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 51590139 CCCCNNC(=O)c1ccc(Br)cc1 InChI=1S/C11H15BrN2O/c1-2-3-8-13-14-11(15)9-4-6-10(12)7-5-9/h4-7,13H,2-3,8H2,1H3,(H,14,15) BVQCFCYPFJOOAV-UHFFFAOYSA-N 163619 UF010::US10807944, Compound UF010::US11731934, Compound UF010 Histone deacetylase 1 Homo sapiens 460 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=163619 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=163619&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 4596836 310305336 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 9R4I,8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51590140 CCCCNNC(=O)c1ccc(Br)cc1 InChI=1S/C11H15BrN2O/c1-2-3-8-13-14-11(15)9-4-6-10(12)7-5-9/h4-7,13H,2-3,8H2,1H3,(H,14,15) BVQCFCYPFJOOAV-UHFFFAOYSA-N 163619 UF010::US10807944, Compound UF010::US11731934, Compound UF010 Histone deacetylase 3 Homo sapiens 190 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=163619 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1995&target=Histone+deacetylase+3&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=163619&enzyme=Histone+deacetylase+3&column=ki&startPg=0&Increment=50&submit=Search 4596836 310305336 1 MAKTVAYFYDPDVGNFHYGAGHPMKPHRLALTHSLVLHYGLYKKMIVFKPYQASQHDMCRFHSEDYIDFLQRVSPTNMQGFTKSLNAFNVGDDCPVFPGLFEFCSRYTGASLQGATQLNNKICDIAINWAGGLHHAKKFEASGFCYVNDIVIGILELLKYHPRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYKHLFQPVINQVVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEYVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVEEAISEELPYSEYFEYFAPDFTLHPDVSTRIENQNSRQYLDQIRQTIFENLKMLNHAPSVQIHDVPADLLTYDRTDEADAEERGPEENYSRPEAPNEFYDGDHDNDKESDVEI 4A69 Histone deacetylase 3 HDAC3_HUMAN O15379 D3DQE1 O43268 Q9UEI5 Q9UEV0 51590141 CCCCNNC(=O)c1ccc(Br)cc1 InChI=1S/C11H15BrN2O/c1-2-3-8-13-14-11(15)9-4-6-10(12)7-5-9/h4-7,13H,2-3,8H2,1H3,(H,14,15) BVQCFCYPFJOOAV-UHFFFAOYSA-N 163619 UF010::US10807944, Compound UF010::US11731934, Compound UF010 Histone deacetylase 8 Homo sapiens 2830 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=163619 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1996&target=Histone+deacetylase+8&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=163619&enzyme=Histone+deacetylase+8&column=ki&startPg=0&Increment=50&submit=Search 4596836 310305336 1 MEEPEEPADSGQSLVPVYIYSPEYVSMCDSLAKIPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIEYGLGYDCPATEGIFDYAAAIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCRPDRNEPHRIQQILNYIKGNLKHVV 3SFH,3SFF,6ODC,6ODB,6ODA,5FCW,1W22,1VKG,1T69,1T67,1T64,3RQD,3MZ3,3F0R,3F07,5VI6 Histone deacetylase 8 HDAC8_HUMAN Q9BY41 A6ND12 A6ND61 A6NET3 A6NJR3 A8MQ62 B4DKN0 B4DV22 Q86VC8 Q9NP76 Q9NYH4 51590142 CCCCNNC(=O)c1ccc(Br)cc1 InChI=1S/C11H15BrN2O/c1-2-3-8-13-14-11(15)9-4-6-10(12)7-5-9/h4-7,13H,2-3,8H2,1H3,(H,14,15) BVQCFCYPFJOOAV-UHFFFAOYSA-N 163619 UF010::US10807944, Compound UF010::US11731934, Compound UF010 Histone deacetylase 6 Homo sapiens 9090 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=163619 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=163619&enzyme=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search 4596836 310305336 1 MTSTGQDSTTTRQRRSRQNPQSPPQDSSVTSKRNIKKGAVPRSIPNLAEVKKKGKMKKLGQAMEEDLIVGLQGMDLNLEAEALAGTGLVLDEQLNEFHCLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCRSAQASVSCALEALEPFWEVLVRSTETVERDNMEEDNVEESEEEGPWEPPVLPILTWPVLQSRTGLVYDQNMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQTISGHALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLSGALASITETIQVHRRYWRSLRVMKVEDREGPSSSKLVTKKAPQPAKPRLAERMTTREKKVLEAGMGKVTSASFGEESTPGQTNSETAVVALTQDQPSEAATGGATLAQTISEAAIGGAMLGQTTSEEAVGGATPDQTTSEETVGGAILDQTTSEDAVGGATLGQTTSEEAVGGATLAQTTSEAAMEGATLDQTTSEEAPGGTELIQTPLASSTDHQTPPTSPVQGTTPQISPSTLIGSLRTLELGSESQGASESQAPGEENLLGEAAGGQDMADSMLMQGSRGLTDQAIFYAVTPLPWCPHLVAVCPIPAAGLDVTQPCGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHGNSGHPLVLSYIDLSAWCYYCQAYVHHQALLDVKNIAHQNKFGEDMPHPH 5EDU,7ZYU,3PHD,3GV4 Protein deacetylase HDAC6 HDAC6_HUMAN Q9UBN7 O94975 Q6NT75 Q7L3E5 Q96CY0 51590143 CCCCNNC(=O)c1ccc(Br)cc1 InChI=1S/C11H15BrN2O/c1-2-3-8-13-14-11(15)9-4-6-10(12)7-5-9/h4-7,13H,2-3,8H2,1H3,(H,14,15) BVQCFCYPFJOOAV-UHFFFAOYSA-N 163619 UF010::US10807944, Compound UF010::US11731934, Compound UF010 Polyamine deacetylase HDAC10 Homo sapiens 15300 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=163619 