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 51609095 COc1ccc2c(ccn2S(=O)(=O)c2ccc(C(=O)NO)cc2)c1 InChI=1S/C16H14N2O5S/c1-23-13-4-7-15-12(10-13)8-9-18(15)24(21,22)14-5-2-11(3-6-14)16(19)17-20/h2-10,20H,1H3,(H,17,19) OPPDFJJHYRWMHD-UHFFFAOYSA-N 50648724 CHEMBL5611957 Histone deacetylase 1 Human 3394 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648724 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1967&target=Histone+deacetylase+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=50648724&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 172378291 519664126 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51609096 O=C(NO)c1ccc(S(=O)(=O)n2ccc3cc(OCc4ccccc4)ccc32)cc1 InChI=1S/C22H18N2O5S/c25-22(23-26)17-6-9-20(10-7-17)30(27,28)24-13-12-18-14-19(8-11-21(18)24)29-15-16-4-2-1-3-5-16/h1-14,26H,15H2,(H,23,25) MMVCCAKXGHEKQP-UHFFFAOYSA-N 50648725 CHEMBL5612800 Histone deacetylase 1 Human 3993 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648725 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1967&target=Histone+deacetylase+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=50648725&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 172378311 519664127 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51609097 O=C(NO)c1ccc(S(=O)(=O)n2ccc3cc(OCCCN4CCCCC4)ccc32)cc1 InChI=1S/C23H27N3O5S/c27-23(24-28)18-5-8-21(9-6-18)32(29,30)26-15-11-19-17-20(7-10-22(19)26)31-16-4-14-25-12-2-1-3-13-25/h5-11,15,17,28H,1-4,12-14,16H2,(H,24,27) WKXOTOAMDAIXAM-UHFFFAOYSA-N 50648726 CHEMBL5612392 Histone deacetylase 1 Human 735 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648726 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1967&target=Histone+deacetylase+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=50648726&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 172378322 519664128 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51609098 C#CCN1CCN(CCCOc2ccc3c(ccn3S(=O)(=O)c3ccc(C(=O)NO)cc3)c2)CC1 InChI=1S/C25H28N4O5S/c1-2-11-27-14-16-28(17-15-27)12-3-18-34-22-6-9-24-21(19-22)10-13-29(24)35(32,33)23-7-4-20(5-8-23)25(30)26-31/h1,4-10,13,19,31H,3,11-12,14-18H2,(H,26,30) GLTMLUZWBIWFLU-UHFFFAOYSA-N 50648727 CHEMBL5612289 Histone deacetylase 1 Human 4000 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648727 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1967&target=Histone+deacetylase+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=50648727&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 172378300 519664129 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51609099 COc1ccc2c(ccn2S(=O)(=O)c2ccc(C(=O)NN)cc2)c1 InChI=1S/C16H15N3O4S/c1-23-13-4-7-15-12(10-13)8-9-19(15)24(21,22)14-5-2-11(3-6-14)16(20)18-17/h2-10H,17H2,1H3,(H,18,20) JUDFDZCQNLICNK-UHFFFAOYSA-N 50648728 CHEMBL5613926 Histone deacetylase 1 Human >10000 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648728 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1967&target=Histone+deacetylase+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=50648728&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 172378317 519664130 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51609100 NNC(=O)c1ccc(S(=O)(=O)n2ccc3cc(OCc4ccccc4)ccc32)cc1 InChI=1S/C22H19N3O4S/c23-24-22(26)17-6-9-20(10-7-17)30(27,28)25-13-12-18-14-19(8-11-21(18)25)29-15-16-4-2-1-3-5-16/h1-14H,15,23H2,(H,24,26) NKFZJQOGHFCNII-UHFFFAOYSA-N 50648729 CHEMBL5614106 Histone deacetylase 1 Human >10000 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648729 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1967&target=Histone+deacetylase+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=50648729&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 172378342 519664131 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51609101 NNC(=O)c1ccc(S(=O)(=O)n2ccc3cc(OCCCN4CCCCC4)ccc32)cc1 InChI=1S/C23H28N4O4S/c24-25-23(28)18-5-8-21(9-6-18)32(29,30)27-15-11-19-17-20(7-10-22(19)27)31-16-4-14-26-12-2-1-3-13-26/h5-11,15,17H,1-4,12-14,16,24H2,(H,25,28) ZJDCLYFDPYCDFQ-UHFFFAOYSA-N 50648730 CHEMBL5613037 Histone deacetylase 1 Human >10000 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648730 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1967&target=Histone+deacetylase+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=50648730&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 172378327 519664132 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51609102 C#CCN1CCN(CCCOc2ccc3c(ccn3S(=O)(=O)c3ccc(C(=O)NN)cc3)c2)CC1 InChI=1S/C25H29N5O4S/c1-2-11-28-14-16-29(17-15-28)12-3-18-34-22-6-9-24-21(19-22)10-13-30(24)35(32,33)23-7-4-20(5-8-23)25(31)27-26/h1,4-10,13,19H,3,11-12,14-18,26H2,(H,27,31) XYYROHFZJGYLHN-UHFFFAOYSA-N 50648731 CHEMBL5613800 Histone deacetylase 1 Human >10000 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648731 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1967&target=Histone+deacetylase+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=50648731&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 172378326 519664133 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51609103 c1ccc(cc1)NC(=O)CCCCCCC(=O)NO InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 Zolinza::suberoylanilide hydroxamic acid::CHEMBL98::cid_5311::N-hydroxy-N'-phenyloctanediamide::Vorinostat::SAHA::US9115116, SAHA::US9695181, Vorinostat::US9428447, SAHA::US9353061, SAHA::US10188756, Compound SAHA::US10011611, SAHA::US11207431, SAHA::US11505523, Compound SAHA::US20240327418, Example SAHA Histone deacetylase 1 Homo sapiens 89 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1967&target=Histone+deacetylase+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=19149&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search SHH 1C3S,1T69,1ZZ1,3C0Z,4BZ6,4LXZ,4QA0,4QA2,4R7L,5EEI,7JVU,7SGG,7ZZS,8BPC,9GKV,9GKX,9GN6,9O8X,9OAF,9OAM,9OBJ 5311 46519184 CHEMBL98 DB02546 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 9R4I,8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51609104 COc1ccc2c(ccn2S(=O)(=O)c2ccc(C(=O)NO)cc2)c1 InChI=1S/C16H14N2O5S/c1-23-13-4-7-15-12(10-13)8-9-18(15)24(21,22)14-5-2-11(3-6-14)16(19)17-20/h2-10,20H,1H3,(H,17,19) OPPDFJJHYRWMHD-UHFFFAOYSA-N 50648724 CHEMBL5611957 Histone deacetylase 6 Human 168 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648724 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2556&target=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50648724&enzyme=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search 172378291 519664126 1 MTSTGQDSTTTRQRRSRQNPQSPPQDSSVTSKRNIKKGAVPRSIPNLAEVKKKGKMKKLGQAMEEDLIVGLQGMDLNLEAEALAGTGLVLDEQLNEFHCLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCRSAQASVSCALEALEPFWEVLVRSTETVERDNMEEDNVEESEEEGPWEPPVLPILTWPVLQSRTGLVYDQNMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQTISGHALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLSGALASITETIQVHRRYWRSLRVMKVEDREGPSSSKLVTKKAPQPAKPRLAERMTTREKKVLEAGMGKVTSASFGEESTPGQTNSETAVVALTQDQPSEAATGGATLAQTISEAAIGGAMLGQTTSEEAVGGATPDQTTSEETVGGAILDQTTSEDAVGGATLGQTTSEEAVGGATLAQTTSEAAMEGATLDQTTSEEAPGGTELIQTPLASSTDHQTPPTSPVQGTTPQISPSTLIGSLRTLELGSESQGASESQAPGEENLLGEAAGGQDMADSMLMQGSRGLTDQAIFYAVTPLPWCPHLVAVCPIPAAGLDVTQPCGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHGNSGHPLVLSYIDLSAWCYYCQAYVHHQALLDVKNIAHQNKFGEDMPHPH 5EDU,7ZYU,3PHD,3GV4 Protein deacetylase HDAC6 HDAC6_HUMAN Q9UBN7 O94975 Q6NT75 Q7L3E5 Q96CY0 51609105 O=C(NO)c1ccc(S(=O)(=O)n2ccc3cc(OCc4ccccc4)ccc32)cc1 InChI=1S/C22H18N2O5S/c25-22(23-26)17-6-9-20(10-7-17)30(27,28)24-13-12-18-14-19(8-11-21(18)24)29-15-16-4-2-1-3-5-16/h1-14,26H,15H2,(H,23,25) MMVCCAKXGHEKQP-UHFFFAOYSA-N 50648725 CHEMBL5612800 Histone deacetylase 6 Human 295 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648725 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2556&target=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50648725&enzyme=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search 172378311 519664127 1 MTSTGQDSTTTRQRRSRQNPQSPPQDSSVTSKRNIKKGAVPRSIPNLAEVKKKGKMKKLGQAMEEDLIVGLQGMDLNLEAEALAGTGLVLDEQLNEFHCLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCRSAQASVSCALEALEPFWEVLVRSTETVERDNMEEDNVEESEEEGPWEPPVLPILTWPVLQSRTGLVYDQNMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQTISGHALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLSGALASITETIQVHRRYWRSLRVMKVEDREGPSSSKLVTKKAPQPAKPRLAERMTTREKKVLEAGMGKVTSASFGEESTPGQTNSETAVVALTQDQPSEAATGGATLAQTISEAAIGGAMLGQTTSEEAVGGATPDQTTSEETVGGAILDQTTSEDAVGGATLGQTTSEEAVGGATLAQTTSEAAMEGATLDQTTSEEAPGGTELIQTPLASSTDHQTPPTSPVQGTTPQISPSTLIGSLRTLELGSESQGASESQAPGEENLLGEAAGGQDMADSMLMQGSRGLTDQAIFYAVTPLPWCPHLVAVCPIPAAGLDVTQPCGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHGNSGHPLVLSYIDLSAWCYYCQAYVHHQALLDVKNIAHQNKFGEDMPHPH 5EDU,7ZYU,3PHD,3GV4 Protein deacetylase HDAC6 HDAC6_HUMAN Q9UBN7 O94975 Q6NT75 Q7L3E5 Q96CY0 51609106 O=C(NO)c1ccc(S(=O)(=O)n2ccc3cc(OCCCN4CCCCC4)ccc32)cc1 InChI=1S/C23H27N3O5S/c27-23(24-28)18-5-8-21(9-6-18)32(29,30)26-15-11-19-17-20(7-10-22(19)26)31-16-4-14-25-12-2-1-3-13-25/h5-11,15,17,28H,1-4,12-14,16H2,(H,24,27) WKXOTOAMDAIXAM-UHFFFAOYSA-N 50648726 CHEMBL5612392 Histone deacetylase 6 Human 12 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648726 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2556&target=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50648726&enzyme=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search 172378322 