/Q2WH2RKB 25189690 Gulcan, HO; Unlu, S; Esiringu, I; Ercetin, T; Sahin, Y; Oz, D; Sahin, MF 9/22/2014 3/6/2016 Eastern Mediterranean University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50253247 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 20 ChEMBL 10.1021/np500558b 10.7270/Q2Z32183 25455147 Kim, H; Yang, I; Patil, RS; Kang, S; Lee, J; Choi, H; Kim, MS; Nam, SJ; Kang, H 12/26/2014 3/15/2016 Seoul National University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50289511 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 20.5 ChEMBL 10.1021/jm0494366 10.7270/Q2JD4W91 15588084 Tumiatti, V; Andrisano, V; Banzi, R; Bartolini, M; Minarini, A; Rosini, M; Melchiorre, C 12/13/2004 11/10/2009 University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50301298 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 6.0 ChEMBL 10.1016/j.bmc.2015.01.045 10.7270/Q2PN979Q 25707322 Guzior, N; Bajda, M; Rakoczy, J; Brus, B; Gobec, S; Malawska, B 3/17/2015 4/9/2016 Jagiellonian University Medical College http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50309213 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 16 ChEMBL 10.1021/jm501501a 10.7270/Q2WS8VX3 25418133 Bautista-Aguilera, OM; Samadi, A; Chioua, M; Nikolic, K; Filipic, S; Agbaba, D; Soriano, E; de Andrés, L; Rodríguez-Franco, MI; Alcaro, S; Ramsay, RR; Ortuso, F; Yañez, M; Marco-Contelles, J 12/29/2014 4/15/2016 Laboratorio De Quimica Medica (Iqog, Csic) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50318267 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 6.0 ChEMBL 10.1016/j.ejmech.2015.01.027 10.7270/Q23T9JXZ 25621991 Guzior, N; Bajda, M; Skrok, M; Kurpiewska, K; Lewinski, K; Brus, B; Pišlar, A; Kos, J; Gobec, S; Malawska, B 2/20/2015 4/24/2016 Jagiellonian University Medical College http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50325447 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 6.0 ChEMBL 10.1021/acs.jmedchem.5b00115 10.7270/Q2HQ41MH 25793650 Rochais, C; Lecoutey, C; Gaven, F; Giannoni, P; Hamidouche, K; Hedou, D; Dubost, E; Genest, D; Yahiaoui, S; Freret, T; Bouet, V; Dauphin, F; Sopkova de Oliveira Santos, J; Ballandonne, C; Corvaisier, S; Malzert-Fréon, A; Legay, R; Boulouard, M; Claeysen, S; Dallemagne, P 4/9/2015 4/28/2016 Cermn http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50341577 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 15 ChEMBL 10.1016/j.ejmech.2015.02.063 10.7270/Q2GQ70HK 25778991 Sang, Z; Qiang, X; Li, Y; Yuan, W; Liu, Q; Shi, Y; Ang, W; Luo, Y; Tan, Z; Deng, Y 4/6/2015 10/8/2016 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50341700 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 12 ChEMBL 10.1016/j.ejmech.2015.02.063 10.7270/Q2GQ70HK 25778991 Sang, Z; Qiang, X; Li, Y; Yuan, W; Liu, Q; Shi, Y; Ang, W; Luo, Y; Tan, Z; Deng, Y 4/6/2015 10/8/2016 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50351102 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 15 ChEMBL 10.1021/acs.jmedchem.5b00599 10.7270/Q26T0PCZ 26107513 Farina, R; Pisani, L; Catto, M; Nicolotti, O; Gadaleta, D; Denora, N; Soto-Otero, R; Mendez-Alvarez, E; Passos, CS; Muncipinto, G; Altomare, CD; Nurisso, A; Carrupt, PA; Carotti, A 7/23/2015 10/13/2016 University of Bari Aldo Moro http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50368941 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 11 ChEMBL 10.1016/j.bmc.2014.07.009 10.7270/Q22809B6 25082512 Li, Y; Peng, P; Tang, L; Hu, Y; Hu, Y; Sheng, R 8/29/2014 10/28/2016 Zhejiang University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50375186 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 15 ChEMBL 10.1016/j.bmc.2015.01.042 10.7270/Q2BG2QS9 25678013 Liu, Q; Qiang, X; Li, Y; Sang, Z; Li, Y; Tan, Z; Deng, Y 2/23/2015 11/2/2016 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50393651 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 40 ChEMBL 10.1016/j.ejmech.2007.04.018 10.7270/Q2TH8MG0 17624631 Andreani, A; Burnelli, S; Granaiola, M; Guardigli, M; Leoni, A; Locatelli, A; Morigi, R; Rambaldi, M; Rizzoli, M; Varoli, L; Roda, A 3/10/2008 1/11/2010 Università http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50412579 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 20 ChEMBL 10.1016/j.ejmech.2008.02.035 10.7270/Q2833RT4 18396354 Belluti, F; Piazzi, L; Bisi, A; Gobbi, S; Bartolini, M; Cavalli, A; Valenti, P; Rampa, A 3/2/2009 1/11/2010 University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50413409 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 12 ChEMBL 10.1016/j.ejmech.2008.03.003 10.7270/Q29W0F8B 18436348 Sheng, R; Xu, Y; Hu, C; Zhang, J; Lin, X; Li, J; Yang, B; He, Q; Hu, Y 12/31/2008 1/11/2010 Zhejiang University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50425406 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 26.8 ChEMBL 10.1016/j.bmc.2008.07.014 10.7270/Q2RR1Z2W 18662884 Shen, Y; Sheng, R; Zhang, J; He, Q; Yang, B; Hu, Y 8/18/2008 1/11/2010 Zhejiang University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50429023 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 14 ChEMBL 10.1016/j.ejmech.2015.08.052 10.7270/Q21V5GT0 26363866 Luo, XT; Wang, CM; Liu, Y; Huang, ZG 10/9/2015 12/14/2016 1St Affiliated Hospital of Guangxi Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50448170 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 7.9 ChEMBL 10.1016/j.bmc.2008.12.067 10.7270/Q24J0F0R 19162488 Zhu, Y; Xiao, K; Ma, L; Xiong, B; Fu, Y; Yu, H; Wang, W; Wang, X; Hu, D; Peng, H; Li, J; Gong, Q; Chai, Q; Tang, X; Zhang, H; Li, J; Shen, J 2/23/2009 1/11/2010 Chinese Academy of Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50464333 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 2.3 ChEMBL 10.1016/S0960-894X(00)80545-4 10.7270/Q29886XS Gregor, VE; Emmerling, MR; Lee, C; Moore, CJ 12/28/1992 8/17/2010 TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50464359 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 5.7 ChEMBL 10.1016/S0960-894X(00)80547-8 10.7270/Q21R6QDV Sugimoto, H; Iimura, Y; Yamanishi, Y; Yamatsu, K 12/28/1992 8/17/2010 TBA http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50468278 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 10.0 ChEMBL 10.1016/j.bmc.2016.02.023 10.7270/Q2125VHK 26917219 Xie, SS; Lan, JS; Wang, X; Wang, ZM; Jiang, N; Li, F; Wu, JJ; Wang, J; Kong, LY 3/13/2016 6/19/2017 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50498585 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 7.0 ChEMBL 10.1021/acsmedchemlett.6b00099 10.7270/Q2NG4SJJ 27096037 Gunaydin, H; Bartberger, MD 4/20/2016 9/10/2017 Merck http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50502591 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 11 ChEMBL 10.1021/acsmedchemlett.5b00483 10.7270/Q2PN97JV 27190595 Costanzo, P; Cariati, L; Desiderio, D; Sgammato, R; Lamberti, A; Arcone, R; Salerno, R; Nardi, M; Masullo, M; Oliverio, M 5/18/2016 9/26/2017 Magna Graecia University of Catanzaro http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50502623 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 10.0 ChEMBL 10.1021/acsmedchemlett.5b00483 10.7270/Q2PN97JV 27190595 Costanzo, P; Cariati, L; Desiderio, D; Sgammato, R; Lamberti, A; Arcone, R; Salerno, R; Nardi, M; Masullo, M; Oliverio, M 5/18/2016 9/26/2017 Magna Graecia University of Catanzaro http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50508688 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 120 ChEMBL 10.1016/j.bmc.2016.07.025 10.7270/Q2DV1MV0 27460699 Wang, J; Wang, ZM; Li, XM; Li, F; Wu, JJ; Kong, LY; Wang, XB 8/22/2016 10/6/2017 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50521824 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 10.0 ChEMBL 10.1016/j.ejmech.2016.05.055 10.7270/Q2HX1FNV 27267007 Estrada, M; Herrera-Arozamena, C; Pérez, C; Viña, D; Romero, A; Morales-García, JA; Pérez-Castillo, A; Rodríguez-Franco, MI 10/4/2016 7/10/2018 IQM-CSIC http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50523812 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 9.0 ChEMBL 10.1016/j.ejmech.2015.10.001 10.7270/Q2B27X8T 26471320 Wu, MY; Esteban, G; Brogi, S; Shionoya, M; Wang, L; Campiani, G; Unzeta, M; Inokuchi, T; Butini, S; Marco-Contelles, J 10/4/2016 7/17/2018 Okayama University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50531952 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 90 ChEMBL 10.1016/j.bmc.2016.10.016 10.7270/Q2B85B3V 27780618 Mughal, EU; Sadiq, A; Murtaza, S; Rafique, H; Zafar, MN; Riaz, T; Khan, BA; Hameed, A; Khan, KM 1/1/2017 8/13/2018 University of Gujrat http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50534800 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 48 ChEMBL 10.1016/j.ejmech.2016.07.052 10.7270/Q2ZW1NW5 27484514 Wang, ZM; Cai, P; Liu, QH; Xu, DQ; Yang, XL; Wu, JJ; Kong, LY; Wang, XB 11/10/2016 8/17/2018 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50543704 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 6.0 ChEMBL 10.1016/j.ejmech.2016.08.016 10.7270/Q2PZ5BT8 27560283 Wieckowska, A; Kolaczkowski, M; Bucki, A; Godyn, J; Marcinkowska, M; Wieckowski, K; Zareba, P; Siwek, A; Kazek, G; Gluch-Lutwin, M; Mierzejewski, P; Bienkowski, P; Sienkiewicz-Jarosz, H; Knez, D; Wichur, T; Gobec, S; Malawska, B 11/29/2016 8/31/2018 Jagiellonian University Collegium Medicum http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50544743 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 12 ChEMBL 10.1016/j.bmc.2009.07.072 10.7270/Q29S1R4M 19692250 Sheng, R; Lin, X; Zhang, J; Chol, KS; Huang, W; Yang, B; He, Q; Hu, Y 9/2/2009 8/31/2010 Zhejiang University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50553458 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 20 ChEMBL 10.1016/j.bmc.2010.01.071 10.7270/Q2P26Z7H 20171894 Rizzo, S; Bartolini, M; Ceccarini, L; Piazzi, L; Gobbi, S; Cavalli, A; Recanatini, M; Andrisano, V; Rampa, A 3/11/2010 9/2/2010 University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50578102 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 8 ChEMBL 10.1016/j.ejmech.2009.12.038 10.7270/Q25H7GFM 20053484 Lv, W; Xue, Y 2/17/2010 11/20/2010 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50585681 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 43 ChEMBL 10.1016/s0960-894x(02)00482-1 10.7270/Q2CZ37Q4 12182861 Clark, JK; Cowley, P; Muir, AW; Palin, R; Pow, E; Prosser, AB; Taylor, R; Zhang, MQ 8/16/2002 10/5/2012 Organon Laboratories http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50588924 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens >100000 ChEMBL 10.1021/jm100293f 10.7270/Q2B56JXF 20420456 Melchiorre, C; Bolognesi, ML; Minarini, A; Rosini, M; Tumiatti, V 8/19/2010 3/19/2011 University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50597927 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 90 ChEMBL 10.1021/jm100573q 10.7270/Q23R0T3D 20684567 Chaudhaery, SS; Roy, KK; Shakya, N; Saxena, G; Sammi, SR; Nazir, A; Nath, C; Saxena, AK 9/2/2010 6/11/2011 Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50635765 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 32 ChEMBL 10.1016/j.bmc.2011.02.030 10.7270/Q2Q240JH 21429752 Mohamed, T; Zhao, X; Habib, LK; Yang, J; Rao, PP 3/29/2011 12/3/2011 University of Waterloo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50636569 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 6 ChEMBL 10.1016/j.bmcl.2010.12.041 10.7270/Q27W6CH9 21216144 Al-Rashid, ZF; Hsung, RP 4/25/2011 12/3/2011 Alchemical Research http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50637195 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 18 ChEMBL 10.1021/jm101299d 10.7270/Q2SQ90QT 21417225 Conejo-Garcia, A; Pisani, L; Nunez, Mdel C; Catto, M; Nicolotti, O; Leonetti, F; Campos, JM; Gallo, MA; Espinosa, A; Carotti, A 4/21/2011 12/4/2011 Universidad De Granada http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50638643 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 23 ChEMBL 10.1016/j.ejmech.2011.02.019 10.7270/Q2X92BM2 21397996 Belluti, F; Bartolini, M; Bottegoni, G; Bisi, A; Cavalli, A; Andrisano, V; Rampa, A 3/28/2011 12/4/2011 University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50645452 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 22 ChEMBL 10.1016/j.ejmech.2011.02.071 10.7270/Q2BK1CPG 21459491 Tasso, B; Catto, M; Nicolotti, O; Novelli, F; Tonelli, M; Giangreco, I; Pisani, L; Sparatore, A; Boido, V; Carotti, A; Sparatore, F 5/2/2011 12/6/2011 University of Genoa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50645460 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 22 ChEMBL 10.1016/j.ejmech.2011.02.071 10.7270/Q2BK1CPG 21459491 Tasso, B; Catto, M; Nicolotti, O; Novelli, F; Tonelli, M; Giangreco, I; Pisani, L; Sparatore, A; Boido, V; Carotti, A; Sparatore, F 5/2/2011 12/6/2011 University of Genoa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50645468 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 4150 ChEMBL 10.1016/j.ejmech.2011.02.071 10.7270/Q2BK1CPG 21459491 Tasso, B; Catto, M; Nicolotti, O; Novelli, F; Tonelli, M; Giangreco, I; Pisani, L; Sparatore, A; Boido, V; Carotti, A; Sparatore, F 5/2/2011 12/6/2011 University of Genoa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50645478 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 4150 ChEMBL 10.1016/j.ejmech.2011.02.071 10.7270/Q2BK1CPG 21459491 Tasso, B; Catto, M; Nicolotti, O; Novelli, F; Tonelli, M; Giangreco, I; Pisani, L; Sparatore, A; Boido, V; Carotti, A; Sparatore, F 5/2/2011 12/6/2011 University of Genoa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50664189 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 32 ChEMBL 10.1016/j.bmcl.2011.07.091 10.7270/Q2C829P7 21873056 Mohamed, T; Yeung, JC; Rao, PP 9/12/2011 3/24/2012 University of Waterloo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50706609 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 5 ChEMBL 10.1016/j.bmc.2011.09.061 10.7270/Q24F1R52 22019465 