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2538&target=Polyamine+deacetylase+HDAC10&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=163619&enzyme=Polyamine+deacetylase+HDAC10&column=ki&startPg=0&Increment=50&submit=Search 4596836 310305336 1 MGTALVYHEDMTATRLLWDDPECEIERPERLTAALDRLRQRGLEQRCLRLSAREASEEELGLVHSPEYVSLVRETQVLGKEELQALSGQFDAIYFHPSTFHCARLAAGAGLQLVDAVLTGAVQNGLALVRPPGHHGQRAAANGFCVFNNVAIAAAHAKQKHGLHRILVVDWDVHHGQGIQYLFEDDPSVLYFSWHRYEHGRFWPFLRESDADAVGRGQGLGFTVNLPWNQVGMGNADYVAAFLHLLLPLAFEFDPELVLVSAGFDSAIGDPEGQMQATPECFAHLTQLLQVLAGGRVCAVLEGGYHLESLAESVCMTVQTLLGDPAPPLSGPMAPCQSALESIQSARAAQAPHWKSLQQQDVTAVPMSPSSHSPEGRPPPLLPGGPVCKAAASAPSSLLDQPCLCPAPSVRTAVALTTPDITLVLPPDVIQQEASALREETEAWARPHESLAREEALTALGKLLYLLDGMLDGQVNSGIAATPASAAAATLDVAVRRGLSHGAQRLLCVALGQLDRPPDLAHDGRSLWLNIRGKEAAALSMFHVSTPLPVMTGGFLSCILGLVLPLAYGFQPDLVLVALGPGHGLQGPHAALLAAMLRGLAGGRVLALLEENSTPQLAGILARVLNGEAPPSLGPSSVASPEDVQALMYLRGQLEPQWKMLQCHPHLVA Polyamine deacetylase HDAC10 HDA10_HUMAN Q969S8 Q08AP4 Q6STF9 Q96P77 Q96P78 Q9H028 Q9UGX1 Q9UGX2 51590144 CCCCNNC(=O)c1ccc(Br)cc1 InChI=1S/C11H15BrN2O/c1-2-3-8-13-14-11(15)9-4-6-10(12)7-5-9/h4-7,13H,2-3,8H2,1H3,(H,14,15) BVQCFCYPFJOOAV-UHFFFAOYSA-N 163619 UF010::US10807944, Compound UF010::US11731934, Compound UF010 Histone deacetylase 5 Homo sapiens >100000 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=163619 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6108&target=Histone+deacetylase+5&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=163619&enzyme=Histone+deacetylase+5&column=ki&startPg=0&Increment=50&submit=Search 4596836 310305336 1 MNSPNESDGMSGREPSLEILPRTSLHSIPVTVEVKPVLPRAMPSSMGGGGGGSPSPVELRGALVGSVDPTLREQQLQQELLALKQQQQLQKQLLFAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKQQQEMLAAKRQQELEQQRQREQQRQEELEKQRLEQQLLILRNKEKSKESAIASTEVKLRLQEFLLSKSKEPTPGGLNHSLPQHPKCWGAHHASLDQSSPPQSGPPGTPPSYKLPLPGPYDSRDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGTVISTFKKRAVEITGAGPGASSVCNSAPGSGPSSPNSSHSTIAENGFTGSVPNIPTEMLPQHRALPLDSSPNQFSLYTSPSLPNISLGLQATVTVTNSHLTASPKLSTQQEAERQALQSLRQGGTLTGKFMSTSSIPGCLLGVALEGDGSPHGHASLLQHVLLLEQARQQSTLIAVPLHGQSPLVTGERVATSMRTVGKLPRHRPLSRTQSSPLPQSPQALQQLVMQQQHQQFLEKQKQQQLQLGKILTKTGELPRQPTTHPEETEEELTEQQEVLLGEGALTMPREGSTESESTQEDLEEEDEEDDGEEEEDCIQVKDEEGESGAEEGPDLEEPGAGYKKLFSDAQPLQPLQVYQAPLSLATVPHQALGRTQSSPAAPGGMKSPPDQPVKHLFTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLNRQKLDSKKLLGPISQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVGYNVNVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRVVLALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPNINAVATLEKVIEIQSKHWSCVQKFAAGLGRSLREAQAGETEEAETVSAMALLSVGAEQAQAAAAREHSPRPAEEPMEQEPAL Histone deacetylase 5 HDAC5_HUMAN Q9UQL6 C9JFV9 O60340 O60528 Q96DY4 51590145 CCCCNNC(=O)c1ccc(Br)cc1 InChI=1S/C11H15BrN2O/c1-2-3-8-13-14-11(15)9-4-6-10(12)7-5-9/h4-7,13H,2-3,8H2,1H3,(H,14,15) BVQCFCYPFJOOAV-UHFFFAOYSA-N 163619 UF010::US10807944, Compound UF010::US11731934, Compound UF010 Histone deacetylase 7 Homo sapiens >100000 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=163619 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2645&target=Histone+deacetylase+7&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=163619&enzyme=Histone+deacetylase+7&column=ki&startPg=0&Increment=50&submit=Search 4596836 310305336 1 MDLRVGQRPPVEPPPEPTLLALQRPQRLHHHLFLAGLQQQRSVEPMRLSMDTPMPELQVGPQEQELRQLLHKDKSKRSAVASSVVKQKLAEVILKKQQAALERTVHPNSPGIPYRTLEPLETEGATRSMLSSFLPPVPSLPSDPPEHFPLRKTVSEPNLKLRYKPKKSLERRKNPLLRKESAPPSLRRRPAETLGDSSPSSSSTPASGCSSPNDSEHGPNPILGSEALLGQRLRLQETSVAPFALPTVSLLPAITLGLPAPARADSDRRTHPTLGPRGPILGSPHTPLFLPHGLEPEAGGTLPSRLQPILLLDPSGSHAPLLTVPGLGPLPFHFAQSLMTTERLSGSGLHWPLSRTRSEPLPPSATAPPPPGPMQPRLEQLKTHVQVIKRSAKPSEKPRLRQIPSAEDLETDGGGPGQVVDDGLEHRELGHGQPEARGPAPLQQHPQVLLWEQQRLAGRLPRGSTGDTVLLPLAQGGHRPLSRAQSSPAAPASLSAPEPASQARVLSSSETPARTLPFTTGLIYDSVMLKHQCSCGDNSRHPEHAGRIQSIWSRLQERGLRSQCECLRGRKASLEELQSVHSERHVLLYGTNPLSRLKLDNGKLAGLLAQRMFVMLPCGGVGVDTDTIWNELHSSNAARWAAGSVTDLAFKVASRELKNGFAVVRPPGHHADHSTAMGFCFFNSVAIACRQLQQQSKASKILIVDWDVHHGNGTQQTFYQDPSVLYISLHRHDDGNFFPGSGAVDEVGAGSGEGFNVNVAWAGGLDPPMGDPEYLAAFRIVVMPIAREFSPDLVLVSAGFDAAEGHPAPLGGYHVSAKCFGYMTQQLMNLAGGAVVLALEGGHDLTAICDASEACVAALLGNRVDPLSEEGWKQKPNLNAIRSLEAVIRVHSKYWGCMQRLASCPDSWVPRVPGADKEEVEAVTALASLSVGILAEDRPSEQLVEEEEPMNL 3ZNS,3ZNR,3C10,3C0Z,3C0Y Histone deacetylase 7 HDAC7_HUMAN Q8WUI4 B3KY08 B4DWI0 B4E0Q5 Q6P1W9 Q6W9G7 Q7Z4K2 Q7Z5I1 Q96K01 Q9BR73 Q9H7L0 Q9NW41 Q9NWA9 Q9NYK9 Q9UFU7 51590146 CCCCNNC(=O)c1ccc(Br)cc1 InChI=1S/C11H15BrN2O/c1-2-3-8-13-14-11(15)9-4-6-10(12)7-5-9/h4-7,13H,2-3,8H2,1H3,(H,14,15) BVQCFCYPFJOOAV-UHFFFAOYSA-N 