519664128 1 MTSTGQDSTTTRQRRSRQNPQSPPQDSSVTSKRNIKKGAVPRSIPNLAEVKKKGKMKKLGQAMEEDLIVGLQGMDLNLEAEALAGTGLVLDEQLNEFHCLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCRSAQASVSCALEALEPFWEVLVRSTETVERDNMEEDNVEESEEEGPWEPPVLPILTWPVLQSRTGLVYDQNMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQTISGHALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLSGALASITETIQVHRRYWRSLRVMKVEDREGPSSSKLVTKKAPQPAKPRLAERMTTREKKVLEAGMGKVTSASFGEESTPGQTNSETAVVALTQDQPSEAATGGATLAQTISEAAIGGAMLGQTTSEEAVGGATPDQTTSEETVGGAILDQTTSEDAVGGATLGQTTSEEAVGGATLAQTTSEAAMEGATLDQTTSEEAPGGTELIQTPLASSTDHQTPPTSPVQGTTPQISPSTLIGSLRTLELGSESQGASESQAPGEENLLGEAAGGQDMADSMLMQGSRGLTDQAIFYAVTPLPWCPHLVAVCPIPAAGLDVTQPCGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHGNSGHPLVLSYIDLSAWCYYCQAYVHHQALLDVKNIAHQNKFGEDMPHPH 5EDU,7ZYU,3PHD,3GV4 Protein deacetylase HDAC6 HDAC6_HUMAN Q9UBN7 O94975 Q6NT75 Q7L3E5 Q96CY0 51609107 C#CCN1CCN(CCCOc2ccc3c(ccn3S(=O)(=O)c3ccc(C(=O)NO)cc3)c2)CC1 InChI=1S/C25H28N4O5S/c1-2-11-27-14-16-28(17-15-27)12-3-18-34-22-6-9-24-21(19-22)10-13-29(24)35(32,33)23-7-4-20(5-8-23)25(30)26-31/h1,4-10,13,19,31H,3,11-12,14-18H2,(H,26,30) GLTMLUZWBIWFLU-UHFFFAOYSA-N 50648727 CHEMBL5612289 Histone deacetylase 6 Human 35 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648727 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2556&target=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50648727&enzyme=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search 172378300 519664129 1 MTSTGQDSTTTRQRRSRQNPQSPPQDSSVTSKRNIKKGAVPRSIPNLAEVKKKGKMKKLGQAMEEDLIVGLQGMDLNLEAEALAGTGLVLDEQLNEFHCLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCRSAQASVSCALEALEPFWEVLVRSTETVERDNMEEDNVEESEEEGPWEPPVLPILTWPVLQSRTGLVYDQNMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQTISGHALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLSGALASITETIQVHRRYWRSLRVMKVEDREGPSSSKLVTKKAPQPAKPRLAERMTTREKKVLEAGMGKVTSASFGEESTPGQTNSETAVVALTQDQPSEAATGGATLAQTISEAAIGGAMLGQTTSEEAVGGATPDQTTSEETVGGAILDQTTSEDAVGGATLGQTTSEEAVGGATLAQTTSEAAMEGATLDQTTSEEAPGGTELIQTPLASSTDHQTPPTSPVQGTTPQISPSTLIGSLRTLELGSESQGASESQAPGEENLLGEAAGGQDMADSMLMQGSRGLTDQAIFYAVTPLPWCPHLVAVCPIPAAGLDVTQPCGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHGNSGHPLVLSYIDLSAWCYYCQAYVHHQALLDVKNIAHQNKFGEDMPHPH 5EDU,7ZYU,3PHD,3GV4 Protein deacetylase HDAC6 HDAC6_HUMAN Q9UBN7 O94975 Q6NT75 Q7L3E5 Q96CY0 51609108 COc1ccc2c(ccn2S(=O)(=O)c2ccc(C(=O)NN)cc2)c1 InChI=1S/C16H15N3O4S/c1-23-13-4-7-15-12(10-13)8-9-19(15)24(21,22)14-5-2-11(3-6-14)16(20)18-17/h2-10H,17H2,1H3,(H,18,20) JUDFDZCQNLICNK-UHFFFAOYSA-N 50648728 CHEMBL5613926 Histone deacetylase 6 Human >10000 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648728 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2556&target=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50648728&enzyme=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search 172378317 519664130 1 MTSTGQDSTTTRQRRSRQNPQSPPQDSSVTSKRNIKKGAVPRSIPNLAEVKKKGKMKKLGQAMEEDLIVGLQGMDLNLEAEALAGTGLVLDEQLNEFHCLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCRSAQASVSCALEALEPFWEVLVRSTETVERDNMEEDNVEESEEEGPWEPPVLPILTWPVLQSRTGLVYDQNMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQTISGHALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLSGALASITETIQVHRRYWRSLRVMKVEDREGPSSSKLVTKKAPQPAKPRLAERMTTREKKVLEAGMGKVTSASFGEESTPGQTNSETAVVALTQDQPSEAATGGATLAQTISEAAIGGAMLGQTTSEEAVGGATPDQTTSEETVGGAILDQTTSEDAVGGATLGQTTSEEAVGGATLAQTTSEAAMEGATLDQTTSEEAPGGTELIQTPLASSTDHQTPPTSPVQGTTPQISPSTLIGSLRTLELGSESQGASESQAPGEENLLGEAAGGQDMADSMLMQGSRGLTDQAIFYAVTPLPWCPHLVAVCPIPAAGLDVTQPCGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHGNSGHPLVLSYIDLSAWCYYCQAYVHHQALLDVKNIAHQNKFGEDMPHPH 5EDU,7ZYU,3PHD,3GV4 Protein deacetylase HDAC6 HDAC6_HUMAN Q9UBN7 O94975 Q6NT75 Q7L3E5 Q96CY0 51609109 NNC(=O)c1ccc(S(=O)(=O)n2ccc3cc(OCc4ccccc4)ccc32)cc1 InChI=1S/C22H19N3O4S/c23-24-22(26)17-6-9-20(10-7-17)30(27,28)25-13-12-18-14-19(8-11-21(18)25)29-15-16-4-2-1-3-5-16/h1-14H,15,23H2,(H,24,26) NKFZJQOGHFCNII-UHFFFAOYSA-N 50648729 CHEMBL5614106 Histone deacetylase 6 Human >10000 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648729 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2556&target=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50648729&enzyme=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search 172378342 519664131 1 MTSTGQDSTTTRQRRSRQNPQSPPQDSSVTSKRNIKKGAVPRSIPNLAEVKKKGKMKKLGQAMEEDLIVGLQGMDLNLEAEALAGTGLVLDEQLNEFHCLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCRSAQASVSCALEALEPFWEVLVRSTETVERDNMEEDNVEESEEEGPWEPPVLPILTWPVLQSRTGLVYDQNMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQTISGHALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLSGALASITETIQVHRRYWRSLRVMKVEDREGPSSSKLVTKKAPQPAKPRLAERMTTREKKVLEAGMGKVTSASFGEESTPGQTNSETAVVALTQDQPSEAATGGATLAQTISEAAIGGAMLGQTTSEEAVGGATPDQTTSEETVGGAILDQTTSEDAVGGATLGQTTSEEAVGGATLAQTTSEAAMEGATLDQTTSEEAPGGTELIQTPLASSTDHQTPPTSPVQGTTPQISPSTLIGSLRTLELGSESQGASESQAPGEENLLGEAAGGQDMADSMLMQGSRGLTDQAIFYAVTPLPWCPHLVAVCPIPAAGLDVTQPCGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHGNSGHPLVLSYIDLSAWCYYCQAYVHHQALLDVKNIAHQNKFGEDMPHPH 5EDU,7ZYU,3PHD,3GV4 Protein deacetylase HDAC6 HDAC6_HUMAN Q9UBN7 O94975 Q6NT75 Q7L3E5 Q96CY0 51609110 NNC(=O)c1ccc(S(=O)(=O)n2ccc3cc(OCCCN4CCCCC4)ccc32)cc1 InChI=1S/C23H28N4O4S/c24-25-23(28)18-5-8-21(9-6-18)32(29,30)27-15-11-19-17-20(7-10-22(19)27)31-16-4-14-26-12-2-1-3-13-26/h5-11,15,17H,1-4,12-14,16,24H2,(H,25,28) ZJDCLYFDPYCDFQ-UHFFFAOYSA-N 50648730 CHEMBL5613037 Histone deacetylase 6 Human >10000 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648730 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2556&target=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50648730&enzyme=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search 172378327 519664132 1 MTSTGQDSTTTRQRRSRQNPQSPPQDSSVTSKRNIKKGAVPRSIPNLAEVKKKGKMKKLGQAMEEDLIVGLQGMDLNLEAEALAGTGLVLDEQLNEFHCLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCRSAQASVSCALEALEPFWEVLVRSTETVERDNMEEDNVEESEEEGPWEPPVLPILTWPVLQSRTGLVYDQNMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQTISGHALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLSGALASITETIQVHRRYWRSLRVMKVEDREGPSSSKLVTKKAPQPAKPRLAERMTTREKKVLEAGMGKVTSASFGEESTPGQTNSETAVVALTQDQPSEAATGGATLAQTISEAAIGGAMLGQTTSEEAVGGATPDQTTSEETVGGAILDQTTSEDAVGGATLGQTTSEEAVGGATLAQTTSEAAMEGATLDQTTSEEAPGGTELIQTPLASSTDHQTPPTSPVQGTTPQISPSTLIGSLRTLELGSESQGASESQAPGEENLLGEAAGGQDMADSMLMQGSRGLTDQAIFYAVTPLPWCPHLVAVCPIPAAGLDVTQPCGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHGNSGHPLVLSYIDLSAWCYYCQAYVHHQALLDVKNIAHQNKFGEDMPHPH 5EDU,7ZYU,3PHD,3GV4 Protein deacetylase HDAC6 HDAC6_HUMAN Q9UBN7 O94975 Q6NT75 Q7L3E5 Q96CY0 51609111 C#CCN1CCN(CCCOc2ccc3c(ccn3S(=O)(=O)c3ccc(C(=O)NN)cc3)c2)CC1 InChI=1S/C25H29N5O4S/c1-2-11-28-14-16-29(17-15-28)12-3-18-34-22-6-9-24-21(19-22)10-13-30(24)35(32,33)23-7-4-20(5-8-23)25(31)27-26/h1,4-10,13,19H,3,11-12,14-18,26H2,(H,27,31) XYYROHFZJGYLHN-UHFFFAOYSA-N 50648731 CHEMBL5613800 Histone deacetylase 6 Human >10000 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648731 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2556&target=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50648731&enzyme=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search 172378326 519664133 1 MTSTGQDSTTTRQRRSRQNPQSPPQDSSVTSKRNIKKGAVPRSIPNLAEVKKKGKMKKLGQAMEEDLIVGLQGMDLNLEAEALAGTGLVLDEQLNEFHCLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCRSAQASVSCALEALEPFWEVLVRSTETVERDNMEEDNVEESEEEGPWEPPVLPILTWPVLQSRTGLVYDQNMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQTISGHALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLSGALASITETIQVHRRYWRSLRVMKVEDREGPSSSKLVTKKAPQPAKPRLAERMTTREKKVLEAGMGKVTSASFGEESTPGQTNSETAVVALTQDQPSEAATGGATLAQTISEAAIGGAMLGQTTSEEAVGGATPDQTTSEETVGGAILDQTTSEDAVGGATLGQTTSEEAVGGATLAQTTSEAAMEGATLDQTTSEEAPGGTELIQTPLASSTDHQTPPTSPVQGTTPQISPSTLIGSLRTLELGSESQGASESQAPGEENLLGEAAGGQDMADSMLMQGSRGLTDQAIFYAVTPLPWCPHLVAVCPIPAAGLDVTQPCGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHGNSGHPLVLSYIDLSAWCYYCQAYVHHQALLDVKNIAHQNKFGEDMPHPH 5EDU,7ZYU,3PHD,3GV4 Protein deacetylase HDAC6 HDAC6_HUMAN Q9UBN7 O94975 Q6NT75 Q7L3E5 Q96CY0 51609112 CCCNNC(=O)c1ccc(S(=O)(=O)n2ccc3cc(OC)ccc32)cc1 InChI=1S/C19H21N3O4S/c1-3-11-20-21-19(23)14-4-7-17(8-5-14)27(24,25)22-12-10-15-13-16(26-2)6-9-18(15)22/h4-10,12-13,20H,3,11H2,1-2H3,(H,21,23) AIUPOKYBQOXKTF-UHFFFAOYSA-N 50648732 CHEMBL5614364 Histone deacetylase 6 Human >10000 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648732 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2556&target=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50648732&enzyme=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search 172378276 519664134 1 MTSTGQDSTTTRQRRSRQNPQSPPQDSSVTSKRNIKKGAVPRSIPNLAEVKKKGKMKKLGQAMEEDLIVGLQGMDLNLEAEALAGTGLVLDEQLNEFHCLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCRSAQASVSCALEALEPFWEVLVRSTETVERDNMEEDNVEESEEEGPWEPPVLPILTWPVLQSRTGLVYDQNMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQTISGHALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLSGALASITETIQVHRRYWRSLRVMKVEDREGPSSSKLVTKKAPQPAKPRLAERMTTREKKVLEAGMGKVTSASFGEESTPGQTNSETAVVALTQDQPSEAATGGATLAQTISEAAIGGAMLGQTTSEEAVGGATPDQTTSEETVGGAILDQTTSEDAVGGATLGQTTSEEAVGGATLAQTTSEAAMEGATLDQTTSEEAPGGTELIQTPLASSTDHQTPPTSPVQGTTPQISPSTLIGSLRTLELGSESQGASESQAPGEENLLGEAAGGQDMADSMLMQGSRGLTDQAIFYAVTPLPWCPHLVAVCPIPAAGLDVTQPCGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHGNSGHPLVLSYIDLSAWCYYCQAYVHHQALLDVKNIAHQNKFGEDMPHPH 