Huang, W; Tang, L; Shi, Y; Huang, S; Xu, L; Sheng, R; Wu, P; Li, J; Zhou, N; Hu, Y 11/9/2011 7/21/2012 Zhejiang University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50714175 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 19 ChEMBL 10.1016/j.ejmech.2016.12.009 10.7270/Q2NG4SW1 27951485 Li, Y; Qiang, X; Luo, L; Yang, X; Xiao, G; Liu, Q; Ai, J; Tan, Z; Deng, Y 1/27/2017 6/19/2019 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50714185 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 36 ChEMBL 10.1016/j.ejmech.2016.12.009 10.7270/Q2NG4SW1 27951485 Li, Y; Qiang, X; Luo, L; Yang, X; Xiao, G; Liu, Q; Ai, J; Tan, Z; Deng, Y 1/27/2017 6/19/2019 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50714970 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 30 ChEMBL 10.1016/j.ejmech.2016.12.005 10.7270/Q2D220WF 27951490 Mohamed, T; Rao, PPN 1/27/2017 6/19/2019 University of Waterloo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50740762 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 11 ChEMBL 10.1016/j.ejmech.2017.02.039 10.7270/Q2F76FVX 28279845 Sang, Z; Pan, W; Wang, K; Ma, Q; Yu, L; Yang, Y; Bai, P; Leng, C; Xu, Q; Li, X; Tan, Z; Liu, W 4/21/2017 8/20/2019 Nanyang Normal University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50740862 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 37 ChEMBL 10.1016/j.ejmech.2017.02.039 10.7270/Q2F76FVX 28279845 Sang, Z; Pan, W; Wang, K; Ma, Q; Yu, L; Yang, Y; Bai, P; Leng, C; Xu, Q; Li, X; Tan, Z; Liu, W 4/21/2017 8/20/2019 Nanyang Normal University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50762714 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 120 ChEMBL 10.1016/j.bmcl.2017.05.050 10.7270/Q2BG2RDS 28552337 Bharkavi, C; Vivek Kumar, S; Ashraf Ali, M; Osman, H; Muthusubramanian, S; Perumal, S 7/15/2017 10/17/2019 Madurai Kamaraj University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50769668 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Mus musculus 5.7 ChEMBL 10.1021/acs.jmedchem.7b01086 10.7270/Q2S75JRJ 29227101 Košak, U; Brus, B; Knez, D; Žakelj, S; Trontelj, J; Pišlar, A; Šink, R; Jukič, M; Živin, M; Podkowa, A; Nachon, F; Brazzolotto, X; Stojan, J; Kos, J; Coquelle, N; Sałat, K; Colletier, JP; Gobec, S 1/11/2018 10/31/2019 University of Ljubljana http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 50774368 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Mus musculus 5.7 ChEMBL 10.1021/jm00024a009 10.7270/Q2QC045T 7490731 Sugimoto, H; Iimura, Y; Yamanishi, Y; Yamatsu, K 1/2/1996 10/31/2012 Eisai http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 50774937 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 8 ChEMBL 10.1021/jm00007a005 10.7270/Q21N81S7 7707311 Nagel, AA; Liston, DR; Jung, S; Mahar, M; Vincent, LA; Chapin, D; Chen, YL; Hubbard, S; Ives, JL; Jones, SB 5/11/1995 10/31/2012 Pfizer http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50787802 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 38 ChEMBL 10.1016/j.ejmech.2017.02.045 10.7270/Q2FB55C0 28388521 Lan, JS; Zhang, T; Liu, Y; Yang, J; Xie, SS; Liu, J; Miao, ZY; Ding, Y 6/16/2017 11/29/2019 Shanghai University of Traditional Chinese Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50790621 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 37 ChEMBL 10.1016/j.bmc.2017.03.070 10.7270/Q2F76G04 28487125 Sang, Z; Pan, W; Wang, K; Ma, Q; Yu, L; Liu, W 6/15/2017 12/3/2019 Nanyang Normal University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50793155 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 16 ChEMBL 10.1021/jm981101z 10.7270/Q26M37JW 10052979 Contreras, JM; Rival, YM; Chayer, S; Bourguignon, JJ; Wermuth, CG 3/16/1999 11/13/2012 Louis Pasteur University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50802100 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 16 ChEMBL 10.1021/jm001088u 10.7270/Q2222VG9 11495583 Contreras, JM; Parrot, I; Sippl, W; Rival, YM; Wermuth, CG 8/9/2001 11/25/2012 Louis Pasteur University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50811176 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Bos taurus 2.9 ChEMBL 10.1021/jm0255668 10.7270/Q2GF0V7X 12502352 Savini, L; Gaeta, A; Fattorusso, C; Catalanotti, B; Campiani, G; Chiasserini, L; Pellerano, C; Novellino, E; McKissic, D; Saxena, A 12/27/2002 11/27/2012 University of Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 50824510 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 16 ChEMBL 10.1016/j.bmcl.2005.05.132 10.7270/Q27H1KBV 15993600 Sheng, R; Lin, X; Li, J; Jiang, Y; Shang, Z; Hu, Y 8/2/2005 12/2/2012 Zhejiang University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50830757 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 22 ChEMBL 10.1021/jm049309+ 10.7270/Q2TM7BWQ 15715468 Luo, W; Yu, QS; Zhan, M; Parrish, D; Deschamps, JR; Kulkarni, SS; Holloway, HW; Alley, GM; Lahiri, DK; Brossi, A; Greig, NH 2/17/2005 12/3/2012 National Institute On Aging http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50848521 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 23 ChEMBL 10.1021/jm070559a 10.7270/Q218379R 17850125 Bolognesi, ML; Banzi, R; Bartolini, M; Cavalli, A; Tarozzi, A; Andrisano, V; Minarini, A; Rosini, M; Tumiatti, V; Bergamini, C; Fato, R; Lenaz, G; Hrelia, P; Cattaneo, A; Recanatini, M; Melchiorre, C 9/27/2007 12/11/2012 University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50853606 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 23 ChEMBL 10.1021/jm7009364 10.7270/Q25B039W 18181565 Cavalli, A; Bolognesi, ML; Minarini, A; Rosini, M; Tumiatti, V; Recanatini, M; Melchiorre, C 2/7/2008 12/14/2012 University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50857406 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 37 ChEMBL 10.1016/j.bmcl.2017.09.055 10.7270/Q22J6F9F 29033232 Sang, Z; Wang, K; Wang, H; Yu, L; Wang, H; Ma, Q; Ye, M; Han, X; Liu, W 11/15/2017 1/26/2020 Nanyang Normal University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50858157 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 19 ChEMBL 10.1016/j.bmcl.2017.09.055 10.7270/Q22J6F9F 29033232 Sang, Z; Wang, K; Wang, H; Yu, L; Wang, H; Ma, Q; Ye, M; Han, X; Liu, W 11/15/2017 1/26/2020 Nanyang Normal University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50864178 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 160 ChEMBL 10.1016/j.bmc.2007.12.048 10.7270/Q27S7PMQ 18249544 Bembenek, SD; Keith, JM; Letavic, MA; Apodaca, R; Barbier, AJ; Dvorak, L; Aluisio, L; Miller, KL; Lovenberg, TW; Carruthers, NI 3/31/2008 12/15/2012 Johnson & Johnson Pharmaceutical Research and Development http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50871835 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Bos taurus 8.12 ChEMBL 10.1021/jm8001313 10.7270/Q2F76DGK 18517184 Camps, P; Formosa, X; Galdeano, C; Gomez, T; Munoz-Torrero, D; Scarpellini, M; Viayna, E; Badia, A; Clos, MV; Camins, A; Pallas, M; Bartolini, M; Mancini, F; Andrisano, V; Estelrich, J; Lizondo, M; Bidon-Chanal, A; Luque, FJ 6/19/2008 12/16/2012 Laboratori De Qu�Mica Farmac�Utica (Unitat Associada Al Csic) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 50871846 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 11.6 ChEMBL 10.1021/jm8001313 10.7270/Q2F76DGK 18517184 Camps, P; Formosa, X; Galdeano, C; Gomez, T; Munoz-Torrero, D; Scarpellini, M; Viayna, E; Badia, A; Clos, MV; Camins, A; Pallas, M; Bartolini, M; Mancini, F; Andrisano, V; Estelrich, J; Lizondo, M; Bidon-Chanal, A; Luque, FJ 6/19/2008 12/16/2012 Laboratori De Qu�Mica Farmac�Utica (Unitat Associada Al Csic) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50871869 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 5.7 ChEMBL 10.1021/jm8001313 10.7270/Q2F76DGK 18517184 Camps, P; Formosa, X; Galdeano, C; Gomez, T; Munoz-Torrero, D; Scarpellini, M; Viayna, E; Badia, A; Clos, MV; Camins, A; Pallas, M; Bartolini, M; Mancini, F; Andrisano, V; Estelrich, J; Lizondo, M; Bidon-Chanal, A; Luque, FJ 6/19/2008 12/16/2012 Laboratori De Qu�Mica Farmac�Utica (Unitat Associada Al Csic) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50871873 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Bos taurus 19 ChEMBL 10.1021/jm8001313 10.7270/Q2F76DGK 18517184 Camps, P; Formosa, X; Galdeano, C; Gomez, T; Munoz-Torrero, D; Scarpellini, M; Viayna, E; Badia, A; Clos, MV; Camins, A; Pallas, M; Bartolini, M; Mancini, F; Andrisano, V; Estelrich, J; Lizondo, M; Bidon-Chanal, A; Luque, FJ 6/19/2008 12/16/2012 Laboratori De Qu�Mica Farmac�Utica (Unitat Associada Al Csic) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 50879191 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 23.1 ChEMBL 10.1021/jm8009684 10.7270/Q2MW2J3W 18954037 Tumiatti, V; Milelli, A; Minarini, A; Rosini, M; Bolognesi, ML; Micco, M; Andrisano, V; Bartolini, M; Mancini, F; Recanatini, M; Cavalli, A; Melchiorre, C 2/20/2009 12/20/2012 University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50881005 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 30 ChEMBL 10.1016/j.ejmech.2017.02.042 10.7270/Q2P55R0J 28242549 Xia, CL; Wang, N; Guo, QL; Liu, ZQ; Wu, JQ; Huang, SL; Ou, TM; Tan, JH; Wang, HG; Li, D; Huang, ZS 4/21/2017 2/5/2020 Sun Yat-Sen University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50881682 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 10.0 ChEMBL 10.1016/j.ejmech.2017.02.034 10.7270/Q2JD5086 28242552 Monjas, L; Arce, MP; León, R; Egea, J; Pérez, C; Villarroya, M; López, MG; Gil, C; Conde, S; Rodríguez-Franco, MI 4/21/2017 2/6/2020 IQM-CSIC http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50888178 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 12 ChEMBL 10.1016/j.ejmech.2017.04.054 10.7270/Q2H41TX2 28458136 Sang, Z; Qiang, X; Li, Y; Xu, R; Cao, Z; Song, Q; Wang, T; Zhang, X; Liu, H; Tan, Z; Deng, Y 7/28/2017 2/26/2020 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50888183 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 15 ChEMBL 10.1016/j.ejmech.2017.04.054 10.7270/Q2H41TX2 28458136 Sang, Z; Qiang, X; Li, Y; Xu, R; Cao, Z; Song, Q; Wang, T; Zhang, X; Liu, H; Tan, Z; Deng, Y 7/28/2017 2/26/2020 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50895443 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 50 ChEMBL 10.1016/j.bmcl.2017.07.013 10.7270/Q20P12G0 28751142 Zhou, LY; Zhu, Y; Jiang, YR; Zhao, XJ; Guo, D 9/1/2017 3/18/2020 Central South University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50913402 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 8.20 ChEMBL 10.1021/jm901902w 10.7270/Q25T3MFV 20575555 de Los Rios, C; Egea, J; Marco-Contelles, J; Leon, R; Samadi, A; Iriepa, I; Moraleda, I; Galvez, E; Garcia, AG; Lopez, MG; Villarroya, M; Romero, A 7/29/2010 12/31/2012 Universidad Autonoma De Madrid http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50919271 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 120 ChEMBL 10.1016/j.bmcl.2010.09.108 10.7270/Q2Q2417W 20951037 Ali, MA; Ismail, R; Choon, TS; Yoon, YK; Wei, AC; Pandian, S; Kumar, RS; Osman, H; Manogaran, E 11/8/2010 1/3/2013 Universiti Sains Malaysia http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50943897 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 32 ChEMBL 10.1016/j.bmcl.2012.05.077 10.7270/Q27S7PSZ 22704921 Mohamed, T; Yeung, JC; Vasefi, MS; Beazely, MA; Rao, PP 7/3/2012 2/8/2013 University of Waterloo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50949799 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 21.5 ChEMBL 10.1016/j.bmc.2011.05.027 10.7270/Q22B903F 22172310 Anand, P; Singh, B 12/30/2011 2/8/2013 Punjabi University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 50953151 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 10 ChEMBL 10.1016/j.ejmech.2012.09.030 10.7270/Q2MP54CK 23078965 Samadi, A; Estrada, M; Perez, C; Rodriguez-Franco, MI; Iriepa, I; Moraleda, I; Chioua, M; Marco-Contelles, J 11/26/2012 2/8/2013 Instituto De Qu£Mica Org£Nica General (Csic) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50983315 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 25 ChEMBL 10.7270/Q2ZP4BBB 36067929 Fang, L; Shen, S; Liu, Q; Liu, Z; Zhao, J 11/1/2022 4/18/2024 Southeast University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50984008 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 5.7 ChEMBL 10.1016/j.ejmech.2017.08.051 10.7270/Q2XS5XWN 28863358 Chierrito, TPC; Pedersoli-Mantoani, S; Roca, C; Requena, C; Sebastian-Perez, V; Castillo, WO; Moreira, NCS; Pérez, C; Sakamoto-Hojo, ET; Takahashi, CS; Jiménez-Barbero, J; Cañada, FJ; Campillo, NE; Martinez, A; Carvalho, I 10/20/2017 6/3/2020 University of S£O Paulo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50986019 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 20 ChEMBL 10.1016/j.ejmech.2017.09.022 10.7270/Q27083ZM 29031067 Pandolfi, F; De Vita, D; Bortolami, M; Coluccia, A; Di Santo, R; Costi, R; Andrisano, V; Alabiso, F; Bergamini, C; Fato, R; Bartolini, M; Scipione, L 12/1/2017 6/12/2020 Sapienza University of Rome http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50994371 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 8 ChEMBL 10.1021/jm950704x 10.7270/Q25D8T1Q 8558505 Tong, W; Collantes, ER; Chen, Y; Welsh, WJ 2/28/1996 5/20/2013 University of Missouri St. Louis http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51007492 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 35.48 ChEMBL 10.1016/j.bmc.2008.10.029 10.7270/Q2FQ9XVP 18976927 Morini, G; Comini, M; Rivara, M; Rivara, S; Bordi, F; Plazzi, PV; Flammini, L; Saccani, F; Bertoni, S; Ballabeni, V; Barocelli, E; Mor, M 11/17/2008 5/21/2013 University of Parma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 51030332 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 41 ChEMBL 10.1016/j.ejmech.2018.01.055 10.7270/Q2M61NST 29407958 Jiang, N; Huang, Q; Liu, J; Liang, N; Li, Q; Li, Q; Xie, SS 2/25/2018 8/6/2020 Jiangxi University of Traditional Chinese Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51031508 