163619 UF010::US10807944, Compound UF010::US11731934, Compound UF010 Histone deacetylase 9 Homo sapiens >100000 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=163619 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6112&target=Histone+deacetylase+9&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=163619&enzyme=Histone+deacetylase+9&column=ki&startPg=0&Increment=50&submit=Search 4596836 310305336 1 MHSMISSVDVKSEVPVGLEPISPLDLRTDLRMMMPVVDPVVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHIKELLAIKQQQELLEKEQKLEQQRQEQEVERHRREQQLPPLRGKDRGRERAVASTEVKQKLQEFLLSKSATKDTPTNGKNHSVSRHPKLWYTAAHHTSLDQSSPPLSGTSPSYKYTLPGAQDAKDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGNVVTSFKKRMFEVTESSVSSSSPGSGPSSPNNGPTGSVTENETSVLPPTPHAEQMVSQQRILIHEDSMNLLSLYTSPSLPNITLGLPAVPSQLNASNSLKEKQKCETQTLRQGVPLPGQYGGSIPASSSHPHVTLEGKPPNSSHQALLQHLLLKEQMRQQKLLVAGGVPLHPQSPLATKERISPGIRGTHKLPRHRPLNRTQSAPLPQSTLAQLVIQQQHQQFLEKQKQYQQQIHMNKLLSKSIEQLKQPGSHLEEAEEELQGDQAMQEDRAPSSGNSTRSDSSACVDDTLGQVGAVKVKEEPVDSDEDAQIQEMESGEQAAFMQQPFLEPTHTRALSVRQAPLAAVGMDGLEKHRLVSRTHSSPAASVLPHPAMDRPLQPGSATGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPLDGQKLDPRILLGDDSQKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMGFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGTGLGEGYNINIAWTGGLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLADGRVVLALEGGHDLTAICDASEACVNALLGNELEPLAEDILHQSPNMNAVISLQKIIEIQSMSLKFS Histone deacetylase 9 HDAC9_HUMAN Q9UKV0 A7E2F3 B7Z4I4 B7Z917 B7Z928 B7Z940 C9JS87 E7EX34 F8W9E0 O94845 O95028 Q2M2R6 Q86SL1 Q86US3 51590147 CCCCCCCCCCCCCCCCNNC(=O)c1ccc(N(C)C)cc1 InChI=1S/C25H45N3O/c1-4-5-6-7-8-9-10-11-12-13-14-15-16-17-22-26-27-25(29)23-18-20-24(21-19-23)28(2)3/h18-21,26H,4-17,22H2,1-3H3,(H,27,29) LHLVOYSHFAXCES-UHFFFAOYSA-N 50640299 CHEMBL5561545 Histone deacetylase 11 Human 910 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50640299 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2640&target=Histone+deacetylase+11&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50640299&enzyme=Histone+deacetylase+11&column=ki&startPg=0&Increment=50&submit=Search 177380564 519665703 1 MLHTTQLYQHVPETRWPIVYSPRYNITFMGLEKLHPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKWSFAVATITEIPPVIFLPNFLVQRKVLRPLRTQTGGTIMAGKLAVERGWAINVGGGFHHCSSDRGGGFCAYADITLAIKFLFERVEGISRATIIDLDAHQGNGHERDFMDDKRVYIMDVYNRHIYPGDRFAKQAIRRKVELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGIVKRDELVFRMVRGRRVPILMVTSGGYQKRTARIIADSILNLFGLGLIGPESPSVSAQNSDTPLLPPAVP Histone deacetylase 11 HDA11_HUMAN Q96DB2 B4DDK1 Q9H6I7 Q9H6X3 Q9NTC9 51590148 CCCCCCCCCCCCCCCCNNC(=O)c1cccs1 InChI=1S/C21H38N2OS/c1-2-3-4-5-6-7-8-9-10-11-12-13-14-15-18-22-23-21(24)20-17-16-19-25-20/h16-17,19,22H,2-15,18H2,1H3,(H,23,24) HSHXDCVZWHOWCS-UHFFFAOYSA-N 50565135 CHEMBL4777961 Histone deacetylase 11 Homo sapiens 830 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50565135 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=2640&target=Histone+deacetylase+11&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50565135&enzyme=Histone+deacetylase+11&column=ki&startPg=0&Increment=50&submit=Search 139035087 461685473 1 MLHTTQLYQHVPETRWPIVYSPRYNITFMGLEKLHPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKWSFAVATITEIPPVIFLPNFLVQRKVLRPLRTQTGGTIMAGKLAVERGWAINVGGGFHHCSSDRGGGFCAYADITLAIKFLFERVEGISRATIIDLDAHQGNGHERDFMDDKRVYIMDVYNRHIYPGDRFAKQAIRRKVELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGIVKRDELVFRMVRGRRVPILMVTSGGYQKRTARIIADSILNLFGLGLIGPESPSVSAQNSDTPLLPPAVP Histone deacetylase 11 HDA11_HUMAN Q96DB2 B4DDK1 Q9H6I7 Q9H6X3 Q9NTC9 51590149 CCCCNNC(=O)c1ccc(cc1)N(C)C InChI=1S/C13H21N3O/c1-4-5-10-14-15-13(17)11-6-8-12(9-7-11)16(2)3/h6-9,14H,4-5,10H2,1-3H3,(H,15,17) GBPRHUHCZVADPX-UHFFFAOYSA-N 163624 SR-3208::US10807944, Compound RLS2-131::US11731934, Compound RLS2-131 Histone deacetylase 1 Homo sapiens 230 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=163624 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=163624&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 71306440 310305341 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 9R4I,8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51590150 CCCCNNC(=O)c1ccc(cc1)N(C)C InChI=1S/C13H21N3O/c1-4-5-10-14-15-13(17)11-6-8-12(9-7-11)16(2)3/h6-9,14H,4-5,10H2,1-3H3,(H,15,17) GBPRHUHCZVADPX-UHFFFAOYSA-N 163624 SR-3208::US10807944, Compound RLS2-131::US11731934, Compound