5EDU,7ZYU,3PHD,3GV4 Protein deacetylase HDAC6 HDAC6_HUMAN Q9UBN7 O94975 Q6NT75 Q7L3E5 Q96CY0 51609113 CCCN(CCC)NC(=O)c1ccc(S(=O)(=O)n2ccc3cc(OC)ccc32)cc1 InChI=1S/C22H27N3O4S/c1-4-13-24(14-5-2)23-22(26)17-6-9-20(10-7-17)30(27,28)25-15-12-18-16-19(29-3)8-11-21(18)25/h6-12,15-16H,4-5,13-14H2,1-3H3,(H,23,26) YZNKLAHTJOHJDO-UHFFFAOYSA-N 50648733 CHEMBL5613368 Histone deacetylase 6 Human >10000 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648733 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2556&target=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50648733&enzyme=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search 172378353 519664135 1 MTSTGQDSTTTRQRRSRQNPQSPPQDSSVTSKRNIKKGAVPRSIPNLAEVKKKGKMKKLGQAMEEDLIVGLQGMDLNLEAEALAGTGLVLDEQLNEFHCLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCRSAQASVSCALEALEPFWEVLVRSTETVERDNMEEDNVEESEEEGPWEPPVLPILTWPVLQSRTGLVYDQNMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQTISGHALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLSGALASITETIQVHRRYWRSLRVMKVEDREGPSSSKLVTKKAPQPAKPRLAERMTTREKKVLEAGMGKVTSASFGEESTPGQTNSETAVVALTQDQPSEAATGGATLAQTISEAAIGGAMLGQTTSEEAVGGATPDQTTSEETVGGAILDQTTSEDAVGGATLGQTTSEEAVGGATLAQTTSEAAMEGATLDQTTSEEAPGGTELIQTPLASSTDHQTPPTSPVQGTTPQISPSTLIGSLRTLELGSESQGASESQAPGEENLLGEAAGGQDMADSMLMQGSRGLTDQAIFYAVTPLPWCPHLVAVCPIPAAGLDVTQPCGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHGNSGHPLVLSYIDLSAWCYYCQAYVHHQALLDVKNIAHQNKFGEDMPHPH 5EDU,7ZYU,3PHD,3GV4 Protein deacetylase HDAC6 HDAC6_HUMAN Q9UBN7 O94975 Q6NT75 Q7L3E5 Q96CY0 51609114 CCCNNC(=O)c1ccc(S(=O)(=O)n2ccc3cc(OCCCN4CCCCC4)ccc32)cc1 InChI=1S/C26H34N4O4S/c1-2-14-27-28-26(31)21-7-10-24(11-8-21)35(32,33)30-18-13-22-20-23(9-12-25(22)30)34-19-6-17-29-15-4-3-5-16-29/h7-13,18,20,27H,2-6,14-17,19H2,1H3,(H,28,31) DBWLJMSQVBCNCC-UHFFFAOYSA-N 50648734 CHEMBL5612956 Histone deacetylase 6 Human >10000 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648734 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2556&target=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50648734&enzyme=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search 172378288 519664136 1 MTSTGQDSTTTRQRRSRQNPQSPPQDSSVTSKRNIKKGAVPRSIPNLAEVKKKGKMKKLGQAMEEDLIVGLQGMDLNLEAEALAGTGLVLDEQLNEFHCLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCRSAQASVSCALEALEPFWEVLVRSTETVERDNMEEDNVEESEEEGPWEPPVLPILTWPVLQSRTGLVYDQNMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQTISGHALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLSGALASITETIQVHRRYWRSLRVMKVEDREGPSSSKLVTKKAPQPAKPRLAERMTTREKKVLEAGMGKVTSASFGEESTPGQTNSETAVVALTQDQPSEAATGGATLAQTISEAAIGGAMLGQTTSEEAVGGATPDQTTSEETVGGAILDQTTSEDAVGGATLGQTTSEEAVGGATLAQTTSEAAMEGATLDQTTSEEAPGGTELIQTPLASSTDHQTPPTSPVQGTTPQISPSTLIGSLRTLELGSESQGASESQAPGEENLLGEAAGGQDMADSMLMQGSRGLTDQAIFYAVTPLPWCPHLVAVCPIPAAGLDVTQPCGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHGNSGHPLVLSYIDLSAWCYYCQAYVHHQALLDVKNIAHQNKFGEDMPHPH 5EDU,7ZYU,3PHD,3GV4 Protein deacetylase HDAC6 HDAC6_HUMAN Q9UBN7 O94975 Q6NT75 Q7L3E5 Q96CY0 51609115 C#CCN1CCN(CCCOc2ccc3c(ccn3S(=O)(=O)c3ccc(C(=O)NNCCC)cc3)c2)CC1 InChI=1S/C28H35N5O4S/c1-3-13-29-30-28(34)23-6-9-26(10-7-23)38(35,36)33-16-12-24-22-25(8-11-27(24)33)37-21-5-15-32-19-17-31(14-4-2)18-20-32/h2,6-12,16,22,29H,3,5,13-15,17-21H2,1H3,(H,30,34) DBADGOOZZBNCRM-UHFFFAOYSA-N 50648735 CHEMBL5613964 Histone deacetylase 6 Human >10000 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648735 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2556&target=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50648735&enzyme=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search 172378341 519664137 1 MTSTGQDSTTTRQRRSRQNPQSPPQDSSVTSKRNIKKGAVPRSIPNLAEVKKKGKMKKLGQAMEEDLIVGLQGMDLNLEAEALAGTGLVLDEQLNEFHCLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCRSAQASVSCALEALEPFWEVLVRSTETVERDNMEEDNVEESEEEGPWEPPVLPILTWPVLQSRTGLVYDQNMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQTISGHALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLSGALASITETIQVHRRYWRSLRVMKVEDREGPSSSKLVTKKAPQPAKPRLAERMTTREKKVLEAGMGKVTSASFGEESTPGQTNSETAVVALTQDQPSEAATGGATLAQTISEAAIGGAMLGQTTSEEAVGGATPDQTTSEETVGGAILDQTTSEDAVGGATLGQTTSEEAVGGATLAQTTSEAAMEGATLDQTTSEEAPGGTELIQTPLASSTDHQTPPTSPVQGTTPQISPSTLIGSLRTLELGSESQGASESQAPGEENLLGEAAGGQDMADSMLMQGSRGLTDQAIFYAVTPLPWCPHLVAVCPIPAAGLDVTQPCGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHGNSGHPLVLSYIDLSAWCYYCQAYVHHQALLDVKNIAHQNKFGEDMPHPH 5EDU,7ZYU,3PHD,3GV4 Protein deacetylase HDAC6 HDAC6_HUMAN Q9UBN7 O94975 Q6NT75 Q7L3E5 Q96CY0 51609116 Nc1ccccc1NC(=O)c1ccc(S(=O)(=O)n2ccc3cc(OCc4ccccc4)ccc32)cc1 InChI=1S/C28H23N3O4S/c29-25-8-4-5-9-26(25)30-28(32)21-10-13-24(14-11-21)36(33,34)31-17-16-22-18-23(12-15-27(22)31)35-19-20-6-2-1-3-7-20/h1-18H,19,29H2,(H,30,32) KKAWPXSGKMTDMD-UHFFFAOYSA-N 50648736 CHEMBL5613087 Histone deacetylase 6 Human >10000 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648736 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2556&target=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50648736&enzyme=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search 172378310 519664138 1 MTSTGQDSTTTRQRRSRQNPQSPPQDSSVTSKRNIKKGAVPRSIPNLAEVKKKGKMKKLGQAMEEDLIVGLQGMDLNLEAEALAGTGLVLDEQLNEFHCLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCRSAQASVSCALEALEPFWEVLVRSTETVERDNMEEDNVEESEEEGPWEPPVLPILTWPVLQSRTGLVYDQNMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQTISGHALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLSGALASITETIQVHRRYWRSLRVMKVEDREGPSSSKLVTKKAPQPAKPRLAERMTTREKKVLEAGMGKVTSASFGEESTPGQTNSETAVVALTQDQPSEAATGGATLAQTISEAAIGGAMLGQTTSEEAVGGATPDQTTSEETVGGAILDQTTSEDAVGGATLGQTTSEEAVGGATLAQTTSEAAMEGATLDQTTSEEAPGGTELIQTPLASSTDHQTPPTSPVQGTTPQISPSTLIGSLRTLELGSESQGASESQAPGEENLLGEAAGGQDMADSMLMQGSRGLTDQAIFYAVTPLPWCPHLVAVCPIPAAGLDVTQPCGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHGNSGHPLVLSYIDLSAWCYYCQAYVHHQALLDVKNIAHQNKFGEDMPHPH 5EDU,7ZYU,3PHD,3GV4 Protein deacetylase HDAC6 HDAC6_HUMAN Q9UBN7 O94975 Q6NT75 Q7L3E5 Q96CY0 51609117 Nc1ccccc1NC(=O)c1ccc(S(=O)(=O)n2ccc3cc(OCCCN4CCCCC4)ccc32)cc1 InChI=1S/C29H32N4O4S/c30-26-7-2-3-8-27(26)31-29(34)22-9-12-25(13-10-22)38(35,36)33-19-15-23-21-24(11-14-28(23)33)37-20-6-18-32-16-4-1-5-17-32/h2-3,7-15,19,21H,1,4-6,16-18,20,30H2,(H,31,34) YYUGEXCSSDWUML-UHFFFAOYSA-N 50648737 CHEMBL5614345 Histone deacetylase 6 Human >10000 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648737 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2556&target=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50648737&enzyme=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search 172378361 519664139 1 MTSTGQDSTTTRQRRSRQNPQSPPQDSSVTSKRNIKKGAVPRSIPNLAEVKKKGKMKKLGQAMEEDLIVGLQGMDLNLEAEALAGTGLVLDEQLNEFHCLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCRSAQASVSCALEALEPFWEVLVRSTETVERDNMEEDNVEESEEEGPWEPPVLPILTWPVLQSRTGLVYDQNMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQTISGHALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLSGALASITETIQVHRRYWRSLRVMKVEDREGPSSSKLVTKKAPQPAKPRLAERMTTREKKVLEAGMGKVTSASFGEESTPGQTNSETAVVALTQDQPSEAATGGATLAQTISEAAIGGAMLGQTTSEEAVGGATPDQTTSEETVGGAILDQTTSEDAVGGATLGQTTSEEAVGGATLAQTTSEAAMEGATLDQTTSEEAPGGTELIQTPLASSTDHQTPPTSPVQGTTPQISPSTLIGSLRTLELGSESQGASESQAPGEENLLGEAAGGQDMADSMLMQGSRGLTDQAIFYAVTPLPWCPHLVAVCPIPAAGLDVTQPCGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHGNSGHPLVLSYIDLSAWCYYCQAYVHHQALLDVKNIAHQNKFGEDMPHPH 5EDU,7ZYU,3PHD,3GV4 Protein deacetylase HDAC6 HDAC6_HUMAN Q9UBN7 O94975 Q6NT75 Q7L3E5 Q96CY0 51609118 C#CCN1CCN(CCCOc2ccc3c(ccn3S(=O)(=O)c3ccc(C(=O)Nc4ccccc4N)cc3)c2)CC1 InChI=1S/C31H33N5O4S/c1-2-15-34-18-20-35(21-19-34)16-5-22-40-26-10-13-30-25(23-26)14-17-36(30)41(38,39)27-11-8-24(9-12-27)31(37)33-29-7-4-3-6-28(29)32/h1,3-4,6-14,17,23H,5,15-16,18-22,32H2,(H,33,37) LGBHOVNURIPVBG-UHFFFAOYSA-N 50648738 CHEMBL5612700 Histone deacetylase 6 Human >3333 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648738 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2556&target=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50648738&enzyme=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search 172378280 519664140 1 MTSTGQDSTTTRQRRSRQNPQSPPQDSSVTSKRNIKKGAVPRSIPNLAEVKKKGKMKKLGQAMEEDLIVGLQGMDLNLEAEALAGTGLVLDEQLNEFHCLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCRSAQASVSCALEALEPFWEVLVRSTETVERDNMEEDNVEESEEEGPWEPPVLPILTWPVLQSRTGLVYDQNMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQTISGHALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLSGALASITETIQVHRRYWRSLRVMKVEDREGPSSSKLVTKKAPQPAKPRLAERMTTREKKVLEAGMGKVTSASFGEESTPGQTNSETAVVALTQDQPSEAATGGATLAQTISEAAIGGAMLGQTTSEEAVGGATPDQTTSEETVGGAILDQTTSEDAVGGATLGQTTSEEAVGGATLAQTTSEAAMEGATLDQTTSEEAPGGTELIQTPLASSTDHQTPPTSPVQGTTPQISPSTLIGSLRTLELGSESQGASESQAPGEENLLGEAAGGQDMADSMLMQGSRGLTDQAIFYAVTPLPWCPHLVAVCPIPAAGLDVTQPCGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHGNSGHPLVLSYIDLSAWCYYCQAYVHHQALLDVKNIAHQNKFGEDMPHPH 5EDU,7ZYU,3PHD,3GV4 Protein deacetylase HDAC6 HDAC6_HUMAN Q9UBN7 O94975 Q6NT75 Q7L3E5 Q96CY0 51609119 c1ccc(cc1)NC(=O)CCCCCCC(=O)NO InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 Zolinza::suberoylanilide hydroxamic acid::CHEMBL98::cid_5311::N-hydroxy-N'-phenyloctanediamide::Vorinostat::SAHA::US9115116, SAHA::US9695181, Vorinostat::US9428447, SAHA::US9353061, SAHA::US10188756, Compound SAHA::US10011611, SAHA::US11207431, SAHA::US11505523, Compound SAHA::US20240327418, Example SAHA Histone deacetylase 6 Homo sapiens 