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 5.7 ChEMBL 10.1016/j.ejmech.2018.01.066 10.7270/Q2K64MM0 29421570 Dias Viegas, FP; de Freitas Silva, M; Divino da Rocha, M; Castelli, MR; Riquiel, MM; Machado, RP; Vaz, SM; Simões de Lima, LM; Mancini, KC; Marques de Oliveira, PC; Morais, ÉP; Gontijo, VS; da Silva, FMR; D'Alincourt da Fonseca Peçanha, D; Castro, NG; Neves, GA; Giusti-Paiva, A; Vilela, FC; Orlandi, L; Camps, I; Veloso, MP; Leomil Coelho, LF; Ionta, M; Ferreira-Silva, GÁ; Pereira, RM; Dardenne, LE; Guedes, IA; de Oliveira Carneiro Junior, W; Quaglio Bellozi, PM; Pinheiro de Oliveira, AC; Ferreira, FF; Pruccoli, L; Tarozzi, A; Viegas, C 3/10/2018 8/8/2020 Federal University of Alfenas http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51039181 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Bos taurus 4.2 ChEMBL 10.1016/j.bmc.2012.10.045 10.7270/Q2QV3NTH 23199476 Catto, M; Pisani, L; Leonetti, F; Nicolotti, O; Pesce, P; Stefanachi, A; Cellamare, S; Carotti, A 12/18/2012 9/24/2013 University of Bari Aldo Moro http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 51039207 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 2.0 ChEMBL 10.1016/j.bmc.2012.10.045 10.7270/Q2QV3NTH 23199476 Catto, M; Pisani, L; Leonetti, F; Nicolotti, O; Pesce, P; Stefanachi, A; Cellamare, S; Carotti, A 12/18/2012 9/24/2013 University of Bari Aldo Moro http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51042060 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 7.2 ChEMBL 10.1016/j.bmcl.2012.11.100 10.7270/Q2F19118 23276831 Mishra, N; Sasmal, D 1/14/2013 9/24/2013 Birla Institute of Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51046182 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 5.7 ChEMBL 10.1016/j.bmc.2012.11.044 10.7270/Q20C4X3F 23273608 Hu, Y; Zhang, J; Chandrashankra, O; Ip, FC; Ip, NY 1/15/2013 9/24/2013 The Hong Kong University of Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51046185 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 32 ChEMBL 10.1016/j.bmc.2012.11.044 10.7270/Q20C4X3F 23273608 Hu, Y; Zhang, J; Chandrashankra, O; Ip, FC; Ip, NY 1/15/2013 9/24/2013 The Hong Kong University of Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 51107699 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 13 ChEMBL 10.1016/j.bmc.2017.09.012 10.7270/Q22V2JP6 29089261 Singh, M; Kaur, M; Singh, N; Silakari, O 12/15/2017 8/15/2020 Punjabi University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 51108988 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Mus musculus 14550 ChEMBL 10.1016/j.bmc.2017.11.033 10.7270/Q2JQ13MH 29195794 Piplani, P; Jain, A; Devi, D; Anjali, na; Sharma, A; Silakari, P 1/1/2018 8/15/2020 Panjab University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 51116764 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 3.5 ChEMBL 10.1016/j.ejmech.2017.07.006 10.7270/Q2HM5C2T 28728106 Zhao, XJ; Gong, DM; Jiang, YR; Guo, D; Zhu, Y; Deng, YC 9/29/2017 8/16/2020 Central South University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51117364 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 32 ChEMBL 10.1016/j.ejmech.2017.07.055 10.7270/Q2GM89X1 28797883 Lan, JS; Ding, Y; Liu, Y; Kang, P; Hou, JW; Zhang, XY; Xie, SS; Zhang, T 10/20/2017 8/16/2020 Shanghai University of Traditional Chinese Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51117539 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 160 ChEMBL 10.1016/j.ejmech.2017.07.077 10.7270/Q2Q52S78 28800459 Wang, J; Cai, P; Yang, XL; Li, F; Wu, JJ; Kong, LY; Wang, XB 10/20/2017 8/16/2020 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51128796 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 6.9 ChEMBL 10.1016/j.bmcl.2018.07.019 10.7270/Q2R21422 30017317 Gabr, MT; Abdel-Raziq, MS 9/15/2018 8/17/2020 Mansoura University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51133953 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 5.7 ChEMBL 10.1016/j.ejmech.2018.01.007 10.7270/Q2JQ13PD 29335209 Chierrito, TPC; Pedersoli-Mantoani, S; Roca, C; Sebastian-Pérez, V; Martínez-Gonzalez, L; Pérez, DI; Perez, C; Canales, A; Cañada, FJ; Campillo, NE; Carvalho, I; Martinez, A 2/10/2018 8/18/2020 University of S£O Paulo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51140790 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 10.0 ChEMBL 10.1016/j.ejmech.2018.07.056 10.7270/Q2F192DM 30245401 Reis, J; Cagide, F; Valencia, ME; Teixeira, J; Bagetta, D; Pérez, C; Uriarte, E; Oliveira, PJ; Ortuso, F; Alcaro, S; Rodríguez-Franco, MI; Borges, F 10/5/2018 8/18/2020 University of Porto http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51143939 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 10.0 ChEMBL 10.1016/j.ejmech.2018.07.026 10.7270/Q2N300PH 30025348 Estrada Valencia, M; Herrera-Arozamena, C; de Andrés, L; Pérez, C; Morales-García, JA; Pérez-Castillo, A; Ramos, E; Romero, A; Viña, D; Yáñez, M; Laurini, E; Pricl, S; Rodríguez-Franco, MI 8/5/2018 8/18/2020 IQM-CSIC http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51144123 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 22 ChEMBL 10.1016/j.ejmech.2018.07.033 10.7270/Q27W6FW2 30031971 Knez, D; Coquelle, N; Pišlar, A; Žakelj, S; Jukič, M; Sova, M; Mravljak, J; Nachon, F; Brazzolotto, X; Kos, J; Colletier, JP; Gobec, S 8/5/2018 8/18/2020 University of Ljubljana http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51144806 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 48 ChEMBL 10.1016/j.ejmech.2018.08.005 10.7270/Q29P34C1 30096650 Cai, P; Fang, SQ; Yang, HL; Yang, XL; Liu, QH; Kong, LY; Wang, XB 9/5/2018 8/18/2020 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51144819 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 38 ChEMBL 10.1016/j.ejmech.2018.08.005 10.7270/Q29P34C1 30096650 Cai, P; Fang, SQ; Yang, HL; Yang, XL; Liu, QH; Kong, LY; Wang, XB 9/5/2018 8/18/2020 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51188481 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 22 ChEMBL 10.1007/s00044-012-0162-3 10.7270/Q25D8VS0 n/a 12/28/2013 8/31/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 51188786 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 16 ChEMBL 10.1007/s00044-012-0227-3 10.7270/Q24F1TN5 n/a 12/28/2013 8/31/2020 n/a http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 51196249 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 40 ChEMBL 10.1016/j.bmcl.2013.05.092 10.7270/Q2JD50Q1 23791077 Mohamed, T; Osman, W; Tin, G; Rao, PP 8/1/2013 9/1/2020 University of Waterloo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51198658 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 10.0 ChEMBL 10.1016/j.ejmech.2013.06.021 10.7270/Q2KW5JZX 23838422 Samadi, A; de la Fuente Revenga, M; Pérez, C; Iriepa, I; Moraleda, I; Rodríguez-Franco, MI; Marco-Contelles, J 9/28/2013 9/1/2020 Instituto De Qu£Mica Org£Nica General (Csic) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51210465 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 12 ChEMBL 10.1016/j.ejmech.2014.09.081 10.7270/Q2CF9T2R 25282266 Huang, L; Miao, H; Sun, Y; Meng, F; Li, X 11/24/2014 9/3/2020 Sun Yat-Sen University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51218670 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 22 ChEMBL 10.1016/j.bmc.2016.01.031 10.7270/Q2B85C4Q 26827140 Makhaeva, GF; Boltneva, NP; Lushchekina, SV; Serebryakova, OG; Stupina, TS; Terentiev, AA; Serkov, IV; Proshin, AN; Bachurin, SO; Richardson, RJ 3/1/2016 9/4/2020 Institute of Physiologically Active Compounds Russian Academy of Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51227518 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Mus musculus 1060 ChEMBL 10.1016/j.bmc.2018.12.007 10.7270/Q21Z47PZ 30578075 Bacalhau, P; Fernandes, L; Rosário Martins, M; Candeias, F; Carreiro, EP; López, Ó; Teresa Caldeira, A; Totobenazara, J; Guedes, RC; Burke, AJ 1/15/2019 2/18/2021 Universidade De £Vora http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 51227524 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Mus musculus 125310 ChEMBL 10.1016/j.bmc.2018.12.007 10.7270/Q21Z47PZ 30578075 Bacalhau, P; Fernandes, L; Rosário Martins, M; Candeias, F; Carreiro, EP; López, Ó; Teresa Caldeira, A; Totobenazara, J; Guedes, RC; Burke, AJ 1/15/2019 2/18/2021 Universidade De £Vora http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 51229230 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 11 ChEMBL 10.1016/j.ejmech.2019.111737 10.7270/Q24J0JCX 31581002 Bai, P; Wang, K; Zhang, P; Shi, J; Cheng, X; Zhang, Q; Zheng, C; Cheng, Y; Yang, J; Lu, X; Sang, Z 12/1/2019 2/18/2021 Chinese Academy of Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51239549 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 6.0 ChEMBL 10.1016/j.ejmech.2018.10.064 10.7270/Q2T72MRJ 30447434 Lalut, J; Santoni, G; Karila, D; Lecoutey, C; Davis, A; Nachon, F; Silman, I; Sussman, J; Weik, M; Maurice, T; Dallemagne, P; Rochais, C 1/15/2019 2/19/2021 Normandie Univ http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51248802 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 5.7 ChEMBL 10.1016/j.bmc.2019.01.025 10.7270/Q2N87F3N 30744931 Mishra, P; Kumar, A; Panda, G 3/15/2019 2/20/2021 Csir-Central Drug Research Institute http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51253587 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 40 ChEMBL 10.1016/j.bmc.2019.07.001 10.7270/Q20V8H48 31288978 Srivastava, P; Tripathi, PN; Sharma, P; Shrivastava, SK 8/15/2019 2/20/2021 Indian Institute of Technology (Banaras Hindu University) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51262098 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 12 ChEMBL 10.1016/j.ejmech.2019.111596 10.7270/Q2988BC8 31419776 Lanthier, C; Payan, H; Liparulo, I; Hatat, B; Lecoutey, C; Since, M; Davis, A; Bergamini, C; Claeysen, S; Dallemagne, P; Bolognesi, ML; Rochais, C 11/15/2019 2/21/2021 Normandie Univ http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51271852 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 5.6 ChEMBL 10.1016/j.ejmech.2019.111785 10.7270/Q2Q81HF9 31669851 Bajda, M; Łażewska, D; Godyń, J; Zaręba, P; Kuder, K; Hagenow, S; Łątka, K; Stawarska, E; Stark, H; Kieć-Kononowicz, K; Malawska, B 1/1/2020 2/23/2021 Jagiellonian University Medical College http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51276583 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 15 ChEMBL 10.1016/j.bmc.2018.11.015 10.7270/Q2WD4400 30470598 Song, Q; Li, Y; Cao, Z; Liu, H; Tian, C; Yang, Z; Qiang, X; Tan, Z; Deng, Y 12/15/2018 2/23/2021 Sichuan University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 51284481 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Mus musculus 12 ChEMBL 10.1016/j.bmcl.2019.04.051 10.7270/Q2251NM8 31078410 Huang, L; Ding, L; Li, X; Wang, N; Yan, Y; Yang, M; Cui, W; Benjamin Naman, C; Cheng, K; Zhang, W; Zhang, B; Jin, H; He, S 7/1/2019 2/24/2021 Ningbo University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 51287048 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 16 ChEMBL 10.1016/j.ejmech.2019.05.062 10.7270/Q2RF5ZGP 31158754 Purgatorio, R; de Candia, M; Catto, M; Carrieri, A; Pisani, L; De Palma, A; Toma, M; Ivanova, OA; Voskressensky, LG; Altomare, CD 9/1/2019 2/24/2021 University of Bari Aldo Moro http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51290383 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 10.0 ChEMBL 10.1016/j.ejmech.2019.01.030 10.7270/Q2VQ363K 30685536 González-Naranjo, P; Pérez-Macias, N; Pérez, C; Roca, C; Vaca, G; Girón, R; Sánchez-Robles, E; Martín-Fontelles, MI; de Ceballos, ML; Martin-Requero, A; Campillo, NE; Páez, JA 3/15/2019 2/25/2021 Instituto De Qu£Mica M£Dica (Csic) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51297463 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 59 ChEMBL 10.1016/j.ejmech.2019.111651 10.7270/Q2ZP49K2 31479975 Mahmoud, WR; Nissan, YM; Elsawah, MM; Refaey, RH; Ragab, MF; Amin, KM 11/15/2019 2/25/2021 Cairo University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51311492 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 5.7 ChEMBL 10.1016/j.bmc.2018.12.030 10.7270/Q2XP78D7 30765302 de Andrade, P; Mantoani, SP; Gonçalves Nunes, PS; Magadán, CR; Pérez, C; Xavier, DJ; Hojo, ETS; Campillo, NE; Martínez, A; Carvalho, I 3/15/2019 2/27/2021 University of S£O Paulo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51321365 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Mus musculus 1820 ChEMBL 10.1016/j.bmc.2016.07.061 10.7270/Q2765JT4 27519464 Singla, S; Piplani, P 10/1/2016 2/28/2021 Panjab University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 51322847 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 33 ChEMBL 10.1016/j.ejmech.2019.02.030 10.7270/Q2JD5192 30784883 Sharma, P; Tripathi, A; Tripathi, PN; Prajapati, SK; Seth, A; Tripathi, MK; Srivastava, P; Tiwari, V; Krishnamurthy, S; Shrivastava, SK 4/1/2019 2/28/2021 Indian Institute of Technology (Banaras Hindu University) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51322910 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Mus musculus 84 ChEMBL 10.1016/j.ejmech.2019.02.053 10.7270/Q2DN48JW 30822710 Wang, D; Hu, M; Li, X; Zhang, D; Chen, C; Fu, J; Shao, S; Shi, G; Zhou, Y; Wu, S; Zhang, T 4/15/2019 2/28/2021 Peking Union Medical College http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 51324278 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 10.0 ChEMBL 10.1021/acs.jmedchem.6b00426 10.7270/Q2SJ1Q44 27253679 Shidore, M; Machhi, J; Shingala, K; Murumkar, P; Sharma, MK; Agrawal, N; Tripathi, A; Parikh, Z; Pillai, P; Yadav, MR 6/23/2016 2/28/2021 The Maharaja Sayajirao University of Baroda http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51336042 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 13 ChEMBL 10.1021/acsmedchemlett.9b00656 10.7270/Q2WS8XS4 32435398 Catto, M; Pisani, L; de la Mora, E; Belviso, BD; Mangiatordi, GF; Pinto, A; Palma, A; Denora, N; Caliandro, R; Colletier, JP; Silman, I; Nicolotti, O; Altomare, CD 