RLS2-131 Histone deacetylase 2 Homo sapiens 880 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=163624 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=163624&enzyme=Histone+deacetylase+2&column=ki&startPg=0&Increment=50&submit=Search 71306440 310305341 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 51590151 CCCCNNC(=O)c1ccc(cc1)N(C)C InChI=1S/C13H21N3O/c1-4-5-10-14-15-13(17)11-6-8-12(9-7-11)16(2)3/h6-9,14H,4-5,10H2,1-3H3,(H,15,17) GBPRHUHCZVADPX-UHFFFAOYSA-N 163624 SR-3208::US10807944, Compound RLS2-131::US11731934, Compound RLS2-131 Histone deacetylase 3 Homo sapiens 120 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=163624 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1995&target=Histone+deacetylase+3&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=163624&enzyme=Histone+deacetylase+3&column=ki&startPg=0&Increment=50&submit=Search 71306440 310305341 1 MAKTVAYFYDPDVGNFHYGAGHPMKPHRLALTHSLVLHYGLYKKMIVFKPYQASQHDMCRFHSEDYIDFLQRVSPTNMQGFTKSLNAFNVGDDCPVFPGLFEFCSRYTGASLQGATQLNNKICDIAINWAGGLHHAKKFEASGFCYVNDIVIGILELLKYHPRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYKHLFQPVINQVVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEYVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVEEAISEELPYSEYFEYFAPDFTLHPDVSTRIENQNSRQYLDQIRQTIFENLKMLNHAPSVQIHDVPADLLTYDRTDEADAEERGPEENYSRPEAPNEFYDGDHDNDKESDVEI 4A69 Histone deacetylase 3 HDAC3_HUMAN O15379 D3DQE1 O43268 Q9UEI5 Q9UEV0 51590152 CCCC(CCC)C(=O)N[C@@H](Cc1ccccc1)C(=O)NNc1ccccc1 InChI=1S/C23H31N3O2/c1-3-11-19(12-4-2)22(27)24-21(17-18-13-7-5-8-14-18)23(28)26-25-20-15-9-6-10-16-20/h5-10,13-16,19,21,25H,3-4,11-12,17H2,1-2H3,(H,24,27)(H,26,28) PTFFMSKYSLJXBT-UHFFFAOYSA-N 50640300 CHEMBL5568268 Histone deacetylase 1 Human 390 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50640300 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=50640300&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 177380565 519665704 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51590153 CCCC(CCC)C(=O)O InChI=1S/C8H16O2/c1-3-5-7(6-4-2)8(9)10/h7H,3-6H2,1-2H3,(H,9,10) NIJJYAXOARWZEE-UHFFFAOYSA-N 50003616 Valproinsaeure::dipropylacetic acid::Di-n-propylessigsaeure::DPA::n-DPA::2-n-propyl-n-valeric acid::CHEMBL109::VALPROIC ACID Histone deacetylase 1 Homo sapiens 39000 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50003616 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=50003616&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 2PP 1DIT 3121 103917584 CHEMBL109 DB00313 C07185 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 9R4I,8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51590154 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 44 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa 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 51590155 CCCNNC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C17H27N3O2/c1-2-14-18-20-17(22)13-9-4-3-8-12-16(21)19-15-10-6-5-7-11-15/h5-7,10-11,18H,2-4,8-9,12-14H2,1H3,(H,19,21)(H,20,22) QDBUPYIRFBUJSV-UHFFFAOYSA-N 50595204 CHEMBL4451085 Histone deacetylase 1 Homo sapiens 45 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50595204 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=50595204&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 155521561 482606056 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 9R4I,8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51590156 CCCNNC(=O)c1ccc(Nc2nccc(N(C)c3ccc4c(C)n(C)cc4c3)n2)cc1 InChI=1S/C25H29N7O/c1-5-13-27-30-24(33)18-6-8-20(9-7-18)28-25-26-14-12-23(29-25)32(4)21-10-11-22-17(2)31(3)16-19(22)15-21/h6-12,14-16,27H,5,13H2,1-4H3,(H,30,33)(H,26,28,29) QIAFMKQJWAZOHG-UHFFFAOYSA-N 50640301 CHEMBL5565952 Histone deacetylase 1 Human 0.420000 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50640301 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=50640301&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 177380566 519665705 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51590157 CCCC(CCC)C(=O)N[C@@H](Cc1ccccc1)C(=O)NNc1ccccc1 InChI=1S/C23H31N3O2/c1-3-11-19(12-4-2)22(27)24-21(17-18-13-7-5-8-14-18)23(28)26-25-20-15-9-6-10-16-20/h5-10,13-16,19,21,25H,3-4,11-12,17H2,1-2H3,(H,24,27)(H,26,28) PTFFMSKYSLJXBT-UHFFFAOYSA-N 50640300 CHEMBL5568268 Histone deacetylase 2 Human 2020 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50640300 