29 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2556&target=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search SHH 1C3S,1T69,1ZZ1,3C0Z,4BZ6,4LXZ,4QA0,4QA2,4R7L,5EEI,7JVU,7SGG,7ZZS,8BPC,9GKV,9GKX,9GN6,9O8X,9OAF,9OAM,9OBJ 5311 46519184 CHEMBL98 DB02546 1 MTSTGQDSTTTRQRRSRQNPQSPPQDSSVTSKRNIKKGAVPRSIPNLAEVKKKGKMKKLGQAMEEDLIVGLQGMDLNLEAEALAGTGLVLDEQLNEFHCLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCRSAQASVSCALEALEPFWEVLVRSTETVERDNMEEDNVEESEEEGPWEPPVLPILTWPVLQSRTGLVYDQNMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQTISGHALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLSGALASITETIQVHRRYWRSLRVMKVEDREGPSSSKLVTKKAPQPAKPRLAERMTTREKKVLEAGMGKVTSASFGEESTPGQTNSETAVVALTQDQPSEAATGGATLAQTISEAAIGGAMLGQTTSEEAVGGATPDQTTSEETVGGAILDQTTSEDAVGGATLGQTTSEEAVGGATLAQTTSEAAMEGATLDQTTSEEAPGGTELIQTPLASSTDHQTPPTSPVQGTTPQISPSTLIGSLRTLELGSESQGASESQAPGEENLLGEAAGGQDMADSMLMQGSRGLTDQAIFYAVTPLPWCPHLVAVCPIPAAGLDVTQPCGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHGNSGHPLVLSYIDLSAWCYYCQAYVHHQALLDVKNIAHQNKFGEDMPHPH 5EDU,7ZYU,3PHD,3GV4 Protein deacetylase HDAC6 HDAC6_HUMAN Q9UBN7 O94975 Q6NT75 Q7L3E5 Q96CY0 51609120 CN(CC#C)Cc1cc2cc(OCCCN3CCCCC3)ccc2n1C InChI=1S/C22H31N3O/c1-4-11-23(2)18-20-16-19-17-21(9-10-22(19)24(20)3)26-15-8-14-25-12-6-5-7-13-25/h1,9-10,16-17H,5-8,11-15,18H2,2-3H3 NQDGCGNKNJWZHP-UHFFFAOYSA-N 50281388 CHEMBL4173258 Histone deacetylase 6 Homo sapiens >10000 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50281388 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2556&target=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50281388&enzyme=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search 134817200 406793978 1 MTSTGQDSTTTRQRRSRQNPQSPPQDSSVTSKRNIKKGAVPRSIPNLAEVKKKGKMKKLGQAMEEDLIVGLQGMDLNLEAEALAGTGLVLDEQLNEFHCLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCRSAQASVSCALEALEPFWEVLVRSTETVERDNMEEDNVEESEEEGPWEPPVLPILTWPVLQSRTGLVYDQNMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQTISGHALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLSGALASITETIQVHRRYWRSLRVMKVEDREGPSSSKLVTKKAPQPAKPRLAERMTTREKKVLEAGMGKVTSASFGEESTPGQTNSETAVVALTQDQPSEAATGGATLAQTISEAAIGGAMLGQTTSEEAVGGATPDQTTSEETVGGAILDQTTSEDAVGGATLGQTTSEEAVGGATLAQTTSEAAMEGATLDQTTSEEAPGGTELIQTPLASSTDHQTPPTSPVQGTTPQISPSTLIGSLRTLELGSESQGASESQAPGEENLLGEAAGGQDMADSMLMQGSRGLTDQAIFYAVTPLPWCPHLVAVCPIPAAGLDVTQPCGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHGNSGHPLVLSYIDLSAWCYYCQAYVHHQALLDVKNIAHQNKFGEDMPHPH 5EDU,7ZYU,3PHD,3GV4 Protein deacetylase HDAC6 HDAC6_HUMAN Q9UBN7 O94975 Q6NT75 Q7L3E5 Q96CY0 51609121 CN1CCc2c(c3ccccc3n2Cc4ccc(cc4)C(=O)NO)C1 InChI=1S/C20H21N3O2/c1-22-11-10-19-17(13-22)16-4-2-3-5-18(16)23(19)12-14-6-8-15(9-7-14)20(24)21-25/h2-9,25H,10-13H2,1H3,(H,21,24) GOVYBPLHWIEHEJ-UHFFFAOYSA-N 50380399 CHEMBL2018302::US8748451, 6::Tubastatin A::US9249087, Tubacin::US9751832, Tubastatin A::US10227295, Compound Tubastatin A::US9956192, Compound Tubastatin-A::US10456394, Tubastatin A::US11207431, Example D Histone deacetylase 6 Homo sapiens 16 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50380399 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2556&target=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50380399&enzyme=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search N9W 6THV,6WBQ 49850262 160859482 CHEMBL2018302 1 MTSTGQDSTTTRQRRSRQNPQSPPQDSSVTSKRNIKKGAVPRSIPNLAEVKKKGKMKKLGQAMEEDLIVGLQGMDLNLEAEALAGTGLVLDEQLNEFHCLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCRSAQASVSCALEALEPFWEVLVRSTETVERDNMEEDNVEESEEEGPWEPPVLPILTWPVLQSRTGLVYDQNMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQTISGHALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLSGALASITETIQVHRRYWRSLRVMKVEDREGPSSSKLVTKKAPQPAKPRLAERMTTREKKVLEAGMGKVTSASFGEESTPGQTNSETAVVALTQDQPSEAATGGATLAQTISEAAIGGAMLGQTTSEEAVGGATPDQTTSEETVGGAILDQTTSEDAVGGATLGQTTSEEAVGGATLAQTTSEAAMEGATLDQTTSEEAPGGTELIQTPLASSTDHQTPPTSPVQGTTPQISPSTLIGSLRTLELGSESQGASESQAPGEENLLGEAAGGQDMADSMLMQGSRGLTDQAIFYAVTPLPWCPHLVAVCPIPAAGLDVTQPCGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHGNSGHPLVLSYIDLSAWCYYCQAYVHHQALLDVKNIAHQNKFGEDMPHPH 5EDU,7ZYU,3PHD,3GV4 Protein deacetylase HDAC6 HDAC6_HUMAN Q9UBN7 O94975 Q6NT75 Q7L3E5 Q96CY0 51609122 CCCNNC(=O)c1ccc(S(=O)(=O)n2ccc3cc(OC)ccc32)cc1 InChI=1S/C19H21N3O4S/c1-3-11-20-21-19(23)14-4-7-17(8-5-14)27(24,25)22-12-10-15-13-16(26-2)6-9-18(15)22/h4-10,12-13,20H,3,11H2,1-2H3,(H,21,23) AIUPOKYBQOXKTF-UHFFFAOYSA-N 50648732 CHEMBL5614364 Histone deacetylase 1 Human 87 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648732 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1967&target=Histone+deacetylase+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=50648732&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 172378276 519664134 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51609123 CCCN(CCC)NC(=O)c1ccc(S(=O)(=O)n2ccc3cc(OC)ccc32)cc1 InChI=1S/C22H27N3O4S/c1-4-13-24(14-5-2)23-22(26)17-6-9-20(10-7-17)30(27,28)25-15-12-18-16-19(29-3)8-11-21(18)25/h6-12,15-16H,4-5,13-14H2,1-3H3,(H,23,26) YZNKLAHTJOHJDO-UHFFFAOYSA-N 50648733 CHEMBL5613368 Histone deacetylase 1 Human >10000 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648733 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1967&target=Histone+deacetylase+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=50648733&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 172378353 519664135 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51609124 CCCNNC(=O)c1ccc(S(=O)(=O)n2ccc3cc(OCCCN4CCCCC4)ccc32)cc1 InChI=1S/C26H34N4O4S/c1-2-14-27-28-26(31)21-7-10-24(11-8-21)35(32,33)30-18-13-22-20-23(9-12-25(22)30)34-19-6-17-29-15-4-3-5-16-29/h7-13,18,20,27H,2-6,14-17,19H2,1H3,(H,28,31) DBWLJMSQVBCNCC-UHFFFAOYSA-N 50648734 CHEMBL5612956 Histone deacetylase 1 Human 112 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648734 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1967&target=Histone+deacetylase+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=50648734&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 172378288 519664136 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51609125 C#CCN1CCN(CCCOc2ccc3c(ccn3S(=O)(=O)c3ccc(C(=O)NNCCC)cc3)c2)CC1 InChI=1S/C28H35N5O4S/c1-3-13-29-30-28(34)23-6-9-26(10-7-23)38(35,36)33-16-12-24-22-25(8-11-27(24)33)37-21-5-15-32-19-17-31(14-4-2)18-20-32/h2,6-12,16,22,29H,3,5,13-15,17-21H2,1H3,(H,30,34) DBADGOOZZBNCRM-UHFFFAOYSA-N 50648735 CHEMBL5613964 Histone deacetylase 1 Human 137 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648735 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1967&target=Histone+deacetylase+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=50648735&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 172378341 519664137 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51609126 Nc1ccccc1NC(=O)c1ccc(S(=O)(=O)n2ccc3cc(OCc4ccccc4)ccc32)cc1 InChI=1S/C28H23N3O4S/c29-25-8-4-5-9-26(25)30-28(32)21-10-13-24(14-11-21)36(33,34)31-17-16-22-18-23(12-15-27(22)31)35-19-20-6-2-1-3-7-20/h1-18H,19,29H2,(H,30,32) KKAWPXSGKMTDMD-UHFFFAOYSA-N 50648736 CHEMBL5613087 Histone deacetylase 1 Human 420 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648736 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1967&target=Histone+deacetylase+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=50648736&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 172378310 519664138 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51609127 Nc1ccccc1NC(=O)c1ccc(S(=O)(=O)n2ccc3cc(OCCCN4CCCCC4)ccc32)cc1 InChI=1S/C29H32N4O4S/c30-26-7-2-3-8-27(26)31-29(34)22-9-12-25(13-10-22)38(35,36)33-19-15-23-21-24(11-14-28(23)33)37-20-6-18-32-16-4-1-5-17-32/h2-3,7-15,19,21H,1,4-6,16-18,20,30H2,(H,31,34) YYUGEXCSSDWUML-UHFFFAOYSA-N 50648737 CHEMBL5614345 Histone deacetylase 1 Human 243 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648737 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1967&target=Histone+deacetylase+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=50648737&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 172378361 519664139 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51609128 C#CCN1CCN(CCCOc2ccc3c(ccn3S(=O)(=O)c3ccc(C(=O)Nc4ccccc4N)cc3)c2)CC1 InChI=1S/C31H33N5O4S/c1-2-15-34-18-20-35(21-19-34)16-5-22-40-26-10-13-30-25(23-26)14-17-36(30)41(38,39)27-11-8-24(9-12-27)31(37)33-29-7-4-3-6-28(29)32/h1,3-4,6-14,17,23H,5,15-16,18-22,32H2,(H,33,37) LGBHOVNURIPVBG-UHFFFAOYSA-N 50648738 CHEMBL5612700 Histone deacetylase 1 Human 140 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648738 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1967&target=Histone+deacetylase+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=50648738&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 172378280 519664140 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51609129 c1ccc(cc1)NC(=O)CCCCCCC(=O)NO InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 Zolinza::suberoylanilide hydroxamic acid::CHEMBL98::cid_5311::N-hydroxy-N'-phenyloctanediamide::Vorinostat::SAHA::US9115116, SAHA::US9695181, Vorinostat::US9428447, SAHA::US9353061, SAHA::US10188756, Compound SAHA::US10011611, SAHA::US11207431, SAHA::US11505523, Compound SAHA::US20240327418, Example SAHA Histone deacetylase 1 Homo sapiens 99 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1967&target=Histone+deacetylase+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=19149&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search