5/14/2020 8/12/2021 University of Bari Aldo Moro http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51336051 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 16 ChEMBL 10.1021/acsmedchemlett.9b00656 10.7270/Q2WS8XS4 32435398 Catto, M; Pisani, L; de la Mora, E; Belviso, BD; Mangiatordi, GF; Pinto, A; Palma, A; Denora, N; Caliandro, R; Colletier, JP; Silman, I; Nicolotti, O; Altomare, CD 5/14/2020 8/12/2021 University of Bari Aldo Moro http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51350197 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 42 ChEMBL 10.1016/j.ejmech.2019.111707 10.7270/Q2833WM3 31561043 Tripathi, A; Choubey, PK; Sharma, P; Seth, A; Tripathi, PN; Tripathi, MK; Prajapati, SK; Krishnamurthy, S; Shrivastava, SK 12/1/2019 3/21/2022 Indian Institute of Technology (Banaras Hindu University) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51350762 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 120 ChEMBL 10.1016/j.bmcl.2020.127404 10.7270/Q2P55S39 32717612 Le-Nhat-Thuy, G; Nguyen Thi, N; Pham-The, H; Dang Thi, TA; Nguyen Thi, H; Nguyen Thi, TH; Nguyen Hoang, S; Nguyen, TV 9/15/2020 3/21/2022 Viet Nam http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 51354731 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 6.0 ChEMBL 10.1039/d0md00009d 10.7270/Q2C82DXM 33479638 de Souza, MM; Andreolla, MC; Ribeiro, TC; Gonçalves, AE; Medeiros, AR; de Souza, AS; Ferreira, LLG; Andricopulo, AD; Yunes, RA; de Oliveira, AS 2/1/2020 3/22/2022 School of Health Sciences/Graduate Program In Pharmaceutical Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51356978 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 10.0 ChEMBL 10.1016/j.bmc.2020.115820 10.7270/Q2WW7N96 33120080 Lin, SX; Curtis, MA; Sperry, J 12/15/2020 3/22/2022 University of Auckland http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 51366748 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 5.0 ChEMBL 10.1016/j.bmc.2020.115940 10.7270/Q20K2D6W 33340937 Jiang, X; Wang, Y; Liu, C; Xing, C; Wang, Y; Lyu, W; Wang, S; Li, Q; Chen, T; Chen, Y; Feng, F; Liu, W; Sun, H 1/15/2021 3/24/2022 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51368515 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 148 ChEMBL 10.1016/j.bmc.2019.02.031 10.7270/Q2CJ8J40 30795991 Tripathi, PN; Srivastava, P; Sharma, P; Seth, A; Shrivastava, SK 4/1/2019 3/25/2022 Indian Institute of Technology (Banaras Hindu University) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51370619 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 42 ChEMBL 10.1016/j.bmc.2020.115721 10.7270/Q2J106T5 33007563 Choubey, PK; Tripathi, A; Sharma, P; Shrivastava, SK 11/15/2020 3/25/2022 Indian Institute of Technology (Banaras Hindu University) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51371635 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 18 ChEMBL 10.1016/j.bmcl.2020.127659 10.7270/Q28919H1 33137375 Du, H; Jiang, X; Ma, M; Xu, H; Liu, S; Ma, F 12/15/2020 3/25/2022 Xinyang Normal University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51373698 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 15 ChEMBL 10.1016/j.ejmech.2019.111958 10.7270/Q2FR0187 31865014 Sang, Z; Wang, K; Shi, J; Cheng, X; Zhu, G; Wei, R; Ma, Q; Yu, L; Zhao, Y; Tan, Z; Liu, W 2/1/2020 3/26/2022 Nanyang Normal University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 51373718 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 11 ChEMBL 10.1016/j.ejmech.2019.111958 10.7270/Q2FR0187 31865014 Sang, Z; Wang, K; Shi, J; Cheng, X; Zhu, G; Wei, R; Ma, Q; Yu, L; Zhao, Y; Tan, Z; Liu, W 2/1/2020 3/26/2022 Nanyang Normal University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51375493 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 6.0 ChEMBL 10.1016/j.ejmech.2020.112743 10.7270/Q2P272S9 32882609 Łażewska, D; Bajda, M; Kaleta, M; Zaręba, P; Doroz-Płonka, A; Siwek, A; Alachkar, A; Mogilski, S; Saad, A; Kuder, K; Olejarz-Maciej, A; Godyń, J; Stary, D; Sudoł, S; Więcek, M; Latacz, G; Walczak, M; Handzlik, J; Sadek, B; Malawska, B; Kieć-Kononowicz, K 12/1/2020 3/26/2022 Jagiellonian University Medical College http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51377763 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 48 ChEMBL 10.1016/j.ejmech.2020.113124 10.7270/Q2SJ1Q8X 33395623 Erdogan, M; Kilic, B; Sagkan, RI; Aksakal, F; Ercetin, T; Gulcan, HO; Dogruer, DS 2/15/2021 3/26/2022 Gazi University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51378984 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 32 ChEMBL 10.1016/j.bmc.2021.116074 10.7270/Q2HX1HBN 33640707 Cao, Z; Song, Q; Yu, G; Liu, Z; Cong, S; Tan, Z; Deng, Y 4/1/2021 3/26/2022 Guizhou Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51384010 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 9.0 ChEMBL 10.1021/acs.jmedchem.0c01192 10.7270/Q2XD15CH 33111525 Ye, N; Qin, W; Tian, S; Xu, Q; Wold, EA; Zhou, J; Zhen, XC 12/24/2020 3/27/2022 Soochow University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51388190 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 7120 ChEMBL 10.1021/acs.jmedchem.0c00756 10.7270/Q29Z98KD 32787143 Gabr, MT; Brogi, S 9/10/2020 3/28/2022 Stanford University School of Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51392420 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 7.0 ChEMBL 10.1016/j.ejmech.2020.113059 10.7270/Q2KP85V3 33310288 Toublet, FX; Lalut, J; Hatat, B; Lecoutey, C; Davis, A; Since, M; Corvaisier, S; Freret, T; Sopková-de Oliveira Santos, J; Claeysen, S; Boulouard, M; Dallemagne, P; Rochais, C 1/15/2021 3/29/2022 Normandie Univ http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51394068 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 27 ChEMBL 10.1016/j.ejmech.2021.113224 10.7270/Q2HM5D5K 33582578 Manzoor, S; Prajapati, SK; Majumdar, S; Raza, MK; Gabr, MT; Kumar, S; Pal, K; Rashid, H; Kumar, S; Krishnamurthy, S; Hoda, N 4/5/2021 3/29/2022 Jamia Millia Islamia http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51396698 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 14 ChEMBL 10.1016/j.ejmech.2020.112140 10.7270/Q2RV0SGV 32088494 Mozaffarnia, S; Teimuri-Mofrad, R; Rashidi, MR 4/1/2020 3/29/2022 University of Tabriz http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51396775 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 9.0 ChEMBL 10.1016/j.ejmech.2020.112180 10.7270/Q2N301PX 32131034 Sang, Z; Wang, K; Shi, J; Liu, W; Cheng, X; Zhu, G; Wang, Y; Zhao, Y; Qiao, Z; Wu, A; Tan, Z 4/15/2020 3/29/2022 Nanyang Normal University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51397323 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 30 ChEMBL 10.1016/j.ejmech.2020.112257 10.7270/Q2K35ZCB 32375073 Singh, YP; Tej, GNVC; Pandey, A; Priya, K; Pandey, P; Shankar, G; Nayak, PK; Rai, G; Chittiboyina, AG; Doerksen, RJ; Vishwakarma, S; Modi, G 7/15/2020 3/29/2022 Indian Institute of Technology (Banaras Hindu University) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51397661 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 2170 ChEMBL 10.1016/j.ejmech.2020.112368 10.7270/Q2XD15DZ 32388114 Rodríguez-Lavado, J; Gallardo-Garrido, C; Mallea, M; Bustos, V; Osorio, R; Hödar-Salazar, M; Chung, H; Araya-Maturana, R; Lorca, M; Pessoa-Mahana, CD; Mella-Raipán, J; Saitz, C; Jaque, P; Reyes-Parada, M; Iturriaga-Vásquez, P; Pessoa-Mahana, H 7/15/2020 3/29/2022 Universidad De Chile http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51398106 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 30 ChEMBL 10.1016/j.ejmech.2020.112415 10.7270/Q27P9344 32454229 Zhou, B; Li, H; Cui, Z; Li, D; Geng, H; Gao, J; Zhou, L 8/15/2020 3/29/2022 Northwest A&F University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51404156 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 60 ChEMBL 10.1016/j.bmc.2021.116385 10.7270/Q28W3J18 34481338 Singh, YP; Shankar, G; Jahan, S; Singh, G; Kumar, N; Barik, A; Upadhyay, P; Singh, L; Kamble, K; Singh, GK; Tiwari, S; Garg, P; Gupta, S; Modi, G 9/15/2021 8/19/2022 Indian Institute of Technology (Banaras Hindu University) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51408021 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 2.0 ChEMBL 10.1021/acs.jmedchem.0c01863 10.7270/Q2JW8JNQ 33570950 Zhou, Y; Fu, Y; Yin, W; Li, J; Wang, W; Bai, F; Xu, S; Gong, Q; Peng, T; Hong, Y; Zhang, D; Zhang, D; Liu, Q; Xu, Y; Xu, HE; Zhang, H; Jiang, H; Liu, H 2/25/2021 8/19/2022 Chinese Academy of Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 51408047 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 8.0 ChEMBL 10.1021/acs.jmedchem.0c01863 10.7270/Q2JW8JNQ 33570950 Zhou, Y; Fu, Y; Yin, W; Li, J; Wang, W; Bai, F; Xu, S; Gong, Q; Peng, T; Hong, Y; Zhang, D; Zhang, D; Liu, Q; Xu, Y; Xu, HE; Zhang, H; Jiang, H; Liu, H 2/25/2021 8/19/2022 Chinese Academy of Sciences http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51408846 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 15 ChEMBL 10.1016/j.ejmech.2021.113310 10.7270/Q28G8QGX 33667847 Sang, Z; Song, Q; Cao, Z; Deng, Y; Tan, Z; Zhang, L 4/15/2021 8/20/2022 Nanyang Normal University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 51417546 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 10.0 ChEMBL 10.1016/j.ejmech.2021.113541 10.7270/Q25D8WNM 34116326 Chowdhury, SR; Gu, J; Hu, Y; Wang, J; Lei, S; Tavallaie, MS; Lam, C; Lu, D; Jiang, F; Fu, L 10/15/2021 8/22/2022 Shanghai Jiao Tong University (Sjtu) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51422165 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 44 ChEMBL 10.1016/j.ejmech.2021.113663 10.7270/Q2222ZKW 34198150 Jiang, X; Liu, C; Zou, M; Xie, H; Lin, T; Lyu, W; Xu, J; Li, Y; Feng, F; Sun, H; Liu, W 11/5/2021 8/23/2022 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51422647 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 18 ChEMBL 10.1016/j.ejmech.2021.113735 10.7270/Q2H41W7X 34371367 Jiang, X; Zhang, Z; Zuo, J; Wu, C; Zha, L; Xu, Y; Wang, S; Shi, J; Liu, XH; Zhang, J; Tang, W 11/5/2021 8/23/2022 Anhui Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51433648 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 27 ChEMBL 10.1016/j.ejmech.2021.113779 10.7270/Q2TB1BQF 34418785 Pont, C; Ginex, T; Griñán-Ferré, C; Scheiner, M; Mattellone, A; Martínez, N; Arce, EM; Soriano-Fernández, Y; Naldi, M; De Simone, A; Barenys, M; Gómez-Catalán, J; Pérez, B; Sabate, R; Andrisano, V; Loza, MI; Brea, J; Bartolini, M; Bolognesi, ML; Decker, M; Pallàs, M; Luque, FJ; Muñoz-Torrero, D 12/5/2021 8/24/2022 University of Barcelona http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51436910 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Mus musculus 6100 ChEMBL 10.1021/acs.jmedchem.1c00160 10.7270/Q2FR01GX 34024109 Yao, H; Uras, G; Zhang, P; Xu, S; Yin, Y; Liu, J; Qin, S; Li, X; Allen, S; Bai, R; Gong, Q; Zhang, H; Zhu, Z; Xu, J 6/10/2021 3/5/2023 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 51440962 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Rattus norvegicus 43 ChEMBL 10.1016/j.ejmech.2021.113827 10.7270/Q2222ZP7 34530383 Ip, FCF; Fu, G; Yang, F; Kang, F; Sun, P; Ling, CY; Cheung, K; Xie, F; Hu, Y; Fu, L; Ip, NY 12/15/2021 3/5/2023 The Hong Kong University of Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1043&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_RAT P37136 51449752 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Mus musculus 6.2 ChEMBL 10.1016/j.ejmech.2021.114045 10.7270/Q29K4G4C 34922191 Li, X; Li, J; Huang, Y; Gong, Q; Fu, Y; Xu, Y; Huang, J; You, H; Zhang, D; Zhang, D; Mao, F; Zhu, J; Wang, H; Zhang, H; Li, J 2/5/2022 3/7/2023 East China University of Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 51449893 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 7.4 ChEMBL 10.1016/j.ejmech.2021.114045 10.7270/Q29K4G4C 34922191 Li, X; Li, J; Huang, Y; Gong, Q; Fu, Y; Xu, Y; Huang, J; You, H; Zhang, D; Zhang, D; Mao, F; Zhu, J; Wang, H; Zhang, H; Li, J 2/5/2022 3/7/2023 East China University of Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51451290 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 23 ChEMBL 10.1021/acs.jmedchem.1c01784 10.7270/Q2BG2SWG 35195417 Rullo, M; Cipolloni, M; Catto, M; Colliva, C; Miniero, DV; Latronico, T; de Candia, M; Benicchi, T; Linusson, A; Giacchè, N; Altomare, CD; Pisani, L 3/10/2022 3/7/2023 University of Bari "Aldo Moro http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51460755 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 17 ChEMBL 10.7270/Q2BV7MK2 35923722 Paolino, M; Rullo, M; Maramai, S; de Candia, M; Pisani, L; Catto, M; Mugnaini, C; Brizzi, A; Cappelli, A; Olivucci, M; Corelli, F; Altomare, CD 7/20/2022 6/18/2023 Universit� http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51462461 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 87.0 ChEMBL 10.7270/Q2J67MWD 36561075 Machado, V; Cenci, AR; Teixeira, KF; Sens, L; Tizziani, T; Nunes, RJ; Ferreira, LLG; Yunes, RA; Sandjo, LP; Andricopulo, AD; de Oliveira, AS 12/14/2022 6/19/2023 Federal University of Santa Catarina http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51470085 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 60 ChEMBL 10.7270/Q2J38XKF 36084304 Turgutalp, B; Bhattarai, P; Ercetin, T; Luise, C; Reis, R; Gurdal, EE; Isaak, A; Biriken, D; Dinter, E; Sipahi, H; Schepmann, D; Junker, A; Wünsch, B; Sippl, W; Gulcan, HO; Kizil, C; Yarim, M 9/22/2022 6/20/2023 Yeditepe University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51471672 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 17 ChEMBL 10.7270/Q2JS9VF3 35462163 Brunetti, L; Leuci, R; Carrieri, A; Catto, M; Occhineri, S; Vinci, G; Gambacorta, L; Baltrukevich, H; Chaves, S; Laghezza, A; Altomare, CD; Tortorella, P; Santos, MA; Loiodice, F; Piemontese, L 7/5/2022 6/21/2023 University of Bari Aldo Moro http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51475772 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 