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=50640300&enzyme=Histone+deacetylase+2&column=ki&startPg=0&Increment=50&submit=Search 177380565 519665704 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 51590158 CCCC(CCC)C(=O)O InChI=1S/C8H16O2/c1-3-5-7(6-4-2)8(9)10/h7H,3-6H2,1-2H3,(H,9,10) NIJJYAXOARWZEE-UHFFFAOYSA-N 50003616 Valproinsaeure::dipropylacetic acid::Di-n-propylessigsaeure::DPA::n-DPA::2-n-propyl-n-valeric acid::CHEMBL109::VALPROIC ACID Histone deacetylase 2 Homo sapiens 62000 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50003616 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=50003616&enzyme=Histone+deacetylase+2&column=ki&startPg=0&Increment=50&submit=Search 2PP 1DIT 3121 103917584 CHEMBL109 DB00313 C07185 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 51590159 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 89 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa 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 51590160 CCCNNC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C17H27N3O2/c1-2-14-18-20-17(22)13-9-4-3-8-12-16(21)19-15-10-6-5-7-11-15/h5-7,10-11,18H,2-4,8-9,12-14H2,1H3,(H,19,21)(H,20,22) QDBUPYIRFBUJSV-UHFFFAOYSA-N 50595204 CHEMBL4451085 Histone deacetylase 2 Homo sapiens 125 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50595204 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=50595204&enzyme=Histone+deacetylase+2&column=ki&startPg=0&Increment=50&submit=Search 155521561 482606056 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 51590161 CCCC(CCC)C(=O)N[C@@H](Cc1ccccc1)C(=O)NNc1ccccc1 InChI=1S/C23H31N3O2/c1-3-11-19(12-4-2)22(27)24-21(17-18-13-7-5-8-14-18)23(28)26-25-20-15-9-6-10-16-20/h5-10,13-16,19,21,25H,3-4,11-12,17H2,1-2H3,(H,24,27)(H,26,28) PTFFMSKYSLJXBT-UHFFFAOYSA-N 50640300 CHEMBL5568268 Histone deacetylase 3 Human 1490 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50640300 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1995&target=Histone+deacetylase+3&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50640300&enzyme=Histone+deacetylase+3&column=ki&startPg=0&Increment=50&submit=Search 177380565 519665704 1 MAKTVAYFYDPDVGNFHYGAGHPMKPHRLALTHSLVLHYGLYKKMIVFKPYQASQHDMCRFHSEDYIDFLQRVSPTNMQGFTKSLNAFNVGDDCPVFPGLFEFCSRYTGASLQGATQLNNKICDIAINWAGGLHHAKKFEASGFCYVNDIVIGILELLKYHPRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYKHLFQPVINQVVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEYVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVEEAISEELPYSEYFEYFAPDFTLHPDVSTRIENQNSRQYLDQIRQTIFENLKMLNHAPSVQIHDVPADLLTYDRTDEADAEERGPEENYSRPEAPNEFYDGDHDNDKESDVEI 4A69 Histone deacetylase 3 HDAC3_HUMAN O15379 D3DQE1 O43268 Q9UEI5 Q9UEV0 51590162 CCCC(CCC)C(=O)O InChI=1S/C8H16O2/c1-3-5-7(6-4-2)8(9)10/h7H,3-6H2,1-2H3,(H,9,10) NIJJYAXOARWZEE-UHFFFAOYSA-N 50003616 Valproinsaeure::dipropylacetic acid::Di-n-propylessigsaeure::DPA::n-DPA::2-n-propyl-n-valeric acid::CHEMBL109::VALPROIC ACID Histone deacetylase 3 Homo sapiens 161000 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50003616 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1995&target=Histone+deacetylase+3&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50003616&enzyme=Histone+deacetylase+3&column=ki&startPg=0&Increment=50&submit=Search 2PP 1DIT 3121 103917584 CHEMBL109 DB00313 C07185 1 MAKTVAYFYDPDVGNFHYGAGHPMKPHRLALTHSLVLHYGLYKKMIVFKPYQASQHDMCRFHSEDYIDFLQRVSPTNMQGFTKSLNAFNVGDDCPVFPGLFEFCSRYTGASLQGATQLNNKICDIAINWAGGLHHAKKFEASGFCYVNDIVIGILELLKYHPRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYKHLFQPVINQVVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEYVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVEEAISEELPYSEYFEYFAPDFTLHPDVSTRIENQNSRQYLDQIRQTIFENLKMLNHAPSVQIHDVPADLLTYDRTDEADAEERGPEENYSRPEAPNEFYDGDHDNDKESDVEI 4A69 Histone deacetylase 3 HDAC3_HUMAN O15379 D3DQE1 O43268 Q9UEI5 Q9UEV0 51590163 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 3 Homo sapiens 145 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa 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=1995&target=Histone+deacetylase+3&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=19149&enzyme=Histone+deacetylase+3&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 MAKTVAYFYDPDVGNFHYGAGHPMKPHRLALTHSLVLHYGLYKKMIVFKPYQASQHDMCRFHSEDYIDFLQRVSPTNMQGFTKSLNAFNVGDDCPVFPGLFEFCSRYTGASLQGATQLNNKICDIAINWAGGLHHAKKFEASGFCYVNDIVIGILELLKYHPRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYKHLFQPVINQVVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEYVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVEEAISEELPYSEYFEYFAPDFTLHPDVSTRIENQNSRQYLDQIRQTIFENLKMLNHAPSVQIHDVPADLLTYDRTDEADAEERGPEENYSRPEAPNEFYDGDHDNDKESDVEI 