SHH 1C3S,1T69,1ZZ1,3C0Z,4BZ6,4LXZ,4QA0,4QA2,4R7L,5EEI,7JVU,7SGG,7ZZS,8BPC,9GKV,9GKX,9GN6,9O8X,9OAF,9OAM,9OBJ 5311 46519184 CHEMBL98 DB02546 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 9R4I,8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51609130 CN(CC#C)Cc1cc2cc(OCCCN3CCCCC3)ccc2n1C InChI=1S/C22H31N3O/c1-4-11-23(2)18-20-16-19-17-21(9-10-22(19)24(20)3)26-15-8-14-25-12-6-5-7-13-25/h1,9-10,16-17H,5-8,11-15,18H2,2-3H3 NQDGCGNKNJWZHP-UHFFFAOYSA-N 50281388 CHEMBL4173258 Histone deacetylase 1 Homo sapiens >10000 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50281388 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1967&target=Histone+deacetylase+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=50281388&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 134817200 406793978 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 9R4I,8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51609131 CN1CCc2c(c3ccccc3n2Cc4ccc(cc4)C(=O)NO)C1 InChI=1S/C20H21N3O2/c1-22-11-10-19-17(13-22)16-4-2-3-5-18(16)23(19)12-14-6-8-15(9-7-14)20(24)21-25/h2-9,25H,10-13H2,1H3,(H,21,24) GOVYBPLHWIEHEJ-UHFFFAOYSA-N 50380399 CHEMBL2018302::US8748451, 6::Tubastatin A::US9249087, Tubacin::US9751832, Tubastatin A::US10227295, Compound Tubastatin A::US9956192, Compound Tubastatin-A::US10456394, Tubastatin A::US11207431, Example D Histone deacetylase 1 Homo sapiens 3160 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50380399 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1967&target=Histone+deacetylase+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=50380399&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search N9W 6THV,6WBQ 49850262 160859482 CHEMBL2018302 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 9R4I,8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51609132 C#CCN1CCN(CCCOc2ccc3c(ccn3S(=O)(=O)c3ccc(C(=O)NNCCC)cc3)c2)CC1 InChI=1S/C28H35N5O4S/c1-3-13-29-30-28(34)23-6-9-26(10-7-23)38(35,36)33-16-12-24-22-25(8-11-27(24)33)37-21-5-15-32-19-17-31(14-4-2)18-20-32/h2,6-12,16,22,29H,3,5,13-15,17-21H2,1H3,(H,30,34) DBADGOOZZBNCRM-UHFFFAOYSA-N 50648735 CHEMBL5613964 Amine oxidase [flavin-containing] B Human 384 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648735 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=385&target=Amine+oxidase+%5Bflavin-containing%5D+B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50648735&enzyme=Amine+oxidase+%5Bflavin-containing%5D+B&column=ki&startPg=0&Increment=50&submit=Search 172378341 519664137 1 MSNKCDVVVVGGGISGMAAAKLLHDSGLNVVVLEARDRVGGRTYTLRNQKVKYVDLGGSYVGPTQNRILRLAKELGLETYKVNEVERLIHHVKGKSYPFRGPFPPVWNPITYLDHNNFWRTMDDMGREIPSDAPWKAPLAEEWDNMTMKELLDKLCWTESAKQLATLFVNLCVTAETHEVSALWFLWYVKQCGGTTRIISTTNGGQERKFVGGSGQVSERIMDLLGDRVKLERPVIYIDQTRENVLVETLNHEMYEAKYVISAIPPTLGMKIHFNPPLPMMRNQMITRVPLGSVIKCIVYYKEPFWRKKDYCGTMIIDGEEAPVAYTLDDTKPEGNYAAIMGFILAHKARKLARLTKEERLKKLCELYAKVLGSLEALEPVHYEEKNWCEEQYSGGCYTTYFPPGILTQYGRVLRQPVDRIYFAGTETATHWSGYMEGAVEAGERAAREILHAMGKIPEDEIWQSEPESVDVPAQPITTTFLERHLPSVPGLLRLIGLTTIFSATALGFLAHKRGLLVRV 9FJT,7ZW3,7P4H,7P4F,7B0Z,7B0V,6RLE,6RKP,6RKB,6FWC,6FW0,6FVZ,5MRL,4CRT,4A7A,4A79,3PO7,2XFQ,2XFP,2XFN,2XCG,2VZ2,2VRM,2VRL,2V61,2V60,2V5Z,2C70,2C67,2C66,2C65,2C64,2BYB,2BK3,1S3E,1S3B,1S2Y,1S2Q,1OJD,1OJC,1OJA,1OJ9,1GOS,9R3K,9R3J,9R2J,6YT2,2XFU Amine oxidase [flavin-containing] B AOFB_HUMAN P27338 B2R6R3 B7Z5H3 D3DWC3 Q7Z6S2 51609133 [H][C@@](C)(NCc1ccc(OCc2cccc(F)c2)cc1)C(N)=O |r| InChI=1S/C17H19FN2O2/c1-12(17(19)21)20-10-13-5-7-16(8-6-13)22-11-14-3-2-4-15(18)9-14/h2-9,12,20H,10-11H2,1H3,(H2,19,21) NEMGRZFTLSKBAP-UHFFFAOYSA-N 19187 CHEMBL396778::(2S)-2-[({4-[(3-fluorophenyl)methoxy]phenyl}methyl)amino]propanamide::SAG::Safinamide::US9051240, (S)-(+)-2-[4-(3-Fluorobenzyloxy)-benzylamino]-propanamide Amine oxidase [flavin-containing] B Homo sapiens 8.0 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19187 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=385&target=Amine+oxidase+%5Bflavin-containing%5D+B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19187&enzyme=Amine+oxidase+%5Bflavin-containing%5D+B&column=ki&startPg=0&Increment=50&submit=Search 131682 46519220 CHEMBL396778 1 MSNKCDVVVVGGGISGMAAAKLLHDSGLNVVVLEARDRVGGRTYTLRNQKVKYVDLGGSYVGPTQNRILRLAKELGLETYKVNEVERLIHHVKGKSYPFRGPFPPVWNPITYLDHNNFWRTMDDMGREIPSDAPWKAPLAEEWDNMTMKELLDKLCWTESAKQLATLFVNLCVTAETHEVSALWFLWYVKQCGGTTRIISTTNGGQERKFVGGSGQVSERIMDLLGDRVKLERPVIYIDQTRENVLVETLNHEMYEAKYVISAIPPTLGMKIHFNPPLPMMRNQMITRVPLGSVIKCIVYYKEPFWRKKDYCGTMIIDGEEAPVAYTLDDTKPEGNYAAIMGFILAHKARKLARLTKEERLKKLCELYAKVLGSLEALEPVHYEEKNWCEEQYSGGCYTTYFPPGILTQYGRVLRQPVDRIYFAGTETATHWSGYMEGAVEAGERAAREILHAMGKIPEDEIWQSEPESVDVPAQPITTTFLERHLPSVPGLLRLIGLTTIFSATALGFLAHKRGLLVRV 9FJT,7ZW3,7P4H,7P4F,7B0Z,7B0V,6RLE,6RKP,6RKB,6FWC,6FW0,6FVZ,5MRL,4CRT,4A7A,4A79,3PO7,2XFQ,2XFP,2XFN,2XCG,2VZ2,2VRM,2VRL,2V61,2V60,2V5Z,2C70,2C67,2C66,2C65,2C64,2BYB,2BK3,1S3E,1S3B,1S2Y,1S2Q,1OJD,1OJC,1OJA,1OJ9,1GOS,9R3K,9R3J,9R2J,6YT2,2XFU Amine oxidase [flavin-containing] B AOFB_HUMAN P27338 B2R6R3 B7Z5H3 D3DWC3 Q7Z6S2 51609134 C#CCN[C@@H]1CCc2c1cccc2 InChI=1S/C12H13N/c1-2-9-13-12-8-7-10-5-3-4-6-11(10)12/h1,3-6,12-13H,7-9H2 RUOKEQAAGRXIBM-UHFFFAOYSA-N 10989 (1R)-N-(prop-2-yn-1-yl)-2,3-dihydro-1H-inden-1-amine::CHEMBL887::Rasagiline::US9034303, Rasagiline Amine oxidase [flavin-containing] B Homo sapiens 25 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=10989 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=385&target=Amine+oxidase+%5Bflavin-containing%5D+B&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=10989&enzyme=Amine+oxidase+%5Bflavin-containing%5D+B&column=ki&startPg=0&Increment=50&submit=Search RAU 5G6S 3052776 46511554 CHEMBL887 DB01367 1 MSNKCDVVVVGGGISGMAAAKLLHDSGLNVVVLEARDRVGGRTYTLRNQKVKYVDLGGSYVGPTQNRILRLAKELGLETYKVNEVERLIHHVKGKSYPFRGPFPPVWNPITYLDHNNFWRTMDDMGREIPSDAPWKAPLAEEWDNMTMKELLDKLCWTESAKQLATLFVNLCVTAETHEVSALWFLWYVKQCGGTTRIISTTNGGQERKFVGGSGQVSERIMDLLGDRVKLERPVIYIDQTRENVLVETLNHEMYEAKYVISAIPPTLGMKIHFNPPLPMMRNQMITRVPLGSVIKCIVYYKEPFWRKKDYCGTMIIDGEEAPVAYTLDDTKPEGNYAAIMGFILAHKARKLARLTKEERLKKLCELYAKVLGSLEALEPVHYEEKNWCEEQYSGGCYTTYFPPGILTQYGRVLRQPVDRIYFAGTETATHWSGYMEGAVEAGERAAREILHAMGKIPEDEIWQSEPESVDVPAQPITTTFLERHLPSVPGLLRLIGLTTIFSATALGFLAHKRGLLVRV 9FJT,7ZW3,7P4H,7P4F,7B0Z,7B0V,6RLE,6RKP,6RKB,6FWC,6FW0,6FVZ,5MRL,4CRT,4A7A,4A79,3PO7,2XFQ,2XFP,2XFN,2XCG,2VZ2,2VRM,2VRL,2V61,2V60,2V5Z,2C70,2C67,2C66,2C65,2C64,2BYB,2BK3,1S3E,1S3B,1S2Y,1S2Q,1OJD,1OJC,1OJA,1OJ9,1GOS,9R3K,9R3J,9R2J,6YT2,2XFU Amine oxidase [flavin-containing] B AOFB_HUMAN P27338 B2R6R3 B7Z5H3 D3DWC3 Q7Z6S2 51609136 CCCNNC(=O)c1ccc(S(=O)(=O)n2ccc3cc(OCCCN4CCCCC4)ccc32)cc1 InChI=1S/C26H34N4O4S/c1-2-14-27-28-26(31)21-7-10-24(11-8-21)35(32,33)30-18-13-22-20-23(9-12-25(22)30)34-19-6-17-29-15-4-3-5-16-29/h7-13,18,20,27H,2-6,14-17,19H2,1H3,(H,28,31) DBWLJMSQVBCNCC-UHFFFAOYSA-N 50648734 CHEMBL5612956 Cholinesterase Horse 1180 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648734 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10127&target=Cholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50648734&enzyme=Cholinesterase&column=ki&startPg=0&Increment=50&submit=Search 172378288 519664136 1 EEDIIITTKNGKVRGMNLPVLGGTVTAFLGIPYAQPPLGRLRFKKPQSLTKWSNIWNATKYANSCYQNTDQSFPGFLGSEMWNPNTELSEDCLYLNVWIPAPKPKNATVMIWIYGGGFQTGTSSLPVYDGKFLARVERVIVVSMNYRVGALGFLALSENPEAPGNMGLFDQQLALQWVQKNIAAFGGNPRSVTLFGESAGAASVSLHLLSPRSQPLFTRAILQSGSSNAPWAVTSLYEARNRTLTLAKRMGCSRDNETEMIKCLRDKDPQEILLNEVFVVPYDTLLSVNFGPTVDGDFLTDMPDTLLQLGQFKRTQILVGVNKDEGTAFLVYGAPGFSKDNNSIITRKEFQEGLKIFFPRVSEFGRESILFHYMDWLDDQRAENYREALDDVVGDYNIICPALEFTRKFSELGNDAFFYYFEHRSTKLPWPEWMGVMHGYEIEFVFGLPLERRVNYTRAEEILSRSIMKRWANFAKYGNPNGTQNNSTRWPVFKSTEQKYLTLNTESPKVYTKLRAQQCRFWTLFFPKVLELTGNIDEAEREWKAGFHRWNNYMMDWKNQFNDYTSKKESCSDF 5NN0,4BBZ,2Y1K,2WIK,2WIJ,2WIF Cholinesterase CHLE_HORSE P81908 51609137 C#CCN1CCN(CCCOc2ccc3c(ccn3S(=O)(=O)c3ccc(C(=O)NNCCC)cc3)c2)CC1 InChI=1S/C28H35N5O4S/c1-3-13-29-30-28(34)23-6-9-26(10-7-23)38(35,36)33-16-12-24-22-25(8-11-27(24)33)37-21-5-15-32-19-17-31(14-4-2)18-20-32/h2,6-12,16,22,29H,3,5,13-15,17-21H2,1H3,(H,30,34) DBADGOOZZBNCRM-UHFFFAOYSA-N 50648735 CHEMBL5613964 Cholinesterase Horse 8806 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648735 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=10127&target=Cholinesterase&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50648735&enzyme=Cholinesterase&column=ki&startPg=0&Increment=50&submit=Search 172378341 519664137 1 EEDIIITTKNGKVRGMNLPVLGGTVTAFLGIPYAQPPLGRLRFKKPQSLTKWSNIWNATKYANSCYQNTDQSFPGFLGSEMWNPNTELSEDCLYLNVWIPAPKPKNATVMIWIYGGGFQTGTSSLPVYDGKFLARVERVIVVSMNYRVGALGFLALSENPEAPGNMGLFDQQLALQWVQKNIAAFGGNPRSVTLFGESAGAASVSLHLLSPRSQPLFTRAILQSGSSNAPWAVTSLYEARNRTLTLAKRMGCSRDNETEMIKCLRDKDPQEILLNEVFVVPYDTLLSVNFGPTVDGDFLTDMPDTLLQLGQFKRTQILVGVNKDEGTAFLVYGAPGFSKDNNSIITRKEFQEGLKIFFPRVSEFGRESILFHYMDWLDDQRAENYREALDDVVGDYNIICPALEFTRKFSELGNDAFFYYFEHRSTKLPWPEWMGVMHGYEIEFVFGLPLERRVNYTRAEEILSRSIMKRWANFAKYGNPNGTQNNSTRWPVFKSTEQKYLTLNTESPKVYTKLRAQQCRFWTLFFPKVLELTGNIDEAEREWKAGFHRWNNYMMDWKNQFNDYTSKKESCSDF 5NN0,4BBZ,2Y1K,2WIK,2WIJ,2WIF Cholinesterase CHLE_HORSE P81908 51609139 O=C(NO)c1ccc(S(=O)(=O)n2ccc3cc(OCCCN4CCCCC4)ccc32)cc1 InChI=1S/C23H27N3O5S/c27-23(24-28)18-5-8-21(9-6-18)32(29,30)26-15-11-19-17-20(7-10-22(19)26)31-16-4-14-25-12-2-1-3-13-25/h5-11,15,17,28H,1-4,12-14,16H2,(H,24,27) WKXOTOAMDAIXAM-UHFFFAOYSA-N 50648726 CHEMBL5612392 5-hydroxytryptamine receptor 6 Human 3392 