4.0 ChEMBL 10.7270/Q2445RHZ 35276424 Fantacuzzi, M; Amoroso, R; Carradori, S; De Filippis, B 4/5/2022 6/21/2023 "G. D'Annunzio" University of Chieti-Pescara http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51483469 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 59 ChEMBL 10.7270/Q2BP06TV 34743062 Sheng, K; Song, Y; Lei, F; Zhao, W; Fan, L; Wu, L; Liu, Y; Wu, S; Zhang, Y 1/5/2022 6/22/2023 Northwest University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51497993 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 54 ChEMBL 10.7270/Q2445RKV 35101650 Waly, OM; Saad, KM; El-Subbagh, HI; Bayomi, SM; Ghaly, MA 3/5/2022 6/24/2023 Mansoura University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51500709 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Mus musculus 5.4 ChEMBL 10.7270/Q26M3BX2 35339839 Liu, Y; Uras, G; Onuwaje, I; Li, W; Yao, H; Xu, S; Li, X; Li, X; Phillips, J; Allen, S; Gong, Q; Zhang, H; Zhu, Z; Liu, J; Xu, J 5/5/2022 6/25/2023 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 51517021 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 32 ChEMBL 10.7270/Q2F19402 33984802 Ferreira, JPS; Albuquerque, HMT; Cardoso, SM; Silva, AMS; Silva, VLM 10/5/2021 4/21/2024 University of Aveiro http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51521399 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 44 ChEMBL 10.7270/Q2BP071Z 36223681 Wang, Y; Xiong, B; Lin, H; Li, Q; Yang, H; Qiao, Y; Li, Q; Xu, Z; Lyu, W; Qu, W; Liu, W; Chen, Y; Feng, F; Sun, H 12/15/2022 4/21/2024 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51521597 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 198000 ChEMBL 10.7270/Q2SN0F6C 36257284 Li, X; Li, T; Zhang, P; Li, X; Lu, L; Sun, Y; Zhang, B; Allen, S; White, L; Phillips, J; Zhu, Z; Yao, H; Xu, J 12/15/2022 4/21/2024 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51526387 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 16 ChEMBL 10.7270/Q2FR01VV 37003157 Asproni, B; Catto, M; Loriga, G; Murineddu, G; Corona, P; Purgatorio, R; Cichero, E; Fossa, P; Scarano, N; Martínez, AL; Brea, J; Pinna, GA 4/15/2023 4/22/2024 University of Sassari http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51543171 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 17 ChEMBL 10.7270/Q2TT4W9N 36753881 Tonelli, M; Catto, M; Sabaté, R; Francesconi, V; Laurini, E; Pricl, S; Pisani, L; Miniero, DV; Liuzzi, GM; Gatta, E; Relini, A; Gavín, R; Del Rio, JA; Sparatore, F; Carotti, A 3/15/2023 12/15/2024 University of Genoa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51544452 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 3.9 ChEMBL 10.7270/Q2J67N96 38516603 Ţînţaş, ML; Peauger, L; Barré, A; Papamicaël, C; Besson, T; Sopkovà-de Oliveira Santos, J; Gembus, V; Levacher, V 3/20/2024 12/16/2024 University of Rouen Normandy http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51548103 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 21 ChEMBL 10.7270/Q20R9TSV 35987018 Guo, J; Cheng, M; Liu, P; Cao, D; Luo, J; Wan, Y; Fang, Y; Jin, Y; Xie, SS; Liu, J 11/15/2022 12/17/2024 Jiangxi University of Chinese Medicine http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51555187 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 80 ChEMBL 10.7270/Q24F1W48 38008338 Nguyen, HT; Tuan, AN; Thi, TAD; Van, KT; Le-Nhat-Thuy, G; Thi, PH; Thi, QGN; Thi, CB; Quang, HT; Van Nguyen, T 1/15/2024 12/18/2024 Vietnam Academy of Science and Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51555781 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 79 ChEMBL 10.7270/Q2Q244NH 38283217 Pourtaher, H; Mohammadi, Y; Hasaninejad, A; Iraji, A 1/25/2024 12/18/2024 Persian Gulf University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50252493 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 93000 ChEMBL 10.1016/j.bmcl.2014.10.055 10.7270/Q28G8N9V 25453812 Wei, Z; Liu, YQ; Zhou, XB; Luo, Y; Huang, CQ; Wang, YA; Zheng, ZB; Li, S 12/3/2014 3/15/2016 Institute of Pharmacology and Toxicology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50252498 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 27000 ChEMBL 10.1016/j.bmcl.2014.10.055 10.7270/Q28G8N9V 25453812 Wei, Z; Liu, YQ; Zhou, XB; Luo, Y; Huang, CQ; Wang, YA; Zheng, ZB; Li, S 12/3/2014 3/15/2016 Institute of Pharmacology and Toxicology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50252520 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 1360000 ChEMBL 10.1016/j.bmcl.2014.10.055 10.7270/Q28G8N9V 25453812 Wei, Z; Liu, YQ; Zhou, XB; Luo, Y; Huang, CQ; Wang, YA; Zheng, ZB; Li, S 12/3/2014 3/15/2016 Institute of Pharmacology and Toxicology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50832331 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 15000 ChEMBL 10.1016/j.bmc.2017.06.041 10.7270/Q2SJ1P2T 28684009 Wei, Z; Liu, YQ; Wang, SZ; Yao, L; Nie, HF; Wang, YA; Liu, XY; Zheng, ZB; Li, S 8/15/2017 1/12/2020 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50832338 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 234000 ChEMBL 10.1016/j.bmc.2017.06.041 10.7270/Q2SJ1P2T 28684009 Wei, Z; Liu, YQ; Wang, SZ; Yao, L; Nie, HF; Wang, YA; Liu, XY; Zheng, ZB; Li, S 8/15/2017 1/12/2020 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50832469 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 667800 ChEMBL 10.1016/j.bmc.2017.06.041 10.7270/Q2SJ1P2T 28684009 Wei, Z; Liu, YQ; Wang, SZ; Yao, L; Nie, HF; Wang, YA; Liu, XY; Zheng, ZB; Li, S 8/15/2017 1/12/2020 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51394264 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 636000 ChEMBL 10.1016/j.ejmech.2021.113286 10.7270/Q2ZP49VN 33611189 Wei, Z; Yang, J; Liu, Y; Nie, H; Yao, L; Yang, J; Guo, L; Zheng, Z; Ouyang, Q 4/5/2021 3/29/2022 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51394283 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 60300 ChEMBL 10.1016/j.ejmech.2021.113286 10.7270/Q2ZP49VN 33611189 Wei, Z; Yang, J; Liu, Y; Nie, H; Yao, L; Yang, J; Guo, L; Zheng, Z; Ouyang, Q 4/5/2021 3/29/2022 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51394291 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 29300 ChEMBL 10.1016/j.ejmech.2021.113286 10.7270/Q2ZP49VN 33611189 Wei, Z; Yang, J; Liu, Y; Nie, H; Yao, L; Yang, J; Guo, L; Zheng, Z; Ouyang, Q 4/5/2021 3/29/2022 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50252493 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 93000 ChEMBL 10.1016/j.bmcl.2014.10.055 10.7270/Q28G8N9V 25453812 Wei, Z; Liu, YQ; Zhou, XB; Luo, Y; Huang, CQ; Wang, YA; Zheng, ZB; Li, S 12/3/2014 3/15/2016 Institute of Pharmacology and Toxicology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50252498 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 27000 ChEMBL 10.1016/j.bmcl.2014.10.055 10.7270/Q28G8N9V 25453812 Wei, Z; Liu, YQ; Zhou, XB; Luo, Y; Huang, CQ; Wang, YA; Zheng, ZB; Li, S 12/3/2014 3/15/2016 Institute of Pharmacology and Toxicology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50252520 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 1360000 ChEMBL 10.1016/j.bmcl.2014.10.055 10.7270/Q28G8N9V 25453812 Wei, Z; Liu, YQ; Zhou, XB; Luo, Y; Huang, CQ; Wang, YA; Zheng, ZB; Li, S 12/3/2014 3/15/2016 Institute of Pharmacology and Toxicology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50832331 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 15000 ChEMBL 10.1016/j.bmc.2017.06.041 10.7270/Q2SJ1P2T 28684009 Wei, Z; Liu, YQ; Wang, SZ; Yao, L; Nie, HF; Wang, YA; Liu, XY; Zheng, ZB; Li, S 8/15/2017 1/12/2020 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50832338 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 234000 ChEMBL 10.1016/j.bmc.2017.06.041 10.7270/Q2SJ1P2T 28684009 Wei, Z; Liu, YQ; Wang, SZ; Yao, L; Nie, HF; Wang, YA; Liu, XY; Zheng, ZB; Li, S 8/15/2017 1/12/2020 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50832469 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 667800 ChEMBL 10.1016/j.bmc.2017.06.041 10.7270/Q2SJ1P2T 28684009 Wei, Z; Liu, YQ; Wang, SZ; Yao, L; Nie, HF; Wang, YA; Liu, XY; Zheng, ZB; Li, S 8/15/2017 1/12/2020 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51394264 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 636000 ChEMBL 10.1016/j.ejmech.2021.113286 10.7270/Q2ZP49VN 33611189 Wei, Z; Yang, J; Liu, Y; Nie, H; Yao, L; Yang, J; Guo, L; Zheng, Z; Ouyang, Q 4/5/2021 3/29/2022 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51394283 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 60300 ChEMBL 10.1016/j.ejmech.2021.113286 10.7270/Q2ZP49VN 33611189 Wei, Z; Yang, J; Liu, Y; Nie, H; Yao, L; Yang, J; Guo, L; Zheng, Z; Ouyang, Q 4/5/2021 3/29/2022 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51394291 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 29300 ChEMBL 10.1016/j.ejmech.2021.113286 10.7270/Q2ZP49VN 33611189 Wei, Z; Yang, J; Liu, Y; Nie, H; Yao, L; Yang, J; Guo, L; Zheng, Z; Ouyang, Q 4/5/2021 3/29/2022 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50252493 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 93000 ChEMBL 10.1016/j.bmcl.2014.10.055 10.7270/Q28G8N9V 25453812 Wei, Z; Liu, YQ; Zhou, XB; Luo, Y; Huang, CQ; Wang, YA; Zheng, ZB; Li, S 12/3/2014 3/15/2016 Institute of Pharmacology and Toxicology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50252498 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 27000 ChEMBL 10.1016/j.bmcl.2014.10.055 10.7270/Q28G8N9V 25453812 Wei, Z; Liu, YQ; Zhou, XB; Luo, Y; Huang, CQ; Wang, YA; Zheng, ZB; Li, S 12/3/2014 3/15/2016 Institute of Pharmacology and Toxicology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50252520 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 1360000 ChEMBL 10.1016/j.bmcl.2014.10.055 10.7270/Q28G8N9V 25453812 Wei, Z; Liu, YQ; Zhou, XB; Luo, Y; Huang, CQ; Wang, YA; Zheng, ZB; Li, S 12/3/2014 3/15/2016 Institute of Pharmacology and Toxicology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50832331 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 15000 ChEMBL 10.1016/j.bmc.2017.06.041 10.7270/Q2SJ1P2T 28684009 Wei, Z; Liu, YQ; Wang, SZ; Yao, L; Nie, HF; Wang, YA; Liu, XY; Zheng, ZB; Li, S 8/15/2017 1/12/2020 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50832338 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 234000 ChEMBL 10.1016/j.bmc.2017.06.041 10.7270/Q2SJ1P2T 28684009 Wei, Z; Liu, YQ; Wang, SZ; Yao, L; Nie, HF; Wang, YA; Liu, XY; Zheng, ZB; Li, S 8/15/2017 1/12/2020 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50832469 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 667800 ChEMBL 10.1016/j.bmc.2017.06.041 10.7270/Q2SJ1P2T 28684009 Wei, Z; Liu, YQ; Wang, SZ; Yao, L; Nie, HF; Wang, YA; Liu, XY; Zheng, ZB; Li, S 8/15/2017 1/12/2020 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51394264 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 636000 ChEMBL 10.1016/j.ejmech.2021.113286 10.7270/Q2ZP49VN 33611189 Wei, Z; Yang, J; Liu, Y; Nie, H; Yao, L; Yang, J; Guo, L; Zheng, Z; Ouyang, Q 4/5/2021 3/29/2022 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51394283 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 60300 ChEMBL 10.1016/j.ejmech.2021.113286 10.7270/Q2ZP49VN 33611189 Wei, Z; Yang, J; Liu, Y; Nie, H; Yao, L; Yang, J; Guo, L; Zheng, Z; Ouyang, Q 4/5/2021 3/29/2022 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51394291 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 29300 ChEMBL 10.1016/j.ejmech.2021.113286 10.7270/Q2ZP49VN 33611189 Wei, Z; Yang, J; Liu, Y; Nie, H; Yao, L; Yang, J; Guo, L; Zheng, Z; Ouyang, Q 4/5/2021 3/29/2022 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50082734 c1c[n+](ccc1C(=O)N)COC[n+]2ccc(cc2\C=N\O)\C=N\O InChI=1S/C15H15N5O4/c16-15(21)13-2-4-19(5-3-13)10-24-11-20-6-1-12(8-17-22)7-14(20)9-18-23/h1-9H,10-11H2,(H2-,16,21,22,23)/p+2 SODKCPHRJDOHMI-UHFFFAOYSA-P 50005571 CHEMBL139138::CHEMBL2181429 Acetylcholinesterase Homo sapiens 7800 ChEMBL 10.1016/j.ejmech.2014.03.044 10.7270/Q2RJ4M0X 24704618 Kliachyna, M; Santoni, G; Nussbaum, V; Renou, J; Sanson, B; Colletier, JP; Arboléas, M; Loiodice, M; Weik, M; Jean, L; Renard, PY; Nachon, F; Baati, R 4/14/2014 2/7/2015 University of Strasburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50005571 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50005571&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HLO 2JEY,2JEZ,6NEA 135520674 103919046 CHEMBL2181429CHEMBL139138 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50082738 c1c[n+](ccc1C(=O)N)COC[n+]2ccc(cc2\C=N\O)\C=N\O InChI=1S/C15H15N5O4/c16-15(21)13-2-4-19(5-3-13)10-24-11-20-6-1-12(8-17-22)7-14(20)9-18-23/h1-9H,10-11H2,(H2-,16,21,22,23)/p+2 SODKCPHRJDOHMI-UHFFFAOYSA-P 50005571 CHEMBL139138::CHEMBL2181429 Acetylcholinesterase Homo sapiens 106000 ChEMBL 10.1016/j.ejmech.2014.03.044 10.7270/Q2RJ4M0X 24704618 Kliachyna, M; Santoni, G; Nussbaum, V; Renou, J; Sanson, B; Colletier, JP; Arboléas, M; Loiodice, M; Weik, M; Jean, L; Renard, PY; Nachon, F; Baati, R 4/14/2014 2/7/2015 University of Strasburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50005571 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50005571&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HLO 2JEY,2JEZ,6NEA 135520674 103919046 CHEMBL2181429CHEMBL139138 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50082743 c1c[n+](ccc1C(=O)N)COC[n+]2ccc(cc2\C=N\O)\C=N\O InChI=1S/C15H15N5O4/c16-15(21)13-2-4-19(5-3-13)10-24-11-20-6-1-12(8-17-22)7-14(20)9-18-23/h1-9H,10-11H2,(H2-,16,21,22,23)/p+2 SODKCPHRJDOHMI-UHFFFAOYSA-P 50005571 CHEMBL139138::CHEMBL2181429 Acetylcholinesterase Homo sapiens 210000 ChEMBL 10.1016/j.ejmech.2014.03.044 10.7270/Q2RJ4M0X 24704618 Kliachyna, M; Santoni, G; Nussbaum, V; Renou, J; Sanson, B; Colletier, JP; Arboléas, M; Loiodice, M; Weik, M; Jean, L; Renard, PY; Nachon, F; Baati, R 4/14/2014 2/7/2015 University of Strasburg http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50005571 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50005571&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HLO 