4A69 Histone deacetylase 3 HDAC3_HUMAN O15379 D3DQE1 O43268 Q9UEI5 Q9UEV0 51590164 CCCNNC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C17H27N3O2/c1-2-14-18-20-17(22)13-9-4-3-8-12-16(21)19-15-10-6-5-7-11-15/h5-7,10-11,18H,2-4,8-9,12-14H2,1H3,(H,19,21)(H,20,22) QDBUPYIRFBUJSV-UHFFFAOYSA-N 50595204 CHEMBL4451085 Histone deacetylase 3 Homo sapiens 20 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50595204 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1995&target=Histone+deacetylase+3&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50595204&enzyme=Histone+deacetylase+3&column=ki&startPg=0&Increment=50&submit=Search 155521561 482606056 1 MAKTVAYFYDPDVGNFHYGAGHPMKPHRLALTHSLVLHYGLYKKMIVFKPYQASQHDMCRFHSEDYIDFLQRVSPTNMQGFTKSLNAFNVGDDCPVFPGLFEFCSRYTGASLQGATQLNNKICDIAINWAGGLHHAKKFEASGFCYVNDIVIGILELLKYHPRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYKHLFQPVINQVVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEYVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVEEAISEELPYSEYFEYFAPDFTLHPDVSTRIENQNSRQYLDQIRQTIFENLKMLNHAPSVQIHDVPADLLTYDRTDEADAEERGPEENYSRPEAPNEFYDGDHDNDKESDVEI 4A69 Histone deacetylase 3 HDAC3_HUMAN O15379 D3DQE1 O43268 Q9UEI5 Q9UEV0 51590165 CCCC(CCC)C(=O)N[C@@H](Cc1ccccc1)C(=O)NNc1ccccc1 InChI=1S/C23H31N3O2/c1-3-11-19(12-4-2)22(27)24-21(17-18-13-7-5-8-14-18)23(28)26-25-20-15-9-6-10-16-20/h5-10,13-16,19,21,25H,3-4,11-12,17H2,1-2H3,(H,24,27)(H,26,28) PTFFMSKYSLJXBT-UHFFFAOYSA-N 50640300 CHEMBL5568268 Histone deacetylase 8 Human 1540 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50640300 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1996&target=Histone+deacetylase+8&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50640300&enzyme=Histone+deacetylase+8&column=ki&startPg=0&Increment=50&submit=Search 177380565 519665704 1 MEEPEEPADSGQSLVPVYIYSPEYVSMCDSLAKIPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIEYGLGYDCPATEGIFDYAAAIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCRPDRNEPHRIQQILNYIKGNLKHVV 3SFH,3SFF,6ODC,6ODB,6ODA,5FCW,1W22,1VKG,1T69,1T67,1T64,3RQD,3MZ3,3F0R,3F07,5VI6 Histone deacetylase 8 HDAC8_HUMAN Q9BY41 A6ND12 A6ND61 A6NET3 A6NJR3 A8MQ62 B4DKN0 B4DV22 Q86VC8 Q9NP76 Q9NYH4 51590166 CCCC(CCC)C(=O)O InChI=1S/C8H16O2/c1-3-5-7(6-4-2)8(9)10/h7H,3-6H2,1-2H3,(H,9,10) NIJJYAXOARWZEE-UHFFFAOYSA-N 50003616 Valproinsaeure::dipropylacetic acid::Di-n-propylessigsaeure::DPA::n-DPA::2-n-propyl-n-valeric acid::CHEMBL109::VALPROIC ACID Histone deacetylase 8 Homo sapiens >100000 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50003616 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1996&target=Histone+deacetylase+8&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50003616&enzyme=Histone+deacetylase+8&column=ki&startPg=0&Increment=50&submit=Search 2PP 1DIT 3121 103917584 CHEMBL109 DB00313 C07185 1 MEEPEEPADSGQSLVPVYIYSPEYVSMCDSLAKIPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIEYGLGYDCPATEGIFDYAAAIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCRPDRNEPHRIQQILNYIKGNLKHVV 3SFH,3SFF,6ODC,6ODB,6ODA,5FCW,1W22,1VKG,1T69,1T67,1T64,3RQD,3MZ3,3F0R,3F07,5VI6 Histone deacetylase 8 HDAC8_HUMAN Q9BY41 A6ND12 A6ND61 A6NET3 A6NJR3 A8MQ62 B4DKN0 B4DV22 Q86VC8 Q9NP76 Q9NYH4 51590167 CCCC(CCC)C(=O)N[C@@H](Cc1ccccc1)C(=O)NNc1ccccc1 InChI=1S/C23H31N3O2/c1-3-11-19(12-4-2)22(27)24-21(17-18-13-7-5-8-14-18)23(28)26-25-20-15-9-6-10-16-20/h5-10,13-16,19,21,25H,3-4,11-12,17H2,1-2H3,(H,24,27)(H,26,28) PTFFMSKYSLJXBT-UHFFFAOYSA-N 50640300 CHEMBL5568268 Histone deacetylase 4 Human 3180 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50640300 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50640300&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 177380565 519665704 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51590168 CCCC(CCC)C(=O)O InChI=1S/C8H16O2/c1-3-5-7(6-4-2)8(9)10/h7H,3-6H2,1-2H3,(H,9,10) NIJJYAXOARWZEE-UHFFFAOYSA-N 50003616 Valproinsaeure::dipropylacetic acid::Di-n-propylessigsaeure::DPA::n-DPA::2-n-propyl-n-valeric acid::CHEMBL109::VALPROIC ACID Histone deacetylase 4 Homo sapiens >100000 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50003616 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=6107&target=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50003616&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 