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648726 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2142&target=5-hydroxytryptamine+receptor+6&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50648726&enzyme=5-hydroxytryptamine+receptor+6&column=ki&startPg=0&Increment=50&submit=Search 172378322 519664128 1 MVPEPGPTANSTPAWGAGPPSAPGGSGWVAAALCVVIALTAAANSLLIALICTQPALRNTSNFFLVSLFTSDLMVGLVVMPPAMLNALYGRWVLARGLCLLWTAFDVMCCSASILNLCLISLDRYLLILSPLRYKLRMTPLRALALVLGAWSLAALASFLPLLLGWHELGHARPPVPGQCRLLASLPFVLVASGLTFFLPSGAICFTYCRILLAARKQAVQVASLTTGMASQASETLQVPRTPRPGVESADSRRLATKHSRKALKASLTLGILLGMFFVTWLPFFVANIVQAVCDCISPGLFDVLTWLGYCNSTMNPIIYPLFMRDFKRALGRFLPCPRCPRERQASLASPSLRTSHSGPRPGLSLQQVLPLPLPPDSDSDSDAGSGGSSGLRLTAQLLLPGEATQDPPLPTRAAAAVNFFNIDPAEPELRPHPLGIPTN 7XTB,8JLZ,7YS6 5-hydroxytryptamine receptor 6 5HT6R_HUMAN P50406 Q13640 Q5TGZ1 51609140 C#CCN1CCN(CCCOc2ccc3c(ccn3S(=O)(=O)c3ccc(C(=O)NO)cc3)c2)CC1 InChI=1S/C25H28N4O5S/c1-2-11-27-14-16-28(17-15-27)12-3-18-34-22-6-9-24-21(19-22)10-13-29(24)35(32,33)23-7-4-20(5-8-23)25(30)26-31/h1,4-10,13,19,31H,3,11-12,14-18H2,(H,26,30) GLTMLUZWBIWFLU-UHFFFAOYSA-N 50648727 CHEMBL5612289 5-hydroxytryptamine receptor 6 Human 6376 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648727 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2142&target=5-hydroxytryptamine+receptor+6&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50648727&enzyme=5-hydroxytryptamine+receptor+6&column=ki&startPg=0&Increment=50&submit=Search 172378300 519664129 1 MVPEPGPTANSTPAWGAGPPSAPGGSGWVAAALCVVIALTAAANSLLIALICTQPALRNTSNFFLVSLFTSDLMVGLVVMPPAMLNALYGRWVLARGLCLLWTAFDVMCCSASILNLCLISLDRYLLILSPLRYKLRMTPLRALALVLGAWSLAALASFLPLLLGWHELGHARPPVPGQCRLLASLPFVLVASGLTFFLPSGAICFTYCRILLAARKQAVQVASLTTGMASQASETLQVPRTPRPGVESADSRRLATKHSRKALKASLTLGILLGMFFVTWLPFFVANIVQAVCDCISPGLFDVLTWLGYCNSTMNPIIYPLFMRDFKRALGRFLPCPRCPRERQASLASPSLRTSHSGPRPGLSLQQVLPLPLPPDSDSDSDAGSGGSSGLRLTAQLLLPGEATQDPPLPTRAAAAVNFFNIDPAEPELRPHPLGIPTN 7XTB,8JLZ,7YS6 5-hydroxytryptamine receptor 6 5HT6R_HUMAN P50406 Q13640 Q5TGZ1 51609141 CCCNNC(=O)c1ccc(S(=O)(=O)n2ccc3cc(OC)ccc32)cc1 InChI=1S/C19H21N3O4S/c1-3-11-20-21-19(23)14-4-7-17(8-5-14)27(24,25)22-12-10-15-13-16(26-2)6-9-18(15)22/h4-10,12-13,20H,3,11H2,1-2H3,(H,21,23) AIUPOKYBQOXKTF-UHFFFAOYSA-N 50648732 CHEMBL5614364 5-hydroxytryptamine receptor 6 Human 5820 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648732 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2142&target=5-hydroxytryptamine+receptor+6&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50648732&enzyme=5-hydroxytryptamine+receptor+6&column=ki&startPg=0&Increment=50&submit=Search 172378276 519664134 1 MVPEPGPTANSTPAWGAGPPSAPGGSGWVAAALCVVIALTAAANSLLIALICTQPALRNTSNFFLVSLFTSDLMVGLVVMPPAMLNALYGRWVLARGLCLLWTAFDVMCCSASILNLCLISLDRYLLILSPLRYKLRMTPLRALALVLGAWSLAALASFLPLLLGWHELGHARPPVPGQCRLLASLPFVLVASGLTFFLPSGAICFTYCRILLAARKQAVQVASLTTGMASQASETLQVPRTPRPGVESADSRRLATKHSRKALKASLTLGILLGMFFVTWLPFFVANIVQAVCDCISPGLFDVLTWLGYCNSTMNPIIYPLFMRDFKRALGRFLPCPRCPRERQASLASPSLRTSHSGPRPGLSLQQVLPLPLPPDSDSDSDAGSGGSSGLRLTAQLLLPGEATQDPPLPTRAAAAVNFFNIDPAEPELRPHPLGIPTN 7XTB,8JLZ,7YS6 5-hydroxytryptamine receptor 6 5HT6R_HUMAN P50406 Q13640 Q5TGZ1 51609142 CCCNNC(=O)c1ccc(S(=O)(=O)n2ccc3cc(OCCCN4CCCCC4)ccc32)cc1 InChI=1S/C26H34N4O4S/c1-2-14-27-28-26(31)21-7-10-24(11-8-21)35(32,33)30-18-13-22-20-23(9-12-25(22)30)34-19-6-17-29-15-4-3-5-16-29/h7-13,18,20,27H,2-6,14-17,19H2,1H3,(H,28,31) DBWLJMSQVBCNCC-UHFFFAOYSA-N 50648734 CHEMBL5612956 5-hydroxytryptamine receptor 6 Human 4307 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648734 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2142&target=5-hydroxytryptamine+receptor+6&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50648734&enzyme=5-hydroxytryptamine+receptor+6&column=ki&startPg=0&Increment=50&submit=Search 172378288 519664136 1 MVPEPGPTANSTPAWGAGPPSAPGGSGWVAAALCVVIALTAAANSLLIALICTQPALRNTSNFFLVSLFTSDLMVGLVVMPPAMLNALYGRWVLARGLCLLWTAFDVMCCSASILNLCLISLDRYLLILSPLRYKLRMTPLRALALVLGAWSLAALASFLPLLLGWHELGHARPPVPGQCRLLASLPFVLVASGLTFFLPSGAICFTYCRILLAARKQAVQVASLTTGMASQASETLQVPRTPRPGVESADSRRLATKHSRKALKASLTLGILLGMFFVTWLPFFVANIVQAVCDCISPGLFDVLTWLGYCNSTMNPIIYPLFMRDFKRALGRFLPCPRCPRERQASLASPSLRTSHSGPRPGLSLQQVLPLPLPPDSDSDSDAGSGGSSGLRLTAQLLLPGEATQDPPLPTRAAAAVNFFNIDPAEPELRPHPLGIPTN 7XTB,8JLZ,7YS6 5-hydroxytryptamine receptor 6 5HT6R_HUMAN P50406 Q13640 Q5TGZ1 51609143 C#CCN1CCN(CCCOc2ccc3c(ccn3S(=O)(=O)c3ccc(C(=O)NNCCC)cc3)c2)CC1 InChI=1S/C28H35N5O4S/c1-3-13-29-30-28(34)23-6-9-26(10-7-23)38(35,36)33-16-12-24-22-25(8-11-27(24)33)37-21-5-15-32-19-17-31(14-4-2)18-20-32/h2,6-12,16,22,29H,3,5,13-15,17-21H2,1H3,(H,30,34) DBADGOOZZBNCRM-UHFFFAOYSA-N 50648735 CHEMBL5613964 5-hydroxytryptamine receptor 6 Human 30650 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648735 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2142&target=5-hydroxytryptamine+receptor+6&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50648735&enzyme=5-hydroxytryptamine+receptor+6&column=ki&startPg=0&Increment=50&submit=Search 172378341 519664137 1 MVPEPGPTANSTPAWGAGPPSAPGGSGWVAAALCVVIALTAAANSLLIALICTQPALRNTSNFFLVSLFTSDLMVGLVVMPPAMLNALYGRWVLARGLCLLWTAFDVMCCSASILNLCLISLDRYLLILSPLRYKLRMTPLRALALVLGAWSLAALASFLPLLLGWHELGHARPPVPGQCRLLASLPFVLVASGLTFFLPSGAICFTYCRILLAARKQAVQVASLTTGMASQASETLQVPRTPRPGVESADSRRLATKHSRKALKASLTLGILLGMFFVTWLPFFVANIVQAVCDCISPGLFDVLTWLGYCNSTMNPIIYPLFMRDFKRALGRFLPCPRCPRERQASLASPSLRTSHSGPRPGLSLQQVLPLPLPPDSDSDSDAGSGGSSGLRLTAQLLLPGEATQDPPLPTRAAAAVNFFNIDPAEPELRPHPLGIPTN 7XTB,8JLZ,7YS6 5-hydroxytryptamine receptor 6 5HT6R_HUMAN P50406 Q13640 Q5TGZ1 51609144 O=C(NO)c1ccc(S(=O)(=O)n2ccc3cc(OCCCN4CCCCC4)ccc32)cc1 InChI=1S/C23H27N3O5S/c27-23(24-28)18-5-8-21(9-6-18)32(29,30)26-15-11-19-17-20(7-10-22(19)26)31-16-4-14-25-12-2-1-3-13-25/h5-11,15,17,28H,1-4,12-14,16H2,(H,24,27) WKXOTOAMDAIXAM-UHFFFAOYSA-N 50648726 CHEMBL5612392 Histone deacetylase 2 Human 1924 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648726 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2482&target=Histone+deacetylase+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=50648726&enzyme=Histone+deacetylase+2&column=ki&startPg=0&Increment=50&submit=Search 172378322 519664128 1 MAYSQGGGKKKVCYYYDGDIGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNRQQTDMAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGIDDESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTFNLPLLMLGGGGYTIRNVARCWTYETAVALDCEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTPEYMEKIKQRLFENLRMLPHAPGVQMQAIPEDAVHEDSGDEDGEDPDKRISIRASDKRIACDEEFSDSEDEGEGGRRNVADHKKGAKKARIEEDKKETEDKKTDVKEEDKSKDNSGEKTDTKGTKSEQLSNP 9I2C,9GGN,9GGM,9GGL,8C60,8BPC,8BPB,8BPA,8A0B,7ZZW,7ZZU,7ZZT,7ZZS,7ZZR,7ZZP,7ZZO,9DTQ,9NTB,9K0G,9JWJ,9JV3,6WI3,6WHZ,6WHQ,6WHO,6WHN,7MOZ,7MOY,7MOX,7MOT,7MOS,7LTL,7LTK,7LTG,7KBG,7JS8,6XEC,6XEB,6XDM,6WBZ,6WBW,7KBH,6G3O,4LY1,4LXZ,5IX0,5IWG Histone deacetylase 2 HDAC2_HUMAN Q92769 B3KRS5 B4DL58 E1P561 Q5SRI8 Q5SZ86 Q8NEH4 51609145 C#CCN1CCN(CCCOc2ccc3c(ccn3S(=O)(=O)c3ccc(C(=O)NO)cc3)c2)CC1 InChI=1S/C25H28N4O5S/c1-2-11-27-14-16-28(17-15-27)12-3-18-34-22-6-9-24-21(19-22)10-13-29(24)35(32,33)23-7-4-20(5-8-23)25(30)26-31/h1,4-10,13,19,31H,3,11-12,14-18H2,(H,26,30) GLTMLUZWBIWFLU-UHFFFAOYSA-N 50648727 CHEMBL5612289 Histone deacetylase 2 Human 5413 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648727 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2482&target=Histone+deacetylase+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=50648727&enzyme=Histone+deacetylase+2&column=ki&startPg=0&Increment=50&submit=Search 172378300 519664129 1 MAYSQGGGKKKVCYYYDGDIGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNRQQTDMAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGIDDESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTFNLPLLMLGGGGYTIRNVARCWTYETAVALDCEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTPEYMEKIKQRLFENLRMLPHAPGVQMQAIPEDAVHEDSGDEDGEDPDKRISIRASDKRIACDEEFSDSEDEGEGGRRNVADHKKGAKKARIEEDKKETEDKKTDVKEEDKSKDNSGEKTDTKGTKSEQLSNP 9I2C,9GGN,9GGM,9GGL,8C60,8BPC,8BPB,8BPA,8A0B,7ZZW,7ZZU,7ZZT,7ZZS,7ZZR,7ZZP,7ZZO,9DTQ,9NTB,9K0G,9JWJ,9JV3,6WI3,6WHZ,6WHQ,6WHO,6WHN,7MOZ,7MOY,7MOX,7MOT,7MOS,7LTL,7LTK,7LTG,7KBG,7JS8,6XEC,6XEB,6XDM,6WBZ,6WBW,7KBH,6G3O,4LY1,4LXZ,5IX0,5IWG Histone deacetylase 2 HDAC2_HUMAN Q92769 B3KRS5 B4DL58 E1P561 Q5SRI8 Q5SZ86 Q8NEH4 51609146 CN1CCc2c(c3ccccc3n2Cc4ccc(cc4)C(=O)NO)C1 InChI=1S/C20H21N3O2/c1-22-11-10-19-17(13-22)16-4-2-3-5-18(16)23(19)12-14-6-8-15(9-7-14)20(24)21-25/h2-9,25H,10-13H2,1H3,(H,21,24) GOVYBPLHWIEHEJ-UHFFFAOYSA-N 50380399 CHEMBL2018302::US8748451, 6::Tubastatin A::US9249087, Tubacin::US9751832, Tubastatin A::US10227295, Compound Tubastatin A::US9956192, Compound Tubastatin-A::US10456394, Tubastatin A::US11207431, Example D Histone deacetylase 2 Homo sapiens 4163 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50380399 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2482&target=Histone+deacetylase+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=50380399&enzyme=Histone+deacetylase+2&column=ki&startPg=0&Increment=50&submit=Search N9W 6THV,6WBQ 49850262 160859482 CHEMBL2018302 1 MAYSQGGGKKKVCYYYDGDIGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNRQQTDMAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGIDDESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTFNLPLLMLGGGGYTIRNVARCWTYETAVALDCEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTPEYMEKIKQRLFENLRMLPHAPGVQMQAIPEDAVHEDSGDEDGEDPDKRISIRASDKRIACDEEFSDSEDEGEGGRRNVADHKKGAKKARIEEDKKETEDKKTDVKEEDKSKDNSGEKTDTKGTKSEQLSNP 