2JEY,2JEZ,6NEA 135520674 103919046 CHEMBL2181429CHEMBL139138 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50252493 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 93000 ChEMBL 10.1016/j.bmcl.2014.10.055 10.7270/Q28G8N9V 25453812 Wei, Z; Liu, YQ; Zhou, XB; Luo, Y; Huang, CQ; Wang, YA; Zheng, ZB; Li, S 12/3/2014 3/15/2016 Institute of Pharmacology and Toxicology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50252498 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 27000 ChEMBL 10.1016/j.bmcl.2014.10.055 10.7270/Q28G8N9V 25453812 Wei, Z; Liu, YQ; Zhou, XB; Luo, Y; Huang, CQ; Wang, YA; Zheng, ZB; Li, S 12/3/2014 3/15/2016 Institute of Pharmacology and Toxicology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50252520 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 1360000 ChEMBL 10.1016/j.bmcl.2014.10.055 10.7270/Q28G8N9V 25453812 Wei, Z; Liu, YQ; Zhou, XB; Luo, Y; Huang, CQ; Wang, YA; Zheng, ZB; Li, S 12/3/2014 3/15/2016 Institute of Pharmacology and Toxicology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50832331 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 15000 ChEMBL 10.1016/j.bmc.2017.06.041 10.7270/Q2SJ1P2T 28684009 Wei, Z; Liu, YQ; Wang, SZ; Yao, L; Nie, HF; Wang, YA; Liu, XY; Zheng, ZB; Li, S 8/15/2017 1/12/2020 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50832338 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 234000 ChEMBL 10.1016/j.bmc.2017.06.041 10.7270/Q2SJ1P2T 28684009 Wei, Z; Liu, YQ; Wang, SZ; Yao, L; Nie, HF; Wang, YA; Liu, XY; Zheng, ZB; Li, S 8/15/2017 1/12/2020 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50832469 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 667800 ChEMBL 10.1016/j.bmc.2017.06.041 10.7270/Q2SJ1P2T 28684009 Wei, Z; Liu, YQ; Wang, SZ; Yao, L; Nie, HF; Wang, YA; Liu, XY; Zheng, ZB; Li, S 8/15/2017 1/12/2020 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51394264 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 636000 ChEMBL 10.1016/j.ejmech.2021.113286 10.7270/Q2ZP49VN 33611189 Wei, Z; Yang, J; Liu, Y; Nie, H; Yao, L; Yang, J; Guo, L; Zheng, Z; Ouyang, Q 4/5/2021 3/29/2022 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51394283 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 60300 ChEMBL 10.1016/j.ejmech.2021.113286 10.7270/Q2ZP49VN 33611189 Wei, Z; Yang, J; Liu, Y; Nie, H; Yao, L; Yang, J; Guo, L; Zheng, Z; Ouyang, Q 4/5/2021 3/29/2022 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51394291 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 29300 ChEMBL 10.1016/j.ejmech.2021.113286 10.7270/Q2ZP49VN 33611189 Wei, Z; Yang, J; Liu, Y; Nie, H; Yao, L; Yang, J; Guo, L; Zheng, Z; Ouyang, Q 4/5/2021 3/29/2022 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50252493 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 93000 ChEMBL 10.1016/j.bmcl.2014.10.055 10.7270/Q28G8N9V 25453812 Wei, Z; Liu, YQ; Zhou, XB; Luo, Y; Huang, CQ; Wang, YA; Zheng, ZB; Li, S 12/3/2014 3/15/2016 Institute of Pharmacology and Toxicology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50252498 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 27000 ChEMBL 10.1016/j.bmcl.2014.10.055 10.7270/Q28G8N9V 25453812 Wei, Z; Liu, YQ; Zhou, XB; Luo, Y; Huang, CQ; Wang, YA; Zheng, ZB; Li, S 12/3/2014 3/15/2016 Institute of Pharmacology and Toxicology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50252520 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 1360000 ChEMBL 10.1016/j.bmcl.2014.10.055 10.7270/Q28G8N9V 25453812 Wei, Z; Liu, YQ; Zhou, XB; Luo, Y; Huang, CQ; Wang, YA; Zheng, ZB; Li, S 12/3/2014 3/15/2016 Institute of Pharmacology and Toxicology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50832331 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 15000 ChEMBL 10.1016/j.bmc.2017.06.041 10.7270/Q2SJ1P2T 28684009 Wei, Z; Liu, YQ; Wang, SZ; Yao, L; Nie, HF; Wang, YA; Liu, XY; Zheng, ZB; Li, S 8/15/2017 1/12/2020 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50832338 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 234000 ChEMBL 10.1016/j.bmc.2017.06.041 10.7270/Q2SJ1P2T 28684009 Wei, Z; Liu, YQ; Wang, SZ; Yao, L; Nie, HF; Wang, YA; Liu, XY; Zheng, ZB; Li, S 8/15/2017 1/12/2020 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50832469 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 667800 ChEMBL 10.1016/j.bmc.2017.06.041 10.7270/Q2SJ1P2T 28684009 Wei, Z; Liu, YQ; Wang, SZ; Yao, L; Nie, HF; Wang, YA; Liu, XY; Zheng, ZB; Li, S 8/15/2017 1/12/2020 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51394264 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 636000 ChEMBL 10.1016/j.ejmech.2021.113286 10.7270/Q2ZP49VN 33611189 Wei, Z; Yang, J; Liu, Y; Nie, H; Yao, L; Yang, J; Guo, L; Zheng, Z; Ouyang, Q 4/5/2021 3/29/2022 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51394283 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 60300 ChEMBL 10.1016/j.ejmech.2021.113286 10.7270/Q2ZP49VN 33611189 Wei, Z; Yang, J; Liu, Y; Nie, H; Yao, L; Yang, J; Guo, L; Zheng, Z; Ouyang, Q 4/5/2021 3/29/2022 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51394291 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 29300 ChEMBL 10.1016/j.ejmech.2021.113286 10.7270/Q2ZP49VN 33611189 Wei, Z; Yang, J; Liu, Y; Nie, H; Yao, L; Yang, J; Guo, L; Zheng, Z; Ouyang, Q 4/5/2021 3/29/2022 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50252493 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 93000 ChEMBL 10.1016/j.bmcl.2014.10.055 10.7270/Q28G8N9V 25453812 Wei, Z; Liu, YQ; Zhou, XB; Luo, Y; Huang, CQ; Wang, YA; Zheng, ZB; Li, S 12/3/2014 3/15/2016 Institute of Pharmacology and Toxicology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50252498 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 27000 ChEMBL 10.1016/j.bmcl.2014.10.055 10.7270/Q28G8N9V 25453812 Wei, Z; Liu, YQ; Zhou, XB; Luo, Y; Huang, CQ; Wang, YA; Zheng, ZB; Li, S 12/3/2014 3/15/2016 Institute of Pharmacology and Toxicology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50252520 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 1360000 ChEMBL 10.1016/j.bmcl.2014.10.055 10.7270/Q28G8N9V 25453812 Wei, Z; Liu, YQ; Zhou, XB; Luo, Y; Huang, CQ; Wang, YA; Zheng, ZB; Li, S 12/3/2014 3/15/2016 Institute of Pharmacology and Toxicology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50832331 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 15000 ChEMBL 10.1016/j.bmc.2017.06.041 10.7270/Q2SJ1P2T 28684009 Wei, Z; Liu, YQ; Wang, SZ; Yao, L; Nie, HF; Wang, YA; Liu, XY; Zheng, ZB; Li, S 8/15/2017 1/12/2020 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50832338 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 234000 ChEMBL 10.1016/j.bmc.2017.06.041 10.7270/Q2SJ1P2T 28684009 Wei, Z; Liu, YQ; Wang, SZ; Yao, L; Nie, HF; Wang, YA; Liu, XY; Zheng, ZB; Li, S 8/15/2017 1/12/2020 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50832469 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 667800 ChEMBL 10.1016/j.bmc.2017.06.041 10.7270/Q2SJ1P2T 28684009 Wei, Z; Liu, YQ; Wang, SZ; Yao, L; Nie, HF; Wang, YA; Liu, XY; Zheng, ZB; Li, S 8/15/2017 1/12/2020 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51394264 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 636000 ChEMBL 10.1016/j.ejmech.2021.113286 10.7270/Q2ZP49VN 33611189 Wei, Z; Yang, J; Liu, Y; Nie, H; Yao, L; Yang, J; Guo, L; Zheng, Z; Ouyang, Q 4/5/2021 3/29/2022 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51394283 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 60300 ChEMBL 10.1016/j.ejmech.2021.113286 10.7270/Q2ZP49VN 33611189 Wei, Z; Yang, J; Liu, Y; Nie, H; Yao, L; Yang, J; Guo, L; Zheng, Z; Ouyang, Q 4/5/2021 3/29/2022 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51394291 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 29300 ChEMBL 10.1016/j.ejmech.2021.113286 10.7270/Q2ZP49VN 33611189 Wei, Z; Yang, J; Liu, Y; Nie, H; Yao, L; Yang, J; Guo, L; Zheng, Z; Ouyang, Q 4/5/2021 3/29/2022 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50252493 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 93000 ChEMBL 10.1016/j.bmcl.2014.10.055 10.7270/Q28G8N9V 25453812 Wei, Z; Liu, YQ; Zhou, XB; Luo, Y; Huang, CQ; Wang, YA; Zheng, ZB; Li, S 12/3/2014 3/15/2016 Institute of Pharmacology and Toxicology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50252498 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 27000 ChEMBL 10.1016/j.bmcl.2014.10.055 10.7270/Q28G8N9V 25453812 Wei, Z; Liu, YQ; Zhou, XB; Luo, Y; Huang, CQ; Wang, YA; Zheng, ZB; Li, S 12/3/2014 3/15/2016 Institute of Pharmacology and Toxicology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50252520 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 1360000 ChEMBL 10.1016/j.bmcl.2014.10.055 10.7270/Q28G8N9V 25453812 Wei, Z; Liu, YQ; Zhou, XB; Luo, Y; Huang, CQ; Wang, YA; Zheng, ZB; Li, S 12/3/2014 3/15/2016 Institute of Pharmacology and Toxicology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50832331 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 15000 ChEMBL 10.1016/j.bmc.2017.06.041 10.7270/Q2SJ1P2T 28684009 Wei, Z; Liu, YQ; Wang, SZ; Yao, L; Nie, HF; Wang, YA; Liu, XY; Zheng, ZB; Li, S 8/15/2017 1/12/2020 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50832338 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 234000 ChEMBL 10.1016/j.bmc.2017.06.041 10.7270/Q2SJ1P2T 28684009 Wei, Z; Liu, YQ; Wang, SZ; Yao, L; Nie, HF; Wang, YA; Liu, XY; Zheng, ZB; Li, S 8/15/2017 1/12/2020 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50832469 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 667800 ChEMBL 10.1016/j.bmc.2017.06.041 10.7270/Q2SJ1P2T 28684009 Wei, Z; Liu, YQ; Wang, SZ; Yao, L; Nie, HF; Wang, YA; Liu, XY; Zheng, ZB; Li, S 8/15/2017 1/12/2020 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51394264 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 636000 ChEMBL 10.1016/j.ejmech.2021.113286 10.7270/Q2ZP49VN 33611189 Wei, Z; Yang, J; Liu, Y; Nie, H; Yao, L; Yang, J; Guo, L; Zheng, Z; Ouyang, Q 4/5/2021 3/29/2022 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51394283 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 60300 ChEMBL 10.1016/j.ejmech.2021.113286 10.7270/Q2ZP49VN 33611189 Wei, Z; Yang, J; Liu, Y; Nie, H; Yao, L; Yang, J; Guo, L; Zheng, Z; Ouyang, Q 4/5/2021 3/29/2022 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51394291 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 29300 ChEMBL 10.1016/j.ejmech.2021.113286 10.7270/Q2ZP49VN 33611189 Wei, Z; Yang, J; Liu, Y; Nie, H; Yao, L; Yang, J; Guo, L; Zheng, Z; Ouyang, Q 4/5/2021 3/29/2022 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50252493 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 93000 ChEMBL 10.1016/j.bmcl.2014.10.055 10.7270/Q28G8N9V 25453812 Wei, Z; Liu, YQ; Zhou, XB; Luo, Y; Huang, CQ; Wang, YA; Zheng, ZB; Li, S 12/3/2014 3/15/2016 Institute of Pharmacology and Toxicology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50252498 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 27000 ChEMBL 10.1016/j.bmcl.2014.10.055 10.7270/Q28G8N9V 25453812 Wei, Z; Liu, YQ; Zhou, XB; Luo, Y; Huang, CQ; Wang, YA; Zheng, ZB; Li, S 12/3/2014 3/15/2016 Institute of Pharmacology and Toxicology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50252520 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 1360000 ChEMBL 10.1016/j.bmcl.2014.10.055 10.7270/Q28G8N9V 25453812 Wei, Z; Liu, YQ; Zhou, XB; Luo, Y; Huang, CQ; Wang, YA; Zheng, ZB; Li, S 12/3/2014 3/15/2016 Institute of Pharmacology and Toxicology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50832331 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 15000 ChEMBL 10.1016/j.bmc.2017.06.041 10.7270/Q2SJ1P2T 28684009 Wei, Z; Liu, YQ; Wang, SZ; Yao, L; Nie, HF; Wang, YA; Liu, XY; Zheng, ZB; Li, S 8/15/2017 1/12/2020 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50832338 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 234000 ChEMBL 10.1016/j.bmc.2017.06.041 10.7270/Q2SJ1P2T 28684009 Wei, Z; Liu, YQ; Wang, SZ; Yao, L; Nie, HF; Wang, YA; Liu, XY; Zheng, ZB; Li, S 8/15/2017 1/12/2020 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50832469 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 667800 ChEMBL 10.1016/j.bmc.2017.06.041 10.7270/Q2SJ1P2T 28684009 Wei, Z; Liu, YQ; Wang, SZ; Yao, L; Nie, HF; Wang, YA; Liu, XY; Zheng, ZB; Li, S 8/15/2017 1/12/2020 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51394264 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 636000 ChEMBL 10.1016/j.ejmech.2021.113286 10.7270/Q2ZP49VN 33611189 Wei, Z; Yang, J; Liu, Y; Nie, H; Yao, L; Yang, J; Guo, L; Zheng, Z; Ouyang, Q 4/5/2021 3/29/2022 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51394283 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 60300 ChEMBL 10.1016/j.ejmech.2021.113286 10.7270/Q2ZP49VN 33611189 Wei, Z; Yang, J; Liu, Y; Nie, H; Yao, L; Yang, J; Guo, L; Zheng, Z; Ouyang, Q 4/5/2021 3/29/2022 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51394291 c1cc[n+](c(c1)\C=N\O)COC[n+]2ccc(cc2)C(=O)N InChI=1S/C14H14N4O3/c15-14(19)12-4-7-17(8-5-12)10-21-11-18-6-2-1-3-13(18)9-16-20/h1-9H,10-11H2,(H-,15,19)/p+2 FJZDLOMCEPUCII-UHFFFAOYSA-P 50035852 HI-6 Acetylcholinesterase Homo sapiens 29300 ChEMBL 10.1016/j.ejmech.2021.113286 10.7270/Q2ZP49VN 33611189 Wei, Z; Yang, J; Liu, Y; Nie, H; Yao, L; Yang, J; Guo, L; Zheng, Z; Ouyang, Q 4/5/2021 3/29/2022 Fourth Military Medical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50035852 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50035852&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HI6 2GYU,2WHP,2WHQ,2WU3,3ZLV,5FPP,5HF9,6CQU,6CQV,6CQW,6CQY,6NTG,6NTM,6NTN,6WUY,6WV1,6WVO 6538225 103943777 C02658 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51350535 c1ccc2c(c1)c(c3c(n2)CCCC3)NCCN=[N+]=[N-] InChI=1S/C15H17N5/c16-20-18-10-9-17-15-11-5-1-3-7-13(11)19-14-8-4-2-6-12(14)15/h1,3,5,7H,2,4,6,8-10H2,(H,17,19) ANJRGTMSMVLPLB-UHFFFAOYSA-N 50546263 CHEMBL4749021 Acetylcholinesterase Mus musculus 10.0 ChEMBL 