2PP 1DIT 3121 103917584 CHEMBL109 DB00313 C07185 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51590169 CCCNNC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C17H27N3O2/c1-2-14-18-20-17(22)13-9-4-3-8-12-16(21)19-15-10-6-5-7-11-15/h5-7,10-11,18H,2-4,8-9,12-14H2,1H3,(H,19,21)(H,20,22) QDBUPYIRFBUJSV-UHFFFAOYSA-N 50595204 CHEMBL4451085 Histone deacetylase 1 Homo sapiens 828 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50595204 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=50595204&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 155521561 482606056 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 9R4I,8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51590170 CCCNNC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C17H27N3O2/c1-2-14-18-20-17(22)13-9-4-3-8-12-16(21)19-15-10-6-5-7-11-15/h5-7,10-11,18H,2-4,8-9,12-14H2,1H3,(H,19,21)(H,20,22) QDBUPYIRFBUJSV-UHFFFAOYSA-N 50595204 CHEMBL4451085 Histone deacetylase 2 Homo sapiens 530 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50595204 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=50595204&enzyme=Histone+deacetylase+2&column=ki&startPg=0&Increment=50&submit=Search 155521561 482606056 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 51590171 CCCNNC(=O)CCCCCCC(=O)Nc1ccccc1 InChI=1S/C17H27N3O2/c1-2-14-18-20-17(22)13-9-4-3-8-12-16(21)19-15-10-6-5-7-11-15/h5-7,10-11,18H,2-4,8-9,12-14H2,1H3,(H,19,21)(H,20,22) QDBUPYIRFBUJSV-UHFFFAOYSA-N 50595204 CHEMBL4451085 Histone deacetylase 3 Homo sapiens 379 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50595204 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1995&target=Histone+deacetylase+3&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50595204&enzyme=Histone+deacetylase+3&column=ki&startPg=0&Increment=50&submit=Search 155521561 482606056 1 MAKTVAYFYDPDVGNFHYGAGHPMKPHRLALTHSLVLHYGLYKKMIVFKPYQASQHDMCRFHSEDYIDFLQRVSPTNMQGFTKSLNAFNVGDDCPVFPGLFEFCSRYTGASLQGATQLNNKICDIAINWAGGLHHAKKFEASGFCYVNDIVIGILELLKYHPRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYKHLFQPVINQVVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEYVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVEEAISEELPYSEYFEYFAPDFTLHPDVSTRIENQNSRQYLDQIRQTIFENLKMLNHAPSVQIHDVPADLLTYDRTDEADAEERGPEENYSRPEAPNEFYDGDHDNDKESDVEI 4A69 Histone deacetylase 3 HDAC3_HUMAN O15379 D3DQE1 O43268 Q9UEI5 Q9UEV0 51590172 CCCNNC(=O)c1ccc(Nc2nccc(N(C)c3ccc4c(C)n(C)cc4c3)n2)cc1 InChI=1S/C25H29N7O/c1-5-13-27-30-24(33)18-6-8-20(9-7-18)28-25-26-14-12-23(29-25)32(4)21-10-11-22-17(2)31(3)16-19(22)15-21/h6-12,14-16,27H,5,13H2,1-4H3,(H,30,33)(H,26,28,29) QIAFMKQJWAZOHG-UHFFFAOYSA-N 50640301 CHEMBL5565952 Histone deacetylase 6 Human 8960 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50640301 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=50640301&enzyme=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search 177380566 519665705 1 MTSTGQDSTTTRQRRSRQNPQSPPQDSSVTSKRNIKKGAVPRSIPNLAEVKKKGKMKKLGQAMEEDLIVGLQGMDLNLEAEALAGTGLVLDEQLNEFHCLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCRSAQASVSCALEALEPFWEVLVRSTETVERDNMEEDNVEESEEEGPWEPPVLPILTWPVLQSRTGLVYDQNMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQTISGHALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLSGALASITETIQVHRRYWRSLRVMKVEDREGPSSSKLVTKKAPQPAKPRLAERMTTREKKVLEAGMGKVTSASFGEESTPGQTNSETAVVALTQDQPSEAATGGATLAQTISEAAIGGAMLGQTTSEEAVGGATPDQTTSEETVGGAILDQTTSEDAVGGATLGQTTSEEAVGGATLAQTTSEAAMEGATLDQTTSEEAPGGTELIQTPLASSTDHQTPPTSPVQGTTPQISPSTLIGSLRTLELGSESQGASESQAPGEENLLGEAAGGQDMADSMLMQGSRGLTDQAIFYAVTPLPWCPHLVAVCPIPAAGLDVTQPCGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHGNSGHPLVLSYIDLSAWCYYCQAYVHHQALLDVKNIAHQNKFGEDMPHPH 5EDU,7ZYU,3PHD,3GV4 Protein deacetylase HDAC6 HDAC6_HUMAN Q9UBN7 O94975 Q6NT75 Q7L3E5 Q96CY0 51590173 NNC(=O)c1ccc(COc2ccccc2Cl)cc1 InChI=1S/C14H13ClN2O2/c15-12-3-1-2-4-13(12)19-9-10-5-7-11(8-6-10)14(18)17-16/h1-8H,9,16H2,(H,17,18) WWQCNJYMQZGQDG-UHFFFAOYSA-N 50640302 CHEMBL5557078 Histone deacetylase 6 Human 12800 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50640302 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=50640302&enzyme=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search 840755 519665706 1 MTSTGQDSTTTRQRRSRQNPQSPPQDSSVTSKRNIKKGAVPRSIPNLAEVKKKGKMKKLGQAMEEDLIVGLQGMDLNLEAEALAGTGLVLDEQLNEFHCLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCRSAQASVSCALEALEPFWEVLVRSTETVERDNMEEDNVEESEEEGPWEPPVLPILTWPVLQSRTGLVYDQNMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQTISGHALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLSGALASITETIQVHRRYWRSLRVMKVEDREGPSSSKLVTKKAPQPAKPRLAERMTTREKKVLEAGMGKVTSASFGEESTPGQTNSETAVVALTQDQPSEAATGGATLAQTISEAAIGGAMLGQTTSEEAVGGATPDQTTSEETVGGAILDQTTSEDAVGGATLGQTTSEEAVGGATLAQTTSEAAMEGATLDQTTSEEAPGGTELIQTPLASSTDHQTPPTSPVQGTTPQISPSTLIGSLRTLELGSESQGASESQAPGEENLLGEAAGGQDMADSMLMQGSRGLTDQAIFYAVTPLPWCPHLVAVCPIPAAGLDVTQPCGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHGNSGHPLVLSYIDLSAWCYYCQAYVHHQALLDVKNIAHQNKFGEDMPHPH 5EDU,7ZYU,3PHD,3GV4 Protein deacetylase HDAC6 HDAC6_HUMAN Q9UBN7 O94975 Q6NT75 Q7L3E5 Q96CY0 51590174 CN1CCN(CC1)NC(=O)c1cccc(c1)C(=O)NO InChI=1S/C13H18N4O3/c1-16-5-7-17(8-6-16)14-12(18)10-3-2-4-11(9-10)13(19)15-20/h2-4,9,20H,5-8H2,1H3,(H,14,18)(H,15,19) LLAPOEIECXFUIX-UHFFFAOYSA-N 50567342 CHEMBL4846377 Histone deacetylase 8 Schistosoma mansoni 750 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50567342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=50007090&target=Histone+deacetylase+8&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50567342&enzyme=Histone+deacetylase+8&column=ki&startPg=0&Increment=50&submit=Search 164609492 471057487 1 MSVGIVYGDQYRQLCCSSPKFGDRYALVMDLINAYKLIPELSRVPPLQWDSPSRMYEAVTAFHSTEYVDALKKLQMLHCEEKELTADDELLMDSFSLNYDCPGFPSVFDYSLAAVQGSLAAASALICRHCEVVINWGGGWHHAKRSEASGFCYLNDIVLAIHRLVSSTPPETSPNRQTRVLYVDLDLHHGDGVEEAFWYSPRVVTFSVHHASPGFFPGTGTWNMVDNDKLPIFLNGAGRGRFSAFNLPLEEGINDLDWSNAIGPILDSLNIVIQPSYVVVQCGADCLATDPHRIFRLTNFYPNLNLDSDCDSECSLSGYLYAIKKILSWKVPTLILGGGGYNFPDTARLWTRVTALTIEEVKGKKMTISPEIPEHSYFSRYGPDFELDIDYFPHESHNKTLDSIQKHHRRILEQLRNYADLNKLIYDYDQVYQLYNLTGM 7P3S,6TLD,6HU3,6HU2,6HU1,6HU0,6HTZ,6HTT,6HTI,6HTH,6HTG,6HT8,6HSZ,6HSH,6HRQ,6HQY,6GXW,6GXU,6GXA,6GX3,6FU1,5FUE,4CQF,4BZ9,4BZ8,4BZ7,4BZ6,4BZ5 histone deacetylase A5H660_SCHMA A5H660 51590175 CN1CCN(CC1)NC(=O)c1cccc(c1)C(=O)NO InChI=1S/C13H18N4O3/c1-16-5-7-17(8-6-16)14-12(18)10-3-2-4-11(9-10)13(19)15-20/h2-4,9,20H,5-8H2,1H3,(H,14,18)(H,15,19) LLAPOEIECXFUIX-UHFFFAOYSA-N 50567342 CHEMBL4846377 Histone deacetylase 8 Homo sapiens 1310 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50567342 http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=pol&polymerid=1996&target=Histone+deacetylase+8&column=ki&startPg=0&Increment=50&submit=Search http://www.bindingdb.org/rwd/jsp/dbsearch/PrimarySearch_ki.jsp?energyterm=kJ/mole&tag=r21&monomerid=50567342&enzyme=Histone+deacetylase+8&column=ki&startPg=0&Increment=50&submit=Search 164609492 471057487 1 MEEPEEPADSGQSLVPVYIYSPEYVSMCDSLAKIPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIEYGLGYDCPATEGIFDYAAAIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCRPDRNEPHRIQQILNYIKGNLKHVV 3SFH,3SFF,6ODC,6ODB,6ODA,5FCW,1W22,1VKG,1T69,1T67,1T64,3RQD,3MZ3,3F0R,3F07,5VI6 Histone deacetylase 8 HDAC8_HUMAN Q9BY41 A6ND12 A6ND61 A6NET3 A6NJR3 A8MQ62 B4DKN0 B4DV22 Q86VC8 Q9NP76 Q9NYH4 51590176 CN1CCN(CC1)NC(=O)c1cccc(c1)C(=O)NO InChI=1S/C13H18N4O3/c1-16-5-7-17(8-6-16)14-12(18)10-3-2-4-11(9-10)13(19)15-20/h2-4,9,20H,5-8H2,1H3,(H,14,18)(H,15,19) LLAPOEIECXFUIX-UHFFFAOYSA-N 50567342 CHEMBL4846377 Histone deacetylase 6 Homo sapiens 7110 ChEMBL 10.7270/Q2VT1XQM 39092855 Carreiras, MDC; Marco-Contelles, J //0 10/11/2025 Universidade de Lisboa http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50567342 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=50567342&enzyme=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search 164609492 471057487 1 MTSTGQDSTTTRQRRSRQNPQSPPQDSSVTSKRNIKKGAVPRSIPNLAEVKKKGKMKKLGQAMEEDLIVGLQGMDLNLEAEALAGTGLVLDEQLNEFHCLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCRSAQASVSCALEALEPFWEVLVRSTETVERDNMEEDNVEESEEEGPWEPPVLPILTWPVLQSRTGLVYDQNMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQTISGHALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLSGALASITETIQVHRRYWRSLRVMKVEDREGPSSSKLVTKKAPQPAKPRLAERMTTREKKVLEAGMGKVTSASFGEESTPGQTNSETAVVALTQDQPSEAATGGATLAQTISEAAIGGAMLGQTTSEEAVGGATPDQTTSEETVGGAILDQTTSEDAVGGATLGQTTSEEAVGGATLAQTTSEAAMEGATLDQTTSEEAPGGTELIQTPLASSTDHQTPPTSPVQGTTPQISPSTLIGSLRTLELGSESQGASESQAPGEENLLGEAAGGQDMADSMLMQGSRGLTDQAIFYAVTPLPWCPHLVAVCPIPAAGLDVTQPCGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHGNSGHPLVLSYIDLSAWCYYCQAYVHHQALLDVKNIAHQNKFGEDMPHPH 5EDU,7ZYU,3PHD,3GV4 Protein deacetylase HDAC6 HDAC6_HUMAN Q9UBN7 O94975 Q6NT75 Q7L3E5 Q96CY0