9I2C,9GGN,9GGM,9GGL,8C60,8BPC,8BPB,8BPA,8A0B,7ZZW,7ZZU,7ZZT,7ZZS,7ZZR,7ZZP,7ZZO,9DTQ,9NTB,9K0G,9JWJ,9JV3,6WI3,6WHZ,6WHQ,6WHO,6WHN,7MOZ,7MOY,7MOX,7MOT,7MOS,7LTL,7LTK,7LTG,7KBG,7JS8,6XEC,6XEB,6XDM,6WBZ,6WBW,7KBH,6G3O,4LY1,4LXZ,5IX0,5IWG Histone deacetylase 2 HDAC2_HUMAN Q92769 B3KRS5 B4DL58 E1P561 Q5SRI8 Q5SZ86 Q8NEH4 51609147 c1ccc(cc1)NC(=O)CCCCCCC(=O)NO InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 Zolinza::suberoylanilide hydroxamic acid::CHEMBL98::cid_5311::N-hydroxy-N'-phenyloctanediamide::Vorinostat::SAHA::US9115116, SAHA::US9695181, Vorinostat::US9428447, SAHA::US9353061, SAHA::US10188756, Compound SAHA::US10011611, SAHA::US11207431, SAHA::US11505523, Compound SAHA::US20240327418, Example SAHA Histone deacetylase 2 Homo sapiens 135 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2482&target=Histone+deacetylase+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=19149&enzyme=Histone+deacetylase+2&column=ki&startPg=0&Increment=50&submit=Search SHH 1C3S,1T69,1ZZ1,3C0Z,4BZ6,4LXZ,4QA0,4QA2,4R7L,5EEI,7JVU,7SGG,7ZZS,8BPC,9GKV,9GKX,9GN6,9O8X,9OAF,9OAM,9OBJ 5311 46519184 CHEMBL98 DB02546 1 MAYSQGGGKKKVCYYYDGDIGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNRQQTDMAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGIDDESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTFNLPLLMLGGGGYTIRNVARCWTYETAVALDCEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTPEYMEKIKQRLFENLRMLPHAPGVQMQAIPEDAVHEDSGDEDGEDPDKRISIRASDKRIACDEEFSDSEDEGEGGRRNVADHKKGAKKARIEEDKKETEDKKTDVKEEDKSKDNSGEKTDTKGTKSEQLSNP 9I2C,9GGN,9GGM,9GGL,8C60,8BPC,8BPB,8BPA,8A0B,7ZZW,7ZZU,7ZZT,7ZZS,7ZZR,7ZZP,7ZZO,9DTQ,9NTB,9K0G,9JWJ,9JV3,6WI3,6WHZ,6WHQ,6WHO,6WHN,7MOZ,7MOY,7MOX,7MOT,7MOS,7LTL,7LTK,7LTG,7KBG,7JS8,6XEC,6XEB,6XDM,6WBZ,6WBW,7KBH,6G3O,4LY1,4LXZ,5IX0,5IWG Histone deacetylase 2 HDAC2_HUMAN Q92769 B3KRS5 B4DL58 E1P561 Q5SRI8 Q5SZ86 Q8NEH4 51609148 O=C(NO)c1ccc(S(=O)(=O)n2ccc3cc(OCCCN4CCCCC4)ccc32)cc1 InChI=1S/C23H27N3O5S/c27-23(24-28)18-5-8-21(9-6-18)32(29,30)26-15-11-19-17-20(7-10-22(19)26)31-16-4-14-25-12-2-1-3-13-25/h5-11,15,17,28H,1-4,12-14,16H2,(H,24,27) WKXOTOAMDAIXAM-UHFFFAOYSA-N 50648726 CHEMBL5612392 Platelet-derived growth factor receptor alpha/beta Mouse 937 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648726 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000002&target=Platelet-derived+growth+factor+receptor+alpha%2Fbeta&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50648726&enzyme=Platelet-derived+growth+factor+receptor+alpha%2Fbeta&column=ki&startPg=0&Increment=50&submit=Search 172378322 519664128 2 MGLPGVIPALVLRGQLLLSVLWLLGPQTSRGLVITPPGPEFVLNISSTFVLTCSGSAPVMWEQMSQVPWQEAAMNQDGTFSSVLTLTNVTGGDTGEYFCVYNNSLGPELSERKRIYIFVPDPTMGFLPMDSEDLFIFVTDVTETTIPCRVTDPQLEVTLHEKKVDIPLHVPYDHQRGFTGTFEDKTYICKTTIGDREVDSDTYYVYSLQVSSINVSVNAVQTVVRQGESITIRCIVMGNDVVNFQWTYPRMKSGRLVEPVTDYLFGVPSRIGSILHIPTAELSDSGTYTCNVSVSVNDHGDEKAINISVIENGYVRLLETLGDVEIAELHRSRTLRVVFEAYPMPSVLWLKDNRTLGDSGAGELVLSTRNMSETRYVSELILVRVKVSEAGYYTMRAFHEDDEVQLSFKLQVNVPVRVLELSESHPANGEQTIRCRGRGMPQPNVTWSTCRDLKRCPRKLSPTPLGNSSKEESQLETNVTFWEEDQEYEVVSTLRLRHVDQPLSVRCMLQNSMGGDSQEVTVVPHSLPFKVVVISAILALVVLTVISLIILIMLWQKKPRYEIRWKVIESVSSDGHEYIYVDPVQLPYDSTWELPRDQLVLGRTLGSGAFGQVVEATAHGLSHSQATMKVAVKMLKSTARSSEKQALMSELKIMSHLGPHLNVVNLLGACTKGGPIYIITEYCRYGDLVDYLHRNKHTFLQRHSNKHCPPSAELYSNALPVGFSLPSHLNLTGESDGGYMDMSKDESIDYVPMLDMKGDIKYADIESPSYMAPYDNYVPSAPERTYRATLINDSPVLSYTDLVGFSYQVANGMDFLASKNCVHRDLAARNVLICEGKLVKICDFGLARDIMRDSNYISKGSTFLPLKWMAPESIFNSLYTTLSDVWSFGILLWEIFTLGGTPYPELPMNDQFYNAIKRGYRMAQPAHASDEIYEIMQKCWEEKFETRPPFSQLVLLLERLLGEGYKKKYQQVDEEFLRSDHPAILRSQARFPGIHSLRSPLDTSSVLYTAVQPNESDNDYIIPLPDPKPDVADEGLPEGSPSLASSTLNEVNTSSTISCDSPLELQEEPQQAEPEAQLEQPQDSGCPGPLAEAEDSFL Platelet-derived growth factor receptor beta PGFRB_MOUSE P05622 E9QPE2 MGTSHQVFLVLSCLLTGPGLISCQLLLPSILPNENEKIVQLNSSFSLRCVGESEVSWQHPMSEEDDPNVEIRSEENNSGLFVTVLEVVNASAAHTGWYTCYYNHTQTDESEIEGRHIYIYVPDPDMAFVPLGMTDSLVIVEEDDSAIIPCRTTDPETQVTLHNNGRLVPASYDSRQGFNGTFSVGPYICEATVKGRTFKTSEFNVYALKATSELNLEMDARQTVYKAGETIVVTCAVFNNEVVDLQWTYPGEVRNKGITMLEEIKLPSIKLVYTLTVPKATVKDSGEYECAARQATKEVKEMKRVTISVHEKGFVEIEPTFGQLEAVNLHEVREFVVEVQAYPTPRISWLKDNLTLIENLTEITTDVQKSQETRYQSKLKLIRAKEEDSGHYTIIVQNEDDVKSYTFELSTLVPASILDLVDDHHGSGGGQTVRCTAEGTPLPEIDWMICKHIKKCNNDTSWTVLASNVSNIITELPRRGRSTVEGRVSFAKVEETIAVRCLAKNNLSVVARELKLVAPTLRSELTVAAAVLVLLVIVIVSLIVLVVIWKQKPRYEIRWRVIESISPDGHEYIYVDPMQLPYDSRWEFPRDGLVLGRILGSGAFGKVVEGTAYGLSRSQPVMKVAVKMLKPTARSSEKQALMSELKIMTHLGPHLNIVNLLGACTKSGPIYIITEYCFYGDLVNYLHKNRDSFMSQHPEKPKKDLDIFGLNPADESTRSYVILSFENNGDYMDMKQADTTQYVPMLERKEVSKYSDIQRSLYDRPASYKKKSMLDSEVKNLLSDDDSEGLTLLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLARDIMHDSNYVSKGSTFLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSLGGTPYPGMMVDSTFYNKIKSGYRMAKPDHATSEVYEIMVQCWNSEPEKRPSFYHLSEIVENLLPGQYKKSYEKIHLDFLKSDHPAVARMRVDSDNAYIGVTYKNEEDKLKDWEGGLDEQRLSADSGYIIPLPDIDPVPEEEDLGKRNRHSSQTSEESAIETGSSSSTFIKREDETIEDIDMMDDIGIDSSDLVEDSFL 6JOL,6JOK,6JOJ,5K5X,5GRN,8PQJ,8PQK,8PQI,8PQH,6A32,8XRR,9GZH,6JOI Platelet-derived growth factor receptor alpha PGFRA_MOUSE P26618 Q3TQ37 Q62046 Q7TSJ3 Q8C4N3 51609149 C#CCN1CCN(CCCOc2ccc3c(ccn3S(=O)(=O)c3ccc(C(=O)NO)cc3)c2)CC1 InChI=1S/C25H28N4O5S/c1-2-11-27-14-16-28(17-15-27)12-3-18-34-22-6-9-24-21(19-22)10-13-29(24)35(32,33)23-7-4-20(5-8-23)25(30)26-31/h1,4-10,13,19,31H,3,11-12,14-18H2,(H,26,30) GLTMLUZWBIWFLU-UHFFFAOYSA-N 50648727 CHEMBL5612289 Platelet-derived growth factor receptor alpha/beta Mouse 2714 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50648727 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000002&target=Platelet-derived+growth+factor+receptor+alpha%2Fbeta&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50648727&enzyme=Platelet-derived+growth+factor+receptor+alpha%2Fbeta&column=ki&startPg=0&Increment=50&submit=Search 172378300 519664129 2 MGLPGVIPALVLRGQLLLSVLWLLGPQTSRGLVITPPGPEFVLNISSTFVLTCSGSAPVMWEQMSQVPWQEAAMNQDGTFSSVLTLTNVTGGDTGEYFCVYNNSLGPELSERKRIYIFVPDPTMGFLPMDSEDLFIFVTDVTETTIPCRVTDPQLEVTLHEKKVDIPLHVPYDHQRGFTGTFEDKTYICKTTIGDREVDSDTYYVYSLQVSSINVSVNAVQTVVRQGESITIRCIVMGNDVVNFQWTYPRMKSGRLVEPVTDYLFGVPSRIGSILHIPTAELSDSGTYTCNVSVSVNDHGDEKAINISVIENGYVRLLETLGDVEIAELHRSRTLRVVFEAYPMPSVLWLKDNRTLGDSGAGELVLSTRNMSETRYVSELILVRVKVSEAGYYTMRAFHEDDEVQLSFKLQVNVPVRVLELSESHPANGEQTIRCRGRGMPQPNVTWSTCRDLKRCPRKLSPTPLGNSSKEESQLETNVTFWEEDQEYEVVSTLRLRHVDQPLSVRCMLQNSMGGDSQEVTVVPHSLPFKVVVISAILALVVLTVISLIILIMLWQKKPRYEIRWKVIESVSSDGHEYIYVDPVQLPYDSTWELPRDQLVLGRTLGSGAFGQVVEATAHGLSHSQATMKVAVKMLKSTARSSEKQALMSELKIMSHLGPHLNVVNLLGACTKGGPIYIITEYCRYGDLVDYLHRNKHTFLQRHSNKHCPPSAELYSNALPVGFSLPSHLNLTGESDGGYMDMSKDESIDYVPMLDMKGDIKYADIESPSYMAPYDNYVPSAPERTYRATLINDSPVLSYTDLVGFSYQVANGMDFLASKNCVHRDLAARNVLICEGKLVKICDFGLARDIMRDSNYISKGSTFLPLKWMAPESIFNSLYTTLSDVWSFGILLWEIFTLGGTPYPELPMNDQFYNAIKRGYRMAQPAHASDEIYEIMQKCWEEKFETRPPFSQLVLLLERLLGEGYKKKYQQVDEEFLRSDHPAILRSQARFPGIHSLRSPLDTSSVLYTAVQPNESDNDYIIPLPDPKPDVADEGLPEGSPSLASSTLNEVNTSSTISCDSPLELQEEPQQAEPEAQLEQPQDSGCPGPLAEAEDSFL Platelet-derived growth factor receptor beta PGFRB_MOUSE P05622 E9QPE2 MGTSHQVFLVLSCLLTGPGLISCQLLLPSILPNENEKIVQLNSSFSLRCVGESEVSWQHPMSEEDDPNVEIRSEENNSGLFVTVLEVVNASAAHTGWYTCYYNHTQTDESEIEGRHIYIYVPDPDMAFVPLGMTDSLVIVEEDDSAIIPCRTTDPETQVTLHNNGRLVPASYDSRQGFNGTFSVGPYICEATVKGRTFKTSEFNVYALKATSELNLEMDARQTVYKAGETIVVTCAVFNNEVVDLQWTYPGEVRNKGITMLEEIKLPSIKLVYTLTVPKATVKDSGEYECAARQATKEVKEMKRVTISVHEKGFVEIEPTFGQLEAVNLHEVREFVVEVQAYPTPRISWLKDNLTLIENLTEITTDVQKSQETRYQSKLKLIRAKEEDSGHYTIIVQNEDDVKSYTFELSTLVPASILDLVDDHHGSGGGQTVRCTAEGTPLPEIDWMICKHIKKCNNDTSWTVLASNVSNIITELPRRGRSTVEGRVSFAKVEETIAVRCLAKNNLSVVARELKLVAPTLRSELTVAAAVLVLLVIVIVSLIVLVVIWKQKPRYEIRWRVIESISPDGHEYIYVDPMQLPYDSRWEFPRDGLVLGRILGSGAFGKVVEGTAYGLSRSQPVMKVAVKMLKPTARSSEKQALMSELKIMTHLGPHLNIVNLLGACTKSGPIYIITEYCFYGDLVNYLHKNRDSFMSQHPEKPKKDLDIFGLNPADESTRSYVILSFENNGDYMDMKQADTTQYVPMLERKEVSKYSDIQRSLYDRPASYKKKSMLDSEVKNLLSDDDSEGLTLLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLARDIMHDSNYVSKGSTFLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSLGGTPYPGMMVDSTFYNKIKSGYRMAKPDHATSEVYEIMVQCWNSEPEKRPSFYHLSEIVENLLPGQYKKSYEKIHLDFLKSDHPAVARMRVDSDNAYIGVTYKNEEDKLKDWEGGLDEQRLSADSGYIIPLPDIDPVPEEEDLGKRNRHSSQTSEESAIETGSSSSTFIKREDETIEDIDMMDDIGIDSSDLVEDSFL 6JOL,6JOK,6JOJ,5K5X,5GRN,8PQJ,8PQK,8PQI,8PQH,6A32,8XRR,9GZH,6JOI Platelet-derived growth factor receptor alpha PGFRA_MOUSE P26618 Q3TQ37 Q62046 Q7TSJ3 Q8C4N3 51609150 CN(CC#C)Cc1cc2cc(OCCCN3CCCCC3)ccc2n1C InChI=1S/C22H31N3O/c1-4-11-23(2)18-20-16-19-17-21(9-10-22(19)24(20)3)26-15-8-14-25-12-6-5-7-13-25/h1,9-10,16-17H,5-8,11-15,18H2,2-3H3 NQDGCGNKNJWZHP-UHFFFAOYSA-N 50281388 CHEMBL4173258 Platelet-derived growth factor receptor alpha/beta Mus musculus >10000 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50281388 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000002&target=Platelet-derived+growth+factor+receptor+alpha%2Fbeta&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50281388&enzyme=Platelet-derived+growth+factor+receptor+alpha%2Fbeta&column=ki&startPg=0&Increment=50&submit=Search 134817200 406793978 2 