10.1021/acs.jmedchem.0c00242 10.7270/Q2KD22HB 32539387 Bancet, A; Raingeval, C; Lomberget, T; Le Borgne, M; Guichou, JF; Krimm, I 10/22/2020 3/21/2022 University of Lyon http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50546263 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50546263&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search TZ2 5EIE,5EIH 86032728 461690026 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 51350535 c1ccc2c(c1)c(c3c(n2)CCCC3)NCCN=[N+]=[N-] InChI=1S/C15H17N5/c16-20-18-10-9-17-15-11-5-1-3-7-13(11)19-14-8-4-2-6-12(14)15/h1,3,5,7H,2,4,6,8-10H2,(H,17,19) ANJRGTMSMVLPLB-UHFFFAOYSA-N 50546263 CHEMBL4749021 Acetylcholinesterase Mus musculus 10.0 ChEMBL 10.1021/acs.jmedchem.0c00242 10.7270/Q2KD22HB 32539387 Bancet, A; Raingeval, C; Lomberget, T; Le Borgne, M; Guichou, JF; Krimm, I 10/22/2020 3/21/2022 University of Lyon http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50546263 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50546263&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search TZ2 5EIE,5EIH 86032728 461690026 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL 1Q84,1Q83,1KU6,9SNJ,9SND,8ORC,7R4E,7R3C,7R2F,7R0A,7R02,7QYN,7QB4,7QAK,6TD2,5FKJ,5EIH,5EIE,5EIA,5EHZ,5EHQ,5EHN,4BTL,4BC1,4BC0,3ZLV,3ZLU,3ZLT,2WLS,2HA3,2HA2,2HA0,2H9Y,2GYW,2GYV,2GYU,1N5R,1MAH,1J07,1J06,5DTJ,5DTI,1N5M,5HCU,1C2B,1C2O,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W Acetylcholinesterase ACES_MOUSE P21836 160401 C[N+](C)(C)CCCCCCCCCC[N+](C)(C)C InChI=1S/C16H38N2/c1-17(2,3)15-13-11-9-7-8-10-12-14-16-18(4,5)6/h7-16H2,1-6H3/q+2 MTCUAOILFDZKCO-UHFFFAOYSA-N 50060582 Decamethonium Iodide::decane-1,10-bis(trimethylammonium bromide)::1,10-Bis(trimethyl ammonium)decane dibromide::DECAMETHONIUM::CHEMBL1134::Syncurine::N,N,N'',N''-Tetramethyl-decane-1,10-diammonium; dibromide::N,N,N,N'',N'',N''-Hexamethyldecane-1,10-diammoniumdibromide::1,10-bis-(trimethyl ammonium) decane dibromide::DECAMETHONIUM BROMIDE Acetylcholinesterase Torpedo marmorata 1063 4.0000 25.00 C Curated from the literature by BindingDB 10.1002/1439-7633(20010601)2 10.7270/Q2J964W8 11828475 aid1799606 Bunyapaiboonsri, T; Ramström, O; Lohmann, S; Lehn, JM; Peng, L; Goeldner, M 6/1/2001 12/23/2011 UniversitÉ http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50060582 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4933&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50060582&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search DME 6EP4,5E2I,5E4J,1ACL,1MAA,2XUD 2968 103956277 CHEMBL1134 DB01245 C11733 1 MREMNLLVTSSLGVLLHLVVLCQADDDSELLVNTKSGKVMRTRIPVLSSHISAFLGIPFAEPPVGNMRFRRPEPKKPWSGVWNASTYPNNCQQYVDEQFPGFPGSEMWNPNREMSEDCLYLNIWVPSPRPKSATVMLWIYGGGFYSGSSTLDVYNGKYLAYTEEVVLVSLSYRVGAFGFLALHGSQEAPGNMGLLDQRMALQWVHDNIQFFGGDPKTVTLFGESAGRASVGMHILSPGSRDLFRRAILQSGSPNCPWASVSVAEGRRRAVELRRNLNCNLNSDEDLIQCLREKKPQELIDVEWNVLPFDSIFRFSFVPVIDGEFFPTSLESMLNAGNFKKTQILLGVNKDEGSFFLLYGAPGFSKDSESKISREDFMSGVKLSVPHANDLGLDAVTLQYTDWMDDNNGIKNRDGLDDIVGDHNVICPLMHFVNKYTKFGNGTYLYFFNHRASNLVWPEWMGVIHGYEIEFVFGLPLVKELNYTAEEEALSRRIMHYWATFAKTGNPNEPHSQESKWPLFTTKEQKFIDLNTEPIKVHQRLRVQMCVFWNQFLPKLLNATACDGELSSSGTSSSKGIIFYVLFSILYLIFY Acetylcholinesterase ACES_TORMA P07692 160401 C[N+](C)(C)CCCCCCCCCC[N+](C)(C)C InChI=1S/C16H38N2/c1-17(2,3)15-13-11-9-7-8-10-12-14-16-18(4,5)6/h7-16H2,1-6H3/q+2 MTCUAOILFDZKCO-UHFFFAOYSA-N 50060582 Decamethonium Iodide::decane-1,10-bis(trimethylammonium bromide)::1,10-Bis(trimethyl ammonium)decane dibromide::DECAMETHONIUM::CHEMBL1134::Syncurine::N,N,N'',N''-Tetramethyl-decane-1,10-diammonium; dibromide::N,N,N,N'',N'',N''-Hexamethyldecane-1,10-diammoniumdibromide::1,10-bis-(trimethyl ammonium) decane dibromide::DECAMETHONIUM BROMIDE Acetylcholinesterase Torpedo marmorata 1063 4.0000 25.00 C Curated from the literature by BindingDB 10.1002/1439-7633(20010601)2 10.7270/Q2J964W8 11828475 aid1799606 Bunyapaiboonsri, T; Ramström, O; Lohmann, S; Lehn, JM; Peng, L; Goeldner, M 6/1/2001 12/23/2011 UniversitÉ http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50060582 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=4933&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50060582&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search DME 6EP4,5E2I,5E4J,1ACL,1MAA,2XUD 2968 103956277 CHEMBL1134 DB01245 C11733 1 MREMNLLVTSSLGVLLHLVVLCQADDDSELLVNTKSGKVMRTRIPVLSSHISAFLGIPFAEPPVGNMRFRRPEPKKPWSGVWNASTYPNNCQQYVDEQFPGFPGSEMWNPNREMSEDCLYLNIWVPSPRPKSATVMLWIYGGGFYSGSSTLDVYNGKYLAYTEEVVLVSLSYRVGAFGFLALHGSQEAPGNMGLLDQRMALQWVHDNIQFFGGDPKTVTLFGESAGRASVGMHILSPGSRDLFRRAILQSGSPNCPWASVSVAEGRRRAVELRRNLNCNLNSDEDLIQCLREKKPQELIDVEWNVLPFDSIFRFSFVPVIDGEFFPTSLESMLNAGNFKKTQILLGVNKDEGSFFLLYGAPGFSKDSESKISREDFMSGVKLSVPHANDLGLDAVTLQYTDWMDDNNGIKNRDGLDDIVGDHNVICPLMHFVNKYTKFGNGTYLYFFNHRASNLVWPEWMGVIHGYEIEFVFGLPLVKELNYTAEEEALSRRIMHYWATFAKTGNPNEPHSQESKWPLFTTKEQKFIDLNTEPIKVHQRLRVQMCVFWNQFLPKLLNATACDGELSSSGTSSSKGIIFYVLFSILYLIFY Acetylcholinesterase ACES_TORMA P07692 50452560 c1ccc2c(c1)cc(o2)CNCCCCCCCNc3c4ccccc4nc5c3CCCC5 InChI=1S/C29H35N3O/c1(2-10-18-30-21-23-20-22-12-4-9-17-28(22)33-23)3-11-19-31-29-24-13-5-7-15-26(24)32-27-16-8-6-14-25(27)29/h4-5,7,9,12-13,15,17,20,30H,1-3,6,8,10-11,14,16,18-19,21H2,(H,31,32) LJASCSHXLYLOCF-UHFFFAOYSA-N 50138279 CHEMBL3752467 Acetylcholinesterase Tetronarce californica 0.032000 ChEMBL 10.1021/acs.jmedchem.5b01119 10.7270/Q2S75J5X 26632651 Zha, X; Lamba, D; Zhang, L; Lou, Y; Xu, C; Kang, D; Chen, L; Xu, Y; Zhang, L; De Simone, A; Samez, S; Pesaresi, A; Stojan, J; Lopez, MG; Egea, J; Andrisano, V; Bartolini, M 1/14/2016 5/31/2017 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50138279 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=236&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50138279&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HTB 4W63 91864546 104028344 CHEMBL3752467 1 MNLLVTSSLGVLLHLVVLCQADDHSELLVNTKSGKVMGTRVPVLSSHISAFLGIPFAEPPVGNMRFRRPEPKKPWSGVWNASTYPNNCQQYVDEQFPGFSGSEMWNPNREMSEDCLYLNIWVPSPRPKSTTVMVWIYGGGFYSGSSTLDVYNGKYLAYTEEVVLVSLSYRVGAFGFLALHGSQEAPGNVGLLDQRMALQWVHDNIQFFGGDPKTVTIFGESAGGASVGMHILSPGSRDLFRRAILQSGSPNCPWASVSVAEGRRRAVELGRNLNCNLNSDEELIHCLREKKPQELIDVEWNVLPFDSIFRFSFVPVIDGEFFPTSLESMLNSGNFKKTQILLGVNKDEGSFFLLYGAPGFSKDSESKISREDFMSGVKLSVPHANDLGLDAVTLQYTDWMDDNNGIKNRDGLDDIVGDHNVICPLMHFVNKYTKFGNGTYLYFFNHRASNLVWPEWMGVIHGYEIEFVFGLPLVKELNYTAEEEALSRRIMHYWATFAKTGNPNEPHSQESKWPLFTTKEQKFIDLNTEPMKVHQRLRVQMCVFWNQFLPKLLNATACDGELSSSGTSSSKGIIFYVLFSILYLIF 7AIX,7AIW,7AIV,7AIU,7AIT,7AIS,2W6C,6H14,6H13,6H12,6G1W,6G1V,6G1U,5NUU,5NAU,5NAP,5E4T,5DLP,3ZV7,3M3D,2VQ6,2J4F,2J3Q,2J3D,2CMF,2CKM,2BAG,1ZGC,1ZGB,1W76,1W75,1W6R,1W4L,1U65,1SOM,1ODC,1HBJ,1H23,1H22,1EVE,1E66,1E3Q,1DX6,7B8E,7B2W,6G4P,6G4O,6G4N,6G4M,6G17,6EZH,6EZG,5BWC,5BWB,2XI4,2WG2,2WG1,2WG0,2WFZ,2VT7,2VT6,2VJD,2VJC,2VJB,2VJA,2VA9,2V98,2V97,2V96,2C5G,2C5F,2C58,2C4H,2ACK,2ACE,1VXR,1VXO,1VOT,1QTI,1QIM,1QIK,1QIJ,1QII,1QIH,1QIG,1QIF,1QIE,1QID,1OCE,1GPN,1GPK,1FSS,1EA5,1CFJ,1AX9,1AMN,1UT6,1ACL,1ACJ,2CEK,5IH7,5EI5,4X3C,4W63,4TVK,3I6Z,3I6M,2DFP,1EEA,6EUE,7B38,6FQN,6FLD,6EWK,5EHX,5E4J,5E2I,1JJB,1GQS,1GQR Acetylcholinesterase ACES_TETCF P04058 50452561 c1ccc2c(c1)cc(o2)CNCCCCCCCNc3c4ccccc4nc5c3CCCC5 InChI=1S/C29H35N3O/c1(2-10-18-30-21-23-20-22-12-4-9-17-28(22)33-23)3-11-19-31-29-24-13-5-7-15-26(24)32-27-16-8-6-14-25(27)29/h4-5,7,9,12-13,15,17,20,30H,1-3,6,8,10-11,14,16,18-19,21H2,(H,31,32) LJASCSHXLYLOCF-UHFFFAOYSA-N 50138279 CHEMBL3752467 Acetylcholinesterase Tetronarce californica 0.031000 ChEMBL 10.1021/acs.jmedchem.5b01119 10.7270/Q2S75J5X 26632651 Zha, X; Lamba, D; Zhang, L; Lou, Y; Xu, C; Kang, D; Chen, L; Xu, Y; Zhang, L; De Simone, A; Samez, S; Pesaresi, A; Stojan, J; Lopez, MG; Egea, J; Andrisano, V; Bartolini, M 1/14/2016 5/31/2017 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50138279 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=236&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50138279&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HTB 4W63 91864546 104028344 CHEMBL3752467 1 MNLLVTSSLGVLLHLVVLCQADDHSELLVNTKSGKVMGTRVPVLSSHISAFLGIPFAEPPVGNMRFRRPEPKKPWSGVWNASTYPNNCQQYVDEQFPGFSGSEMWNPNREMSEDCLYLNIWVPSPRPKSTTVMVWIYGGGFYSGSSTLDVYNGKYLAYTEEVVLVSLSYRVGAFGFLALHGSQEAPGNVGLLDQRMALQWVHDNIQFFGGDPKTVTIFGESAGGASVGMHILSPGSRDLFRRAILQSGSPNCPWASVSVAEGRRRAVELGRNLNCNLNSDEELIHCLREKKPQELIDVEWNVLPFDSIFRFSFVPVIDGEFFPTSLESMLNSGNFKKTQILLGVNKDEGSFFLLYGAPGFSKDSESKISREDFMSGVKLSVPHANDLGLDAVTLQYTDWMDDNNGIKNRDGLDDIVGDHNVICPLMHFVNKYTKFGNGTYLYFFNHRASNLVWPEWMGVIHGYEIEFVFGLPLVKELNYTAEEEALSRRIMHYWATFAKTGNPNEPHSQESKWPLFTTKEQKFIDLNTEPMKVHQRLRVQMCVFWNQFLPKLLNATACDGELSSSGTSSSKGIIFYVLFSILYLIF 7AIX,7AIW,7AIV,7AIU,7AIT,7AIS,2W6C,6H14,6H13,6H12,6G1W,6G1V,6G1U,5NUU,5NAU,5NAP,5E4T,5DLP,3ZV7,3M3D,2VQ6,2J4F,2J3Q,2J3D,2CMF,2CKM,2BAG,1ZGC,1ZGB,1W76,1W75,1W6R,1W4L,1U65,1SOM,1ODC,1HBJ,1H23,1H22,1EVE,1E66,1E3Q,1DX6,7B8E,7B2W,6G4P,6G4O,6G4N,6G4M,6G17,6EZH,6EZG,5BWC,5BWB,2XI4,2WG2,2WG1,2WG0,2WFZ,2VT7,2VT6,2VJD,2VJC,2VJB,2VJA,2VA9,2V98,2V97,2V96,2C5G,2C5F,2C58,2C4H,2ACK,2ACE,1VXR,1VXO,1VOT,1QTI,1QIM,1QIK,1QIJ,1QII,1QIH,1QIG,1QIF,1QIE,1QID,1OCE,1GPN,1GPK,1FSS,1EA5,1CFJ,1AX9,1AMN,1UT6,1ACL,1ACJ,2CEK,5IH7,5EI5,4X3C,4W63,4TVK,3I6Z,3I6M,2DFP,1EEA,6EUE,7B38,6FQN,6FLD,6EWK,5EHX,5E4J,5E2I,1JJB,1GQS,1GQR Acetylcholinesterase ACES_TETCF P04058 50452562 c1ccc2c(c1)cc(o2)CNCCCCCCCNc3c4ccccc4nc5c3CCCC5 InChI=1S/C29H35N3O/c1(2-10-18-30-21-23-20-22-12-4-9-17-28(22)33-23)3-11-19-31-29-24-13-5-7-15-26(24)32-27-16-8-6-14-25(27)29/h4-5,7,9,12-13,15,17,20,30H,1-3,6,8,10-11,14,16,18-19,21H2,(H,31,32) LJASCSHXLYLOCF-UHFFFAOYSA-N 50138279 CHEMBL3752467 Acetylcholinesterase Tetronarce californica 2.2 ChEMBL 10.1021/acs.jmedchem.5b01119 10.7270/Q2S75J5X 26632651 Zha, X; Lamba, D; Zhang, L; Lou, Y; Xu, C; Kang, D; Chen, L; Xu, Y; Zhang, L; De Simone, A; Samez, S; Pesaresi, A; Stojan, J; Lopez, MG; Egea, J; Andrisano, V; Bartolini, M 1/14/2016 5/31/2017 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50138279 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=236&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50138279&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HTB 4W63 91864546 104028344 CHEMBL3752467 1 MNLLVTSSLGVLLHLVVLCQADDHSELLVNTKSGKVMGTRVPVLSSHISAFLGIPFAEPPVGNMRFRRPEPKKPWSGVWNASTYPNNCQQYVDEQFPGFSGSEMWNPNREMSEDCLYLNIWVPSPRPKSTTVMVWIYGGGFYSGSSTLDVYNGKYLAYTEEVVLVSLSYRVGAFGFLALHGSQEAPGNVGLLDQRMALQWVHDNIQFFGGDPKTVTIFGESAGGASVGMHILSPGSRDLFRRAILQSGSPNCPWASVSVAEGRRRAVELGRNLNCNLNSDEELIHCLREKKPQELIDVEWNVLPFDSIFRFSFVPVIDGEFFPTSLESMLNSGNFKKTQILLGVNKDEGSFFLLYGAPGFSKDSESKISREDFMSGVKLSVPHANDLGLDAVTLQYTDWMDDNNGIKNRDGLDDIVGDHNVICPLMHFVNKYTKFGNGTYLYFFNHRASNLVWPEWMGVIHGYEIEFVFGLPLVKELNYTAEEEALSRRIMHYWATFAKTGNPNEPHSQESKWPLFTTKEQKFIDLNTEPMKVHQRLRVQMCVFWNQFLPKLLNATACDGELSSSGTSSSKGIIFYVLFSILYLIF 7AIX,7AIW,7AIV,7AIU,7AIT,7AIS,2W6C,6H14,6H13,6H12,6G1W,6G1V,6G1U,5NUU,5NAU,5NAP,5E4T,5DLP,3ZV7,3M3D,2VQ6,2J4F,2J3Q,2J3D,2CMF,2CKM,2BAG,1ZGC,1ZGB,1W76,1W75,1W6R,1W4L,1U65,1SOM,1ODC,1HBJ,1H23,1H22,1EVE,1E66,1E3Q,1DX6,7B8E,7B2W,6G4P,6G4O,6G4N,6G4M,6G17,6EZH,6EZG,5BWC,5BWB,2XI4,2WG2,2WG1,2WG0,2WFZ,2VT7,2VT6,2VJD,2VJC,2VJB,2VJA,2VA9,2V98,2V97,2V96,2C5G,2C5F,2C58,2C4H,2ACK,2ACE,1VXR,1VXO,1VOT,1QTI,1QIM,1QIK,1QIJ,1QII,1QIH,1QIG,1QIF,1QIE,1QID,1OCE,1GPN,1GPK,1FSS,1EA5,1CFJ,1AX9,1AMN,1UT6,1ACL,1ACJ,2CEK,5IH7,5EI5,4X3C,4W63,4TVK,3I6Z,3I6M,2DFP,1EEA,6EUE,7B38,6FQN,6FLD,6EWK,5EHX,5E4J,5E2I,1JJB,1GQS,1GQR Acetylcholinesterase ACES_TETCF P04058 50452563 c1ccc2c(c1)cc(o2)CNCCCCCCCNc3c4ccccc4nc5c3CCCC5 InChI=1S/C29H35N3O/c1(2-10-18-30-21-23-20-22-12-4-9-17-28(22)33-23)3-11-19-31-29-24-13-5-7-15-26(24)32-27-16-8-6-14-25(27)29/h4-5,7,9,12-13,15,17,20,30H,1-3,6,8,10-11,14,16,18-19,21H2,(H,31,32) LJASCSHXLYLOCF-UHFFFAOYSA-N 50138279 CHEMBL3752467 Acetylcholinesterase Tetronarce californica 2.1 ChEMBL 10.1021/acs.jmedchem.5b01119 10.7270/Q2S75J5X 26632651 Zha, X; Lamba, D; Zhang, L; Lou, Y; Xu, C; Kang, D; Chen, L; Xu, Y; Zhang, L; De Simone, A; Samez, S; Pesaresi, A; Stojan, J; Lopez, MG; Egea, J; Andrisano, V; Bartolini, M 1/14/2016 5/31/2017 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50138279 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=236&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50138279&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search HTB 4W63 91864546 104028344 CHEMBL3752467 1 MNLLVTSSLGVLLHLVVLCQADDHSELLVNTKSGKVMGTRVPVLSSHISAFLGIPFAEPPVGNMRFRRPEPKKPWSGVWNASTYPNNCQQYVDEQFPGFSGSEMWNPNREMSEDCLYLNIWVPSPRPKSTTVMVWIYGGGFYSGSSTLDVYNGKYLAYTEEVVLVSLSYRVGAFGFLALHGSQEAPGNVGLLDQRMALQWVHDNIQFFGGDPKTVTIFGESAGGASVGMHILSPGSRDLFRRAILQSGSPNCPWASVSVAEGRRRAVELGRNLNCNLNSDEELIHCLREKKPQELIDVEWNVLPFDSIFRFSFVPVIDGEFFPTSLESMLNSGNFKKTQILLGVNKDEGSFFLLYGAPGFSKDSESKISREDFMSGVKLSVPHANDLGLDAVTLQYTDWMDDNNGIKNRDGLDDIVGDHNVICPLMHFVNKYTKFGNGTYLYFFNHRASNLVWPEWMGVIHGYEIEFVFGLPLVKELNYTAEEEALSRRIMHYWATFAKTGNPNEPHSQESKWPLFTTKEQKFIDLNTEPMKVHQRLRVQMCVFWNQFLPKLLNATACDGELSSSGTSSSKGIIFYVLFSILYLIF 7AIX,7AIW,7AIV,7AIU,7AIT,7AIS,2W6C,6H14,6H13,6H12,6G1W,6G1V,6G1U,5NUU,5NAU,5NAP,5E4T,5DLP,3ZV7,3M3D,2VQ6,2J4F,2J3Q,2J3D,2CMF,2CKM,2BAG,1ZGC,1ZGB,1W76,1W75,1W6R,1W4L,1U65,1SOM,1ODC,1HBJ,1H23,1H22,1EVE,1E66,1E3Q,1DX6,7B8E,7B2W,6G4P,6G4O,6G4N,6G4M,6G17,6EZH,6EZG,5BWC,5BWB,2XI4,2WG2,2WG1,2WG0,2WFZ,2VT7,2VT6,2VJD,2VJC,2VJB,2VJA,2VA9,2V98,2V97,2V96,2C5G,2C5F,2C58,2C4H,2ACK,2ACE,1VXR,1VXO,1VOT,1QTI,1QIM,1QIK,1QIJ,1QII,1QIH,1QIG,1QIF,1QIE,1QID,1OCE,1GPN,1GPK,1FSS,1EA5,1CFJ,1AX9,1AMN,1UT6,1ACL,1ACJ,2CEK,5IH7,5EI5,4X3C,4W63,4TVK,3I6Z,3I6M,2DFP,1EEA,6EUE,7B38,6FQN,6FLD,6EWK,5EHX,5E4J,5E2I,1JJB,1GQS,1GQR Acetylcholinesterase ACES_TETCF P04058 248233 C[C@@]12CC[C@@]3([C@@]([C@]1(CC4=C(O2)C=C(OC4=O)c5cc(c(c(c5)OC)OC)OC)O)(C(=O)C=CC3(C)C)C)O InChI=1S/C29H34O9/c1-25(2)9-8-22(30)27(4)28(25,32)11-10-26(3)29(27,33)15-17-19(38-26)14-18(37-24(17)31)16-12-20(34-5)23(36-7)21(13-16)35-6/h8-9,12-14,32-33H,10-11,15H2,1-7H3 PBXNNDFKPQPJBB-UHFFFAOYSA-N 50089616 CHEMBL24686::territrem B::4a,12a-Dihydroxy-4,4,6a,12b-tetramethyl-9-(3,4,5-trimethoxy-phenyl)-4a,6,6a,12,12a,12b-hexahydro-4H,5H-7,10-dioxa-benzo[a]anthracene-1,11-dione Acetylcholinesterase Homo sapiens 1.7 7.0000 25.00 C Curated from the literature by BindingDB 10.1021/bi401043w 10.7270/Q24X56GT 24040835 aid1800423 Beri, V; Wildman, SA; Shiomi, K; Al-Rashid, ZF; Cheung, J; Rosenberry, TL 10/22/2013 