MGLPGVIPALVLRGQLLLSVLWLLGPQTSRGLVITPPGPEFVLNISSTFVLTCSGSAPVMWEQMSQVPWQEAAMNQDGTFSSVLTLTNVTGGDTGEYFCVYNNSLGPELSERKRIYIFVPDPTMGFLPMDSEDLFIFVTDVTETTIPCRVTDPQLEVTLHEKKVDIPLHVPYDHQRGFTGTFEDKTYICKTTIGDREVDSDTYYVYSLQVSSINVSVNAVQTVVRQGESITIRCIVMGNDVVNFQWTYPRMKSGRLVEPVTDYLFGVPSRIGSILHIPTAELSDSGTYTCNVSVSVNDHGDEKAINISVIENGYVRLLETLGDVEIAELHRSRTLRVVFEAYPMPSVLWLKDNRTLGDSGAGELVLSTRNMSETRYVSELILVRVKVSEAGYYTMRAFHEDDEVQLSFKLQVNVPVRVLELSESHPANGEQTIRCRGRGMPQPNVTWSTCRDLKRCPRKLSPTPLGNSSKEESQLETNVTFWEEDQEYEVVSTLRLRHVDQPLSVRCMLQNSMGGDSQEVTVVPHSLPFKVVVISAILALVVLTVISLIILIMLWQKKPRYEIRWKVIESVSSDGHEYIYVDPVQLPYDSTWELPRDQLVLGRTLGSGAFGQVVEATAHGLSHSQATMKVAVKMLKSTARSSEKQALMSELKIMSHLGPHLNVVNLLGACTKGGPIYIITEYCRYGDLVDYLHRNKHTFLQRHSNKHCPPSAELYSNALPVGFSLPSHLNLTGESDGGYMDMSKDESIDYVPMLDMKGDIKYADIESPSYMAPYDNYVPSAPERTYRATLINDSPVLSYTDLVGFSYQVANGMDFLASKNCVHRDLAARNVLICEGKLVKICDFGLARDIMRDSNYISKGSTFLPLKWMAPESIFNSLYTTLSDVWSFGILLWEIFTLGGTPYPELPMNDQFYNAIKRGYRMAQPAHASDEIYEIMQKCWEEKFETRPPFSQLVLLLERLLGEGYKKKYQQVDEEFLRSDHPAILRSQARFPGIHSLRSPLDTSSVLYTAVQPNESDNDYIIPLPDPKPDVADEGLPEGSPSLASSTLNEVNTSSTISCDSPLELQEEPQQAEPEAQLEQPQDSGCPGPLAEAEDSFL Platelet-derived growth factor receptor beta PGFRB_MOUSE P05622 E9QPE2 MGTSHQVFLVLSCLLTGPGLISCQLLLPSILPNENEKIVQLNSSFSLRCVGESEVSWQHPMSEEDDPNVEIRSEENNSGLFVTVLEVVNASAAHTGWYTCYYNHTQTDESEIEGRHIYIYVPDPDMAFVPLGMTDSLVIVEEDDSAIIPCRTTDPETQVTLHNNGRLVPASYDSRQGFNGTFSVGPYICEATVKGRTFKTSEFNVYALKATSELNLEMDARQTVYKAGETIVVTCAVFNNEVVDLQWTYPGEVRNKGITMLEEIKLPSIKLVYTLTVPKATVKDSGEYECAARQATKEVKEMKRVTISVHEKGFVEIEPTFGQLEAVNLHEVREFVVEVQAYPTPRISWLKDNLTLIENLTEITTDVQKSQETRYQSKLKLIRAKEEDSGHYTIIVQNEDDVKSYTFELSTLVPASILDLVDDHHGSGGGQTVRCTAEGTPLPEIDWMICKHIKKCNNDTSWTVLASNVSNIITELPRRGRSTVEGRVSFAKVEETIAVRCLAKNNLSVVARELKLVAPTLRSELTVAAAVLVLLVIVIVSLIVLVVIWKQKPRYEIRWRVIESISPDGHEYIYVDPMQLPYDSRWEFPRDGLVLGRILGSGAFGKVVEGTAYGLSRSQPVMKVAVKMLKPTARSSEKQALMSELKIMTHLGPHLNIVNLLGACTKSGPIYIITEYCFYGDLVNYLHKNRDSFMSQHPEKPKKDLDIFGLNPADESTRSYVILSFENNGDYMDMKQADTTQYVPMLERKEVSKYSDIQRSLYDRPASYKKKSMLDSEVKNLLSDDDSEGLTLLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLARDIMHDSNYVSKGSTFLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSLGGTPYPGMMVDSTFYNKIKSGYRMAKPDHATSEVYEIMVQCWNSEPEKRPSFYHLSEIVENLLPGQYKKSYEKIHLDFLKSDHPAVARMRVDSDNAYIGVTYKNEEDKLKDWEGGLDEQRLSADSGYIIPLPDIDPVPEEEDLGKRNRHSSQTSEESAIETGSSSSTFIKREDETIEDIDMMDDIGIDSSDLVEDSFL 6JOL,6JOK,6JOJ,5K5X,5GRN,8PQJ,8PQK,8PQI,8PQH,6A32,8XRR,9GZH,6JOI Platelet-derived growth factor receptor alpha PGFRA_MOUSE P26618 Q3TQ37 Q62046 Q7TSJ3 Q8C4N3 51609151 CN1CCc2c(c3ccccc3n2Cc4ccc(cc4)C(=O)NO)C1 InChI=1S/C20H21N3O2/c1-22-11-10-19-17(13-22)16-4-2-3-5-18(16)23(19)12-14-6-8-15(9-7-14)20(24)21-25/h2-9,25H,10-13H2,1H3,(H,21,24) GOVYBPLHWIEHEJ-UHFFFAOYSA-N 50380399 CHEMBL2018302::US8748451, 6::Tubastatin A::US9249087, Tubacin::US9751832, Tubastatin A::US10227295, Compound Tubastatin A::US9956192, Compound Tubastatin-A::US10456394, Tubastatin A::US11207431, Example D Platelet-derived growth factor receptor alpha/beta Mus musculus 2526 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50380399 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000002&target=Platelet-derived+growth+factor+receptor+alpha%2Fbeta&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50380399&enzyme=Platelet-derived+growth+factor+receptor+alpha%2Fbeta&column=ki&startPg=0&Increment=50&submit=Search N9W 49850262 160859482 CHEMBL2018302 2 MGLPGVIPALVLRGQLLLSVLWLLGPQTSRGLVITPPGPEFVLNISSTFVLTCSGSAPVMWEQMSQVPWQEAAMNQDGTFSSVLTLTNVTGGDTGEYFCVYNNSLGPELSERKRIYIFVPDPTMGFLPMDSEDLFIFVTDVTETTIPCRVTDPQLEVTLHEKKVDIPLHVPYDHQRGFTGTFEDKTYICKTTIGDREVDSDTYYVYSLQVSSINVSVNAVQTVVRQGESITIRCIVMGNDVVNFQWTYPRMKSGRLVEPVTDYLFGVPSRIGSILHIPTAELSDSGTYTCNVSVSVNDHGDEKAINISVIENGYVRLLETLGDVEIAELHRSRTLRVVFEAYPMPSVLWLKDNRTLGDSGAGELVLSTRNMSETRYVSELILVRVKVSEAGYYTMRAFHEDDEVQLSFKLQVNVPVRVLELSESHPANGEQTIRCRGRGMPQPNVTWSTCRDLKRCPRKLSPTPLGNSSKEESQLETNVTFWEEDQEYEVVSTLRLRHVDQPLSVRCMLQNSMGGDSQEVTVVPHSLPFKVVVISAILALVVLTVISLIILIMLWQKKPRYEIRWKVIESVSSDGHEYIYVDPVQLPYDSTWELPRDQLVLGRTLGSGAFGQVVEATAHGLSHSQATMKVAVKMLKSTARSSEKQALMSELKIMSHLGPHLNVVNLLGACTKGGPIYIITEYCRYGDLVDYLHRNKHTFLQRHSNKHCPPSAELYSNALPVGFSLPSHLNLTGESDGGYMDMSKDESIDYVPMLDMKGDIKYADIESPSYMAPYDNYVPSAPERTYRATLINDSPVLSYTDLVGFSYQVANGMDFLASKNCVHRDLAARNVLICEGKLVKICDFGLARDIMRDSNYISKGSTFLPLKWMAPESIFNSLYTTLSDVWSFGILLWEIFTLGGTPYPELPMNDQFYNAIKRGYRMAQPAHASDEIYEIMQKCWEEKFETRPPFSQLVLLLERLLGEGYKKKYQQVDEEFLRSDHPAILRSQARFPGIHSLRSPLDTSSVLYTAVQPNESDNDYIIPLPDPKPDVADEGLPEGSPSLASSTLNEVNTSSTISCDSPLELQEEPQQAEPEAQLEQPQDSGCPGPLAEAEDSFL Platelet-derived growth factor receptor beta PGFRB_MOUSE P05622 E9QPE2 MGTSHQVFLVLSCLLTGPGLISCQLLLPSILPNENEKIVQLNSSFSLRCVGESEVSWQHPMSEEDDPNVEIRSEENNSGLFVTVLEVVNASAAHTGWYTCYYNHTQTDESEIEGRHIYIYVPDPDMAFVPLGMTDSLVIVEEDDSAIIPCRTTDPETQVTLHNNGRLVPASYDSRQGFNGTFSVGPYICEATVKGRTFKTSEFNVYALKATSELNLEMDARQTVYKAGETIVVTCAVFNNEVVDLQWTYPGEVRNKGITMLEEIKLPSIKLVYTLTVPKATVKDSGEYECAARQATKEVKEMKRVTISVHEKGFVEIEPTFGQLEAVNLHEVREFVVEVQAYPTPRISWLKDNLTLIENLTEITTDVQKSQETRYQSKLKLIRAKEEDSGHYTIIVQNEDDVKSYTFELSTLVPASILDLVDDHHGSGGGQTVRCTAEGTPLPEIDWMICKHIKKCNNDTSWTVLASNVSNIITELPRRGRSTVEGRVSFAKVEETIAVRCLAKNNLSVVARELKLVAPTLRSELTVAAAVLVLLVIVIVSLIVLVVIWKQKPRYEIRWRVIESISPDGHEYIYVDPMQLPYDSRWEFPRDGLVLGRILGSGAFGKVVEGTAYGLSRSQPVMKVAVKMLKPTARSSEKQALMSELKIMTHLGPHLNIVNLLGACTKSGPIYIITEYCFYGDLVNYLHKNRDSFMSQHPEKPKKDLDIFGLNPADESTRSYVILSFENNGDYMDMKQADTTQYVPMLERKEVSKYSDIQRSLYDRPASYKKKSMLDSEVKNLLSDDDSEGLTLLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLARDIMHDSNYVSKGSTFLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSLGGTPYPGMMVDSTFYNKIKSGYRMAKPDHATSEVYEIMVQCWNSEPEKRPSFYHLSEIVENLLPGQYKKSYEKIHLDFLKSDHPAVARMRVDSDNAYIGVTYKNEEDKLKDWEGGLDEQRLSADSGYIIPLPDIDPVPEEEDLGKRNRHSSQTSEESAIETGSSSSTFIKREDETIEDIDMMDDIGIDSSDLVEDSFL 6JOL,6JOK,6JOJ,5K5X,5GRN,8PQJ,8PQK,8PQI,8PQH,6A32,8XRR,9GZH,6JOI Platelet-derived growth factor receptor alpha PGFRA_MOUSE P26618 Q3TQ37 Q62046 Q7TSJ3 Q8C4N3 51609152 c1ccc(cc1)NC(=O)CCCCCCC(=O)NO InChI=1S/C14H20N2O3/c17-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(18)16-19/h3-5,8-9,19H,1-2,6-7,10-11H2,(H,15,17)(H,16,18) WAEXFXRVDQXREF-UHFFFAOYSA-N 19149 Zolinza::suberoylanilide hydroxamic acid::CHEMBL98::cid_5311::N-hydroxy-N'-phenyloctanediamide::Vorinostat::SAHA::US9115116, SAHA::US9695181, Vorinostat::US9428447, SAHA::US9353061, SAHA::US10188756, Compound SAHA::US10011611, SAHA::US11207431, SAHA::US11505523, Compound SAHA::US20240327418, Example SAHA Platelet-derived growth factor receptor alpha/beta Mus musculus 62 ChEMBL 10.7270/Q2GB28QW 39256214 Toledano-Pinedo, M; Porro-Pérez, A; Schäker-Hübner, L; Romero, F; Dong, M; Samadi, A; Almendros, P; Iriepa, I; Bautista-Aguilera, ÒM; Rodríguez-Fernández, MM; Solana-Manrique, C; Sanchis, I; Mora-Morell, A; Rodrìguez, AC; Sànchez-Pérez, AM; Knez, D; Gobec, S; Bellver-Sanchis, A; Pérez, B; Dobrydnev, AV; Artetxe-Zurutuza, A; Matheu, A; Siwek, A; Wolak, M; Satała, G; Bojarski, AJ; Doroz-Płonka, A; Handzlik, J; Godyń, J; Więckowska, A; Paricio, N; Griñán-Ferré, C; Hansen, FK; Marco-Contelles, J //0 10/12/2025 Institute of General Organic Chemistry (CSIC) http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=19149 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=com&complexid=50000002&target=Platelet-derived+growth+factor+receptor+alpha%2Fbeta&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Platelet-derived+growth+factor+receptor+alpha%2Fbeta&column=ki&startPg=0&Increment=50&submit=Search SHH 5311 46519184 CHEMBL98 DB02546 2 MGLPGVIPALVLRGQLLLSVLWLLGPQTSRGLVITPPGPEFVLNISSTFVLTCSGSAPVMWEQMSQVPWQEAAMNQDGTFSSVLTLTNVTGGDTGEYFCVYNNSLGPELSERKRIYIFVPDPTMGFLPMDSEDLFIFVTDVTETTIPCRVTDPQLEVTLHEKKVDIPLHVPYDHQRGFTGTFEDKTYICKTTIGDREVDSDTYYVYSLQVSSINVSVNAVQTVVRQGESITIRCIVMGNDVVNFQWTYPRMKSGRLVEPVTDYLFGVPSRIGSILHIPTAELSDSGTYTCNVSVSVNDHGDEKAINISVIENGYVRLLETLGDVEIAELHRSRTLRVVFEAYPMPSVLWLKDNRTLGDSGAGELVLSTRNMSETRYVSELILVRVKVSEAGYYTMRAFHEDDEVQLSFKLQVNVPVRVLELSESHPANGEQTIRCRGRGMPQPNVTWSTCRDLKRCPRKLSPTPLGNSSKEESQLETNVTFWEEDQEYEVVSTLRLRHVDQPLSVRCMLQNSMGGDSQEVTVVPHSLPFKVVVISAILALVVLTVISLIILIMLWQKKPRYEIRWKVIESVSSDGHEYIYVDPVQLPYDSTWELPRDQLVLGRTLGSGAFGQVVEATAHGLSHSQATMKVAVKMLKSTARSSEKQALMSELKIMSHLGPHLNVVNLLGACTKGGPIYIITEYCRYGDLVDYLHRNKHTFLQRHSNKHCPPSAELYSNALPVGFSLPSHLNLTGESDGGYMDMSKDESIDYVPMLDMKGDIKYADIESPSYMAPYDNYVPSAPERTYRATLINDSPVLSYTDLVGFSYQVANGMDFLASKNCVHRDLAARNVLICEGKLVKICDFGLARDIMRDSNYISKGSTFLPLKWMAPESIFNSLYTTLSDVWSFGILLWEIFTLGGTPYPELPMNDQFYNAIKRGYRMAQPAHASDEIYEIMQKCWEEKFETRPPFSQLVLLLERLLGEGYKKKYQQVDEEFLRSDHPAILRSQARFPGIHSLRSPLDTSSVLYTAVQPNESDNDYIIPLPDPKPDVADEGLPEGSPSLASSTLNEVNTSSTISCDSPLELQEEPQQAEPEAQLEQPQDSGCPGPLAEAEDSFL Platelet-derived growth factor receptor beta PGFRB_MOUSE P05622 E9QPE2 MGTSHQVFLVLSCLLTGPGLISCQLLLPSILPNENEKIVQLNSSFSLRCVGESEVSWQHPMSEEDDPNVEIRSEENNSGLFVTVLEVVNASAAHTGWYTCYYNHTQTDESEIEGRHIYIYVPDPDMAFVPLGMTDSLVIVEEDDSAIIPCRTTDPETQVTLHNNGRLVPASYDSRQGFNGTFSVGPYICEATVKGRTFKTSEFNVYALKATSELNLEMDARQTVYKAGETIVVTCAVFNNEVVDLQWTYPGEVRNKGITMLEEIKLPSIKLVYTLTVPKATVKDSGEYECAARQATKEVKEMKRVTISVHEKGFVEIEPTFGQLEAVNLHEVREFVVEVQAYPTPRISWLKDNLTLIENLTEITTDVQKSQETRYQSKLKLIRAKEEDSGHYTIIVQNEDDVKSYTFELSTLVPASILDLVDDHHGSGGGQTVRCTAEGTPLPEIDWMICKHIKKCNNDTSWTVLASNVSNIITELPRRGRSTVEGRVSFAKVEETIAVRCLAKNNLSVVARELKLVAPTLRSELTVAAAVLVLLVIVIVSLIVLVVIWKQKPRYEIRWRVIESISPDGHEYIYVDPMQLPYDSRWEFPRDGLVLGRILGSGAFGKVVEGTAYGLSRSQPVMKVAVKMLKPTARSSEKQALMSELKIMTHLGPHLNIVNLLGACTKSGPIYIITEYCFYGDLVNYLHKNRDSFMSQHPEKPKKDLDIFGLNPADESTRSYVILSFENNGDYMDMKQADTTQYVPMLERKEVSKYSDIQRSLYDRPASYKKKSMLDSEVKNLLSDDDSEGLTLLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLARDIMHDSNYVSKGSTFLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSLGGTPYPGMMVDSTFYNKIKSGYRMAKPDHATSEVYEIMVQCWNSEPEKRPSFYHLSEIVENLLPGQYKKSYEKIHLDFLKSDHPAVARMRVDSDNAYIGVTYKNEEDKLKDWEGGLDEQRLSADSGYIIPLPDIDPVPEEEDLGKRNRHSSQTSEESAIETGSSSSTFIKREDETIEDIDMMDDIGIDSSDLVEDSFL 6JOL,6JOK,6JOJ,5K5X,5GRN,8PQJ,8PQK,8PQI,8PQH,6A32,8XRR,9GZH,6JOI Platelet-derived growth factor receptor alpha PGFRA_MOUSE P26618 Q3TQ37 Q62046 Q7TSJ3 Q8C4N3