10/6/2014 Mayo Clinic http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50089616 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50089616&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search 1YK 4M0F 114734 103988316 CHEMBL24686 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50159840 C[C@@]12CC[C@@]3([C@@]([C@]1(CC4=C(O2)C=C(OC4=O)c5cc(c(c(c5)OC)OC)OC)O)(C(=O)C=CC3(C)C)C)O InChI=1S/C29H34O9/c1-25(2)9-8-22(30)27(4)28(25,32)11-10-26(3)29(27,33)15-17-19(38-26)14-18(37-24(17)31)16-12-20(34-5)23(36-7)21(13-16)35-6/h8-9,12-14,32-33H,10-11,15H2,1-7H3 PBXNNDFKPQPJBB-UHFFFAOYSA-N 50089616 CHEMBL24686::territrem B::4a,12a-Dihydroxy-4,4,6a,12b-tetramethyl-9-(3,4,5-trimethoxy-phenyl)-4a,6,6a,12,12a,12b-hexahydro-4H,5H-7,10-dioxa-benzo[a]anthracene-1,11-dione Acetylcholinesterase Homo sapiens 8 ChEMBL 10.1016/s0960-894x(00)00218-3 10.7270/Q23B5ZCD 10890154 Obata, R; Sunazuka, T; Otoguro, K; Tomoda, H; Harigaya, Y; Omura, S 11/15/2000 11/10/2009 Kitasato University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50089616 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50089616&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search 1YK 4M0F 114734 103988316 CHEMBL24686 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50433268 C[C@@]12CC[C@@]3([C@@]([C@]1(CC4=C(O2)C=C(OC4=O)c5cc(c(c(c5)OC)OC)OC)O)(C(=O)C=CC3(C)C)C)O InChI=1S/C29H34O9/c1-25(2)9-8-22(30)27(4)28(25,32)11-10-26(3)29(27,33)15-17-19(38-26)14-18(37-24(17)31)16-12-20(34-5)23(36-7)21(13-16)35-6/h8-9,12-14,32-33H,10-11,15H2,1-7H3 PBXNNDFKPQPJBB-UHFFFAOYSA-N 50089616 CHEMBL24686::territrem B::4a,12a-Dihydroxy-4,4,6a,12b-tetramethyl-9-(3,4,5-trimethoxy-phenyl)-4a,6,6a,12,12a,12b-hexahydro-4H,5H-7,10-dioxa-benzo[a]anthracene-1,11-dione Acetylcholinesterase Homo sapiens 7.6 ChEMBL 10.1016/j.bmcl.2015.06.047 10.7270/Q2668G1T 26159481 Al-Rashid, ZF; Hsung, RP 10/14/2015 12/17/2016 Alchemical Research http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50089616 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50089616&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search 1YK 4M0F 114734 103988316 CHEMBL24686 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 50636574 C[C@@]12CC[C@@]3([C@@]([C@]1(CC4=C(O2)C=C(OC4=O)c5cc(c(c(c5)OC)OC)OC)O)(C(=O)C=CC3(C)C)C)O InChI=1S/C29H34O9/c1-25(2)9-8-22(30)27(4)28(25,32)11-10-26(3)29(27,33)15-17-19(38-26)14-18(37-24(17)31)16-12-20(34-5)23(36-7)21(13-16)35-6/h8-9,12-14,32-33H,10-11,15H2,1-7H3 PBXNNDFKPQPJBB-UHFFFAOYSA-N 50089616 CHEMBL24686::territrem B::4a,12a-Dihydroxy-4,4,6a,12b-tetramethyl-9-(3,4,5-trimethoxy-phenyl)-4a,6,6a,12,12a,12b-hexahydro-4H,5H-7,10-dioxa-benzo[a]anthracene-1,11-dione Acetylcholinesterase Homo sapiens 6 ChEMBL 10.1016/j.bmcl.2010.12.041 10.7270/Q27W6CH9 21216144 Al-Rashid, ZF; Hsung, RP 4/25/2011 12/3/2011 Alchemical Research http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50089616 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50089616&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search 1YK 4M0F 114734 103988316 CHEMBL24686 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51202290 C[C@@]12CC[C@@]3([C@@]([C@]1(CC4=C(O2)C=C(OC4=O)c5cc(c(c(c5)OC)OC)OC)O)(C(=O)C=CC3(C)C)C)O InChI=1S/C29H34O9/c1-25(2)9-8-22(30)27(4)28(25,32)11-10-26(3)29(27,33)15-17-19(38-26)14-18(37-24(17)31)16-12-20(34-5)23(36-7)21(13-16)35-6/h8-9,12-14,32-33H,10-11,15H2,1-7H3 PBXNNDFKPQPJBB-UHFFFAOYSA-N 50089616 CHEMBL24686::territrem B::4a,12a-Dihydroxy-4,4,6a,12b-tetramethyl-9-(3,4,5-trimethoxy-phenyl)-4a,6,6a,12,12a,12b-hexahydro-4H,5H-7,10-dioxa-benzo[a]anthracene-1,11-dione Acetylcholinesterase Homo sapiens 1.7 ChEMBL 10.1021/ml400304w 10.7270/Q2VT1W2P 24900610 Cheung, J; Gary, EN; Shiomi, K; Rosenberry, TL 11/14/2013 9/1/2020 New York Structural Biology Center http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50089616 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50089616&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search 1YK 4M0F 114734 103988316 CHEMBL24686 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 248232 Cc1cccc2c1ccc3c2C(=O)C(=O)C4=C3OC[C@@H]4C InChI=1S/C18H14O3/c1-9-4-3-5-12-11(9)6-7-13-15(12)17(20)16(19)14-10(2)8-21-18(13)14/h3-7,10H,8H2,1-2H3 HARGZZNYNSYSGJ-UHFFFAOYSA-N 50423877 Dihydrotanshinone I::DIHYDROTANSHINONE::acs.jmedchem.1c00409_ST.562 Acetylcholinesterase Homo sapiens 750 7.0000 25.00 C Curated from the literature by BindingDB 10.1021/bi401043w 10.7270/Q24X56GT 24040835 aid1800423 Beri, V; Wildman, SA; Shiomi, K; Al-Rashid, ZF; Cheung, J; Rosenberry, TL 10/22/2013 10/6/2014 Mayo Clinic http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50423877 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50423877&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search 1YL 4M0E 11425923 164152752 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51051480 Cc1cccc2c1ccc3c2C(=O)C(=O)C4=C3OC[C@@H]4C InChI=1S/C18H14O3/c1-9-4-3-5-12-11(9)6-7-13-15(12)17(20)16(19)14-10(2)8-21-18(13)14/h3-7,10H,8H2,1-2H3 HARGZZNYNSYSGJ-UHFFFAOYSA-N 50423877 Dihydrotanshinone I::DIHYDROTANSHINONE::acs.jmedchem.1c00409_ST.562 Acetylcholinesterase Homo sapiens >100000 ChEMBL 10.1021/np300628a 10.7270/Q2VX0HWJ 23286284 Hatfield, MJ; Tsurkan, LG; Hyatt, JL; Edwards, CC; Lemoff, A; Jeffries, C; Yan, B; Potter, PM 1/25/2013 9/24/2013 St. Jude Children'S Research Hospital http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50423877 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50423877&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search 1YL 4M0E 11425923 164152752 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51051486 Cc1cccc2c1ccc3c2C(=O)C(=O)C4=C3OC[C@@H]4C InChI=1S/C18H14O3/c1-9-4-3-5-12-11(9)6-7-13-15(12)17(20)16(19)14-10(2)8-21-18(13)14/h3-7,10H,8H2,1-2H3 HARGZZNYNSYSGJ-UHFFFAOYSA-N 50423877 Dihydrotanshinone I::DIHYDROTANSHINONE::acs.jmedchem.1c00409_ST.562 Acetylcholinesterase Homo sapiens 1950 ChEMBL 10.1021/np300628a 10.7270/Q2VX0HWJ 23286284 Hatfield, MJ; Tsurkan, LG; Hyatt, JL; Edwards, CC; Lemoff, A; Jeffries, C; Yan, B; Potter, PM 1/25/2013 9/24/2013 St. Jude Children'S Research Hospital http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50423877 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50423877&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search 1YL 4M0E 11425923 164152752 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51202287 Cc1cccc2c1ccc3c2C(=O)C(=O)C4=C3OC[C@@H]4C InChI=1S/C18H14O3/c1-9-4-3-5-12-11(9)6-7-13-15(12)17(20)16(19)14-10(2)8-21-18(13)14/h3-7,10H,8H2,1-2H3 HARGZZNYNSYSGJ-UHFFFAOYSA-N 50423877 Dihydrotanshinone I::DIHYDROTANSHINONE::acs.jmedchem.1c00409_ST.562 Acetylcholinesterase Homo sapiens 1000 ChEMBL 10.1021/ml400304w 10.7270/Q2VT1W2P 24900610 Cheung, J; Gary, EN; Shiomi, K; Rosenberry, TL 11/14/2013 9/1/2020 New York Structural Biology Center http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50423877 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50423877&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search 1YL 4M0E 11425923 164152752 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 51202291 Cc1cccc2c1ccc3c2C(=O)C(=O)C4=C3OC[C@@H]4C InChI=1S/C18H14O3/c1-9-4-3-5-12-11(9)6-7-13-15(12)17(20)16(19)14-10(2)8-21-18(13)14/h3-7,10H,8H2,1-2H3 HARGZZNYNSYSGJ-UHFFFAOYSA-N 50423877 Dihydrotanshinone I::DIHYDROTANSHINONE::acs.jmedchem.1c00409_ST.562 Acetylcholinesterase Homo sapiens 600 ChEMBL 10.1021/ml400304w 10.7270/Q2VT1W2P 24900610 Cheung, J; Gary, EN; Shiomi, K; Rosenberry, TL 11/14/2013 9/1/2020 New York Structural Biology Center http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50423877 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50423877&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search 1YL 4M0E 11425923 164152752 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 15299 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 2.9 8.0000 25.00 C Curated from the literature by BindingDB 10.1021/jm049510k 10.7270/Q27P8WMJ 15771436 aid1796269 Campiani, G; Fattorusso, C; Butini, S; Gaeta, A; Agnusdei, M; Gemma, S; Persico, M; Catalanotti, B; Savini, L; Nacci, V; Novellino, E; Holloway, HW; Greig, NH; Belinskaya, T; Fedorko, JM; Saxena, A 3/24/2005 5/2/2006 Universita Di Siena http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 15518 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Bos taurus 19 8.0000 30.00 C Curated from the literature by BindingDB 10.1016/j.bmc.2005.09.029 10.7270/Q2G73BW9 16230018 aid1796282 Alonso, D; Dorronsoro, I; Rubio, L; Munoz, P; Garcia-Palomero, E; Del Monte, M; Bidon-Chanal, A; Orozco, M; Luque, FJ; Castro, A; Medina, M; Martinez, A 12/15/2005 5/8/2006 Neuropharma http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1045&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWCPLHTPSLTPPLLLLLFLIGGGAEAEGPEDPELLVMVRGGRLRGLRLMAPRGPVSAFLGIPFAEPPVGPRRFLPPEPKRPWPGVLNATAFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPSSPTPVLVWIYGGGFYSGASSLDVYDGRFLTQAEGTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGVGEARRRATLLARLVGCPPGGAGGNDTELVACLRARPAQDLVDHEWRVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAQFLAGVRVGVPQASDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLSWPLWMGVPHGYEIEFIFGLPLEPSLNYTIEERTFAQRLMRYWANFARTGDPNDPRDPKAPQWPPYTAGAQQYVSLNLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 6F25,1B41,6O69,1KU6 Acetylcholinesterase ACES_BOVIN P23795 O97579 Q08D79 17743 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 22 Curated from the literature by BindingDB 10.1021/jm050578p 10.7270/Q2S75DJ6 16570913 aid1796482 Luo, W; Yu, QS; Kulkarni, SS; Parrish, DA; Holloway, HW; Tweedie, D; Shafferman, A; Lahiri, DK; Brossi, A; Greig, NH 4/6/2006 8/13/2006 National Institutes of Health http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 18638 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 20.5 23.1 8.0000 37.00 C Curated from the literature by BindingDB 10.1021/jm0340602 10.7270/Q29Z9332 12773032 aid1796570 Piazzi, L; Rampa, A; Bisi, A; Gobbi, S; Belluti, F; Cavalli, A; Bartolini, M; Andrisano, V; Valenti, P; Recanatini, M 6/5/2003 9/12/2006 University of Bologna http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 18676 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 22 8.0000 37.00 C Curated from the literature by BindingDB 10.1021/jm010491d 10.7270/Q22J6933 12166941 aid1796572 Yu, QS; Zhu, X; Holloway, HW; Whittaker, NF; Brossi, A; Greig, NH 8/15/2002 9/12/2006 National Institutes of Health http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 200777 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 26 Curated from the literature by BindingDB 10.1111/j.1747-0285.2012.01435.x 10.7270/Q28P5Z3T 22726458 aid1799797 Raza, R; Saeed, A; Arif, M; Mahmood, S; Muddassar, M; Raza, A; Iqbal, J 10/28/2012 10/29/2012 Comsats Institute of Information Technology http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 293169 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 23 8.0000 25.00 C Curated from the literature by BindingDB 10.1016/j.bioorg.2015.05.005 10.7270/Q2WS8S05 26042530 aid1801052 Kanhed, AM; Sinha, A; Machhi, J; Tripathi, A; Parikh, ZS; Pillai, PP; Giridhar, R; Yadav, MR 8/28/2015 9/8/2015 The M. S. University of Baroda http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 344013 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 1e+1 8.0000 25.00 C Curated from the literature by BindingDB 10.1016/j.bioorg.2016.05.002 10.7270/Q2P849PS 27231830 aid1801892 Chigurupati, S; Selvaraj, M; Mani, V; Selvarajan, KK; Mohammad, JI; Kaveti, B; Bera, H; Palanimuthu, VR; Teh, LK; Salleh, MZ 8/28/2016 9/8/2016 Aimst University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 354300 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 4e+1 8.0000 25.00 C Curated from the literature by BindingDB 10.1111/cbdd.12800 10.7270/Q26D5RSX 27282589 aid1802080 Osman, W; Mohamed, T; Sit, VM; Vasefi, MS; Beazely, MA; Rao, PP 11/28/2016 11/4/2016 University of Waterloo http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 393850 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Homo sapiens 6.16 8.0000 25.00 C Curated from the literature by BindingDB 10.7270/Q2JM28HK aid1802741 Ozadali-Sari, K; Küçükkilinç, TT; Ayazgok, B; Balkan, A; Unsal-Tan, O 5/2/2017 5/9/2017 Hacettepe University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=3619&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL 4BDT,2X8B,9OMT,9OMS,8DT7,8DT5,8DT4,8DT2,7RB7,7RB6,7RB5,6U3P,6U37,6U34,6O66,6O5V,6O5S,6O5R,6O52,6O50,6O4X,6O4W,9F6R,8AEN,4PQE,7D9Q,7D9P,7D9O,6ZWE,6WVQ,6WVP,6WVO,6WVC,6WV1,6WUZ,6WUY,6WUV,6NTO,6NTN,6NTM,6NTL,6NTK,6NTH,6NTG,6NEA,6CQZ,6CQY,6CQX,6CQW,6CQV,6CQU,6CQT,5HFA,5HF9,5HF8,5HF6,5HF5,5FPQ,4M0F,4M0E,4EY8,4EY7,4EY6,4EY5,4EY4,7XN1,7E3H,7E3D,3LII,6F25,1B41,1MAA Acetylcholinesterase ACES_HUMAN P22303 A4D2E2 B7ZKZ0 D6W5X7 Q16169 Q29S23 Q2M324 Q504V3 Q53F46 Q86TM9 Q86YX9 Q9BXP7 404157 COc1cc2c(cc1OC)C(=O)[C@@H](C2)CC3CCN(CC3)Cc4ccccc4 InChI=1S/C24H29NO3/c1-27-22-14-19-13-20(24(26)21(19)15-23(22)28-2)12-17-8-10-25(11-9-17)16-18-6-4-3-5-7-18/h3-7,14-15,17,20H,8-13,16H2,1-2H3 ADEBPBSSDYVVLD-UHFFFAOYSA-N 8960 2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-2,3-dihydro-1H-inden-1-one::DONEPEZIL HYDROCHLORIDE::E2020::Aricept::CHEMBL2337271::CHEMBL1678::(+/-)-2-[(1-benzylpiperidin-4-yl)methyl]-5,6-dimethoxy-indan-1-one::CHEMBL502::Donepezil::US8999994, Donepezil::Aricept odt::Donepzil::US9346818, DPH::US9586925, Donepezil::US9663465, Donepezil Acetylcholinesterase Mus musculus 94 US Patent 10.7270/Q2WD3ZFC aid1802876 US9346818 Bai, H; Zhao, X; Zhong, J; Gong, Y; Zhu, Q; Liu, X; Zheng, X; Liu, L 5/24/2016 6/5/2017 Zhejiang Hisun Pharmaceutical http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=8960 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1064&target=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=8960&enzyme=Acetylcholinesterase&column=ki&startPg=0&Increment=50&submit=Search E20 1EVE,4EY7,6O4W,7E3H 3152 46509735 CHEMBL502CHEMBL1678CHEMBL2337271 DB00843 1 MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPG