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 51584627 O=C(CCCN1C(=O)C/C(=C\c2ccccc2)C1=O)NO InChI=1S/C15H16N2O4/c18-13(16-21)7-4-8-17-14(19)10-12(15(17)20)9-11-5-2-1-3-6-11/h1-3,5-6,9,21H,4,7-8,10H2,(H,16,18) ATFSHRCFTWALEY-UHFFFAOYSA-N 50637767 CHEMBL5548853 Histone deacetylase 1 Human 182 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637767 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=50637767&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 169092120 519658170 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51584628 O=C(CCCCN1C(=O)C/C(=C\c2ccccc2)C1=O)NO InChI=1S/C16H18N2O4/c19-14(17-22)8-4-5-9-18-15(20)11-13(16(18)21)10-12-6-2-1-3-7-12/h1-3,6-7,10,22H,4-5,8-9,11H2,(H,17,19) LFIVRUCYCAABRJ-UHFFFAOYSA-N 50637768 CHEMBL5556089 Histone deacetylase 1 Human 136 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637768 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=50637768&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 169092111 519658171 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51584629 O=C(CCCCCN1C(=O)C/C(=C\c2ccccc2)C1=O)NO InChI=1S/C17H20N2O4/c20-15(18-23)9-5-2-6-10-19-16(21)12-14(17(19)22)11-13-7-3-1-4-8-13/h1,3-4,7-8,11,23H,2,5-6,9-10,12H2,(H,18,20) NWZJVULBGFNRLY-UHFFFAOYSA-N 50637769 CHEMBL5558731 Histone deacetylase 1 Human 32 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637769 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=50637769&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 169092060 519658172 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51584630 O=C(CCCCCCN1C(=O)C/C(=C\c2ccccc2)C1=O)NO InChI=1S/C18H22N2O4/c21-16(19-24)10-6-1-2-7-11-20-17(22)13-15(18(20)23)12-14-8-4-3-5-9-14/h3-5,8-9,12,24H,1-2,6-7,10-11,13H2,(H,19,21) AHFRWYPXGQTKKY-UHFFFAOYSA-N 50637770 CHEMBL5560673 Histone deacetylase 1 Human 13 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637770 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=50637770&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 169092108 519658173 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51584631 O=C(CCCCCCCN1C(=O)C/C(=C\c2ccccc2)C1=O)NO InChI=1S/C19H24N2O4/c22-17(20-25)11-7-2-1-3-8-12-21-18(23)14-16(19(21)24)13-15-9-5-4-6-10-15/h4-6,9-10,13,25H,1-3,7-8,11-12,14H2,(H,20,22) IKXZLNQXTYYDCI-UHFFFAOYSA-N 50637771 CHEMBL5558617 Histone deacetylase 1 Human 25 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637771 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=50637771&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 177375521 519658174 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51584632 O=C(NO)c1ccc(CN2C(=O)C/C(=C\c3ccccc3)C2=O)cc1 InChI=1S/C19H16N2O4/c22-17-11-16(10-13-4-2-1-3-5-13)19(24)21(17)12-14-6-8-15(9-7-14)18(23)20-25/h1-10,25H,11-12H2,(H,20,23) SPJDDUDXKSJEBC-UHFFFAOYSA-N 50637772 CHEMBL5563723 Histone deacetylase 1 Human 33 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637772 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=50637772&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 169092123 519658175 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51584633 Nc1cc(F)ccc1NC(=O)CCCN1C(=O)C/C(=C\c2ccccc2)C1=O InChI=1S/C21H20FN3O3/c22-16-8-9-18(17(23)13-16)24-19(26)7-4-10-25-20(27)12-15(21(25)28)11-14-5-2-1-3-6-14/h1-3,5-6,8-9,11,13H,4,7,10,12,23H2,(H,24,26) KSVOKZBTNQEFMV-UHFFFAOYSA-N 50637773 CHEMBL5560916 Histone deacetylase 1 Human 231 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637773 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=50637773&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 169092106 519658176 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51584634 Nc1cc(F)ccc1NC(=O)CCCCN1C(=O)C/C(=C\c2ccccc2)C1=O InChI=1S/C22H22FN3O3/c23-17-9-10-19(18(24)14-17)25-20(27)8-4-5-11-26-21(28)13-16(22(26)29)12-15-6-2-1-3-7-15/h1-3,6-7,9-10,12,14H,4-5,8,11,13,24H2,(H,25,27) RFAQCOWVLBCWRX-UHFFFAOYSA-N 50637774 CHEMBL5556211 Histone deacetylase 1 Human 173 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637774 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=50637774&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 176235491 519658177 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51584635 Nc1cc(F)ccc1NC(=O)CCCCCN1C(=O)C/C(=C\c2ccccc2)C1=O InChI=1S/C23H24FN3O3/c24-18-10-11-20(19(25)15-18)26-21(28)9-5-2-6-12-27-22(29)14-17(23(27)30)13-16-7-3-1-4-8-16/h1,3-4,7-8,10-11,13,15H,2,5-6,9,12,14,25H2,(H,26,28) GVFGZVDPOQAIEH-UHFFFAOYSA-N 50637775 CHEMBL5527988 Histone deacetylase 1 Human 105 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637775 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=50637775&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 169092057 519658178 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51584636 Nc1cc(F)ccc1NC(=O)CCCCCCN1C(=O)C/C(=C\c2ccccc2)C1=O InChI=1S/C24H26FN3O3/c25-19-11-12-21(20(26)16-19)27-22(29)10-6-1-2-7-13-28-23(30)15-18(24(28)31)14-17-8-4-3-5-9-17/h3-5,8-9,11-12,14,16H,1-2,6-7,10,13,15,26H2,(H,27,29) UZDGNSLKFDQOKZ-UHFFFAOYSA-N 50637776 CHEMBL5562110 Histone deacetylase 1 Human 144 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637776 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=50637776&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 169092072 519658179 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51584637 CC(C)c1ccc(/C=C2\CC(=O)N(CCCCCCC(=O)NO)C2=O)cc1 InChI=1S/C21H28N2O4/c1-15(2)17-10-8-16(9-11-17)13-18-14-20(25)23(21(18)26)12-6-4-3-5-7-19(24)22-27/h8-11,13,15,27H,3-7,12,14H2,1-2H3,(H,22,24) NKHSXSJACURIAJ-UHFFFAOYSA-N 50637777 CHEMBL5559591 Histone deacetylase 1 Human 29 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637777 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=50637777&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 169092080 519658180 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51584638 CN(C)c1ccc(/C=C2\CC(=O)N(CCCCCCC(=O)NO)C2=O)cc1 InChI=1S/C20H27N3O4/c1-22(2)17-10-8-15(9-11-17)13-16-14-19(25)23(20(16)26)12-6-4-3-5-7-18(24)21-27/h8-11,13,27H,3-7,12,14H2,1-2H3,(H,21,24) RQPLGBGTFISBSA-UHFFFAOYSA-N 50637778 CHEMBL5566842 Histone deacetylase 1 Human 27 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637778 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=50637778&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 169092065 519658181 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51584639 O=C(CCCCCCN1C(=O)C/C(=C\c2ccc(C(F)(F)F)cc2)C1=O)NO InChI=1S/C19H21F3N2O4/c20-19(21,22)15-8-6-13(7-9-15)11-14-12-17(26)24(18(14)27)10-4-2-1-3-5-16(25)23-28/h6-9,11,28H,1-5,10,12H2,(H,23,25) RWVYOOGEJQIBOP-UHFFFAOYSA-N 50637779 CHEMBL5555580 Histone deacetylase 1 Human 34 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637779 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=50637779&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 169092071 519658182 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51584640 Cc1ccc(/C=C2\CC(=O)N(CCCCCCC(=O)NO)C2=O)cc1 InChI=1S/C19H24N2O4/c1-14-7-9-15(10-8-14)12-16-13-18(23)21(19(16)24)11-5-3-2-4-6-17(22)20-25/h7-10,12,25H,2-6,11,13H2,1H3,(H,20,22) MBZUWHZKVVZPHX-UHFFFAOYSA-N 50637780 CHEMBL5557847 Histone deacetylase 1 Human 26 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637780 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=50637780&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 169092102 519658183 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51584641 Cc1ccccc1/C=C1\CC(=O)N(CCCCCCC(=O)NO)C1=O InChI=1S/C19H24N2O4/c1-14-8-5-6-9-15(14)12-16-13-18(23)21(19(16)24)11-7-3-2-4-10-17(22)20-25/h5-6,8-9,12,25H,2-4,7,10-11,13H2,1H3,(H,20,22) KUUMXMNKHHTLBZ-UHFFFAOYSA-N 50637781 CHEMBL5561907 Histone deacetylase 1 Human 22 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637781 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=50637781&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 169092121 519658184 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51584642 N#Cc1ccccc1/C=C1\CC(=O)N(CCCCCCC(=O)NO)C1=O InChI=1S/C19H21N3O4/c20-13-15-8-5-4-7-14(15)11-16-12-18(24)22(19(16)25)10-6-2-1-3-9-17(23)21-26/h4-5,7-8,11,26H,1-3,6,9-10,12H2,(H,21,23) ALTHDBDXVKUOLS-UHFFFAOYSA-N 50637782 CHEMBL5563656 Histone deacetylase 1 Human 40 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637782 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=50637782&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 169092115 519658185 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51584643 O=C(CCCCCCN1C(=O)C/C(=C\c2cccs2)C1=O)NO InChI=1S/C16H20N2O4S/c19-14(17-22)7-3-1-2-4-8-18-15(20)11-12(16(18)21)10-13-6-5-9-23-13/h5-6,9-10,22H,1-4,7-8,11H2,(H,17,19) QTVQDIBSOXHIPS-UHFFFAOYSA-N 50637783 CHEMBL5559467 Histone deacetylase 1 Human 25 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637783 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=50637783&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 177375522 519658186 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51584644 O=C(CCCCCCN1C(=O)C/C(=C\c2ccccc2Cl)C1=O)NO InChI=1S/C18H21ClN2O4/c19-15-8-5-4-7-13(15)11-14-12-17(23)21(18(14)24)10-6-2-1-3-9-16(22)20-25/h4-5,7-8,11,25H,1-3,6,9-10,12H2,(H,20,22) LOZPGNPVVHLMMZ-UHFFFAOYSA-N 50637784 CHEMBL5559632 Histone deacetylase 1 Human 19 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637784 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=50637784&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 169092073 519658187 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51584645 O=C(CCCCCCN1C(=O)C/C(=C\c2cccc(Cl)c2)C1=O)NO InChI=1S/C18H21ClN2O4/c19-15-7-5-6-13(11-15)10-14-12-17(23)21(18(14)24)9-4-2-1-3-8-16(22)20-25/h5-7,10-11,25H,1-4,8-9,12H2,(H,20,22) PZHJFCSWCOJMME-UHFFFAOYSA-N 50637785 CHEMBL5557863 Histone deacetylase 1 Human 19 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637785 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=50637785&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 169092058 519658188 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51584646 O=C(CCCCCCN1C(=O)C/C(=C\c2ccc(Cl)cc2)C1=O)NO InChI=1S/C18H21ClN2O4/c19-15-8-6-13(7-9-15)11-14-12-17(23)21(18(14)24)10-4-2-1-3-5-16(22)20-25/h6-9,11,25H,1-5,10,12H2,(H,20,22) WORBBDXVHXXSJP-UHFFFAOYSA-N 50637786 CHEMBL5557149 Histone deacetylase 1 Human 23 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637786 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=50637786&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 169092089 519658189 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51584647 O=C(CCCCCCN1C(=O)C/C(=C\c2cccc(Br)c2)C1=O)NO InChI=1S/C18H21BrN2O4/c19-15-7-5-6-13(11-15)10-14-12-17(23)21(18(14)24)9-4-2-1-3-8-16(22)20-25/h5-7,10-11,25H,1-4,8-9,12H2,(H,20,22) KKFUSWGIJYOQOH-UHFFFAOYSA-N 50637787 CHEMBL5560794 Histone deacetylase 1 Human 19 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637787 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=50637787&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 169092090 519658190 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51584648 O=C(CCCCCCN1C(=O)C/C(=C\c2cccc(F)c2)C1=O)NO InChI=1S/C18H21FN2O4/c19-15-7-5-6-13(11-15)10-14-12-17(23)21(18(14)24)9-4-2-1-3-8-16(22)20-25/h5-7,10-11,25H,1-4,8-9,12H2,(H,20,22) FDHMBAWJZOHTFF-UHFFFAOYSA-N 50637788 CHEMBL5542593 Histone deacetylase 1 Human 75 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637788 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=50637788&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 169092110 519658191 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51584649 O=C(CCCCCCN1C(=O)C/C(=C\c2cccc(I)c2)C1=O)NO InChI=1S/C18H21IN2O4/c19-15-7-5-6-13(11-15)10-14-12-17(23)21(18(14)24)9-4-2-1-3-8-16(22)20-25/h5-7,10-11,25H,1-4,8-9,12H2,(H,20,22) TXJHSGLFCPRREA-UHFFFAOYSA-N 50637789 CHEMBL5532327 Histone deacetylase 1 Human 29 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637789 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=50637789&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 169092061 519658192 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51584650 O=C(CCCCCCN1C(=O)C/C(=C\c2ccc(Cl)c(Cl)c2)C1=O)NO InChI=1S/C18H20Cl2N2O4/c19-14-7-6-12(10-15(14)20)9-13-11-17(24)22(18(13)25)8-4-2-1-3-5-16(23)21-26/h6-7,9-10,26H,1-5,8,11H2,(H,21,23) DGRNLWVQNPZYQI-UHFFFAOYSA-N 50637790 CHEMBL5563329 Histone deacetylase 1 Human 28 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637790 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=50637790&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 169092116 519658193 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51584651 COc1ccc(/C=C2\CC(=O)N(CCCCCCC(=O)NO)C2=O)cc1 InChI=1S/C19H24N2O5/c1-26-16-9-7-14(8-10-16)12-15-13-18(23)21(19(15)24)11-5-3-2-4-6-17(22)20-25/h7-10,12,25H,2-6,11,13H2,1H3,(H,20,22) JZKDRFIQFIEUQU-UHFFFAOYSA-N 50637791 CHEMBL5532269 Histone deacetylase 1 Human 13 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637791 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=50637791&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 169092118 519658194 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51584652 COc1cccc(/C=C2\CC(=O)N(CCCCCCC(=O)NO)C2=O)c1 InChI=1S/C19H24N2O5/c1-26-16-8-6-7-14(12-16)11-15-13-18(23)21(19(15)24)10-5-3-2-4-9-17(22)20-25/h6-8,11-12,25H,2-5,9-10,13H2,1H3,(H,20,22) XJEFVLVPFYENFG-UHFFFAOYSA-N 50637792 CHEMBL5567675 Histone deacetylase 1 Human 19 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637792 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=50637792&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 169092081 519658195 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51584653 COc1ccccc1/C=C1\CC(=O)N(CCCCCCC(=O)NO)C1=O InChI=1S/C19H24N2O5/c1-26-16-9-6-5-8-14(16)12-15-13-18(23)21(19(15)24)11-7-3-2-4-10-17(22)20-25/h5-6,8-9,12,25H,2-4,7,10-11,13H2,1H3,(H,20,22) FKCQAJYTZWXNQB-UHFFFAOYSA-N 50637793 CHEMBL5559821 Histone deacetylase 1 Human 13 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637793 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=50637793&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 169092096 519658196 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51584654 COc1ccc(/C=C2\CC(=O)N(CCCCCCC(=O)NO)C2=O)cc1OC InChI=1S/C20H26N2O6/c1-27-16-9-8-14(12-17(16)28-2)11-15-13-19(24)22(20(15)25)10-6-4-3-5-7-18(23)21-26/h8-9,11-12,26H,3-7,10,13H2,1-2H3,(H,21,23) CQDOLCKZWDEIDI-UHFFFAOYSA-N 50637794 CHEMBL5561081 Histone deacetylase 1 Human 25 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637794 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=50637794&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 169092124 519658197 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51584655 COc1cc(/C=C2\CC(=O)N(CCCCCCC(=O)NO)C2=O)cc(OC)c1OC InChI=1S/C21H28N2O7/c1-28-16-11-14(12-17(29-2)20(16)30-3)10-15-13-19(25)23(21(15)26)9-7-5-4-6-8-18(24)22-27/h10-12,27H,4-9,13H2,1-3H3,(H,22,24) KUJAMDVWCYHFQS-UHFFFAOYSA-N 50637795 CHEMBL5561055 Histone deacetylase 1 Human 28 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637795 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=50637795&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 169092056 519658198 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51584656 O=C(CCCCCCN1C(=O)C/C(=C\c2ccccc2O)C1=O)NO InChI=1S/C18H22N2O5/c21-15-8-5-4-7-13(15)11-14-12-17(23)20(18(14)24)10-6-2-1-3-9-16(22)19-25/h4-5,7-8,11,21,25H,1-3,6,9-10,12H2,(H,19,22) DGXTWWOXDVLLDE-UHFFFAOYSA-N 50637796 CHEMBL5556260 Histone deacetylase 1 Human 19 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637796 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=50637796&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 169092075 519658199 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51584657 CCOc1ccccc1/C=C1\CC(=O)N(CCCCCCC(=O)NO)C1=O InChI=1S/C20H26N2O5/c1-2-27-17-10-7-6-9-15(17)13-16-14-19(24)22(20(16)25)12-8-4-3-5-11-18(23)21-26/h6-7,9-10,13,26H,2-5,8,11-12,14H2,1H3,(H,21,23) UUPCRZBAAWZWPO-UHFFFAOYSA-N 50637797 CHEMBL5563892 Histone deacetylase 1 Human 17 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637797 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=50637797&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 169092105 519658200 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51584658 COc1ccc(Br)cc1/C=C1\CC(=O)N(CCCCCCC(=O)NO)C1=O InChI=1S/C19H23BrN2O5/c1-27-16-8-7-15(20)11-13(16)10-14-12-18(24)22(19(14)25)9-5-3-2-4-6-17(23)21-26/h7-8,10-11,26H,2-6,9,12H2,1H3,(H,21,23) ZYBRICTUJHDRKX-UHFFFAOYSA-N 50637798 CHEMBL5568342 Histone deacetylase 1 Human 78 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637798 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=50637798&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 169092091 519658201 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51584659 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 15 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University 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 7SGG,3C0Z,9GKX,9GKV,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,9GN6,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 CHEMBL98 DB02546 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51584660 Nc1cc(F)ccc1NC(=O)c1ccc(CNC(=O)\C=C\c2cccnc2)cc1 InChI=1S/C22H19FN4O2/c23-18-8-9-20(19(24)12-18)27-22(29)17-6-3-16(4-7-17)14-26-21(28)10-5-15-2-1-11-25-13-15/h1-13H,14,24H2,(H,26,28)(H,27,29) SZMJVTADHFNAIS-UHFFFAOYSA-N 50457079 CS-055::CS055::Chidamide::Epidaza in China::HBI-8000::Tucidinostat::US11377423, HUYA::US11672788, Compound Chidamide Histone deacetylase 1 Homo sapiens 122 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50457079 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=50457079&enzyme=Histone+deacetylase+1&column=ki&startPg=0&Increment=50&submit=Search 12136798 433924346 1 MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA 8VRT,8VPQ,8VOJ,7AOA,7AO9,7AO8,6Z2K,6Z2J,4BKX,5ICN,3MAX Histone deacetylase 1 HDAC1_HUMAN Q13547 Q92534 51584661 COc1ccccc1/C=C1\CC(=O)N(CCCCCCC(=O)NO)C1=O InChI=1S/C19H24N2O5/c1-26-16-9-6-5-8-14(16)12-15-13-18(23)21(19(15)24)11-7-3-2-4-10-17(22)20-25/h5-6,8-9,12,25H,2-4,7,10-11,13H2,1H3,(H,20,22) FKCQAJYTZWXNQB-UHFFFAOYSA-N 50637793 CHEMBL5559821 Histone deacetylase 2 Human 14 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637793 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=50637793&enzyme=Histone+deacetylase+2&column=ki&startPg=0&Increment=50&submit=Search 169092096 519658196 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 51584662 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 24 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University 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 7SGG,3C0Z,9GKX,9GKV,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,9GN6,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 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 51584663 Nc1cc(F)ccc1NC(=O)c1ccc(CNC(=O)\C=C\c2cccnc2)cc1 InChI=1S/C22H19FN4O2/c23-18-8-9-20(19(24)12-18)27-22(29)17-6-3-16(4-7-17)14-26-21(28)10-5-15-2-1-11-25-13-15/h1-13H,14,24H2,(H,26,28)(H,27,29) SZMJVTADHFNAIS-UHFFFAOYSA-N 50457079 CS-055::CS055::Chidamide::Epidaza in China::HBI-8000::Tucidinostat::US11377423, HUYA::US11672788, Compound Chidamide Histone deacetylase 2 Homo sapiens 48 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50457079 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=50457079&enzyme=Histone+deacetylase+2&column=ki&startPg=0&Increment=50&submit=Search 12136798 433924346 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 51584664 COc1ccccc1/C=C1\CC(=O)N(CCCCCCC(=O)NO)C1=O InChI=1S/C19H24N2O5/c1-26-16-9-6-5-8-14(16)12-15-13-18(23)21(19(15)24)11-7-3-2-4-10-17(22)20-25/h5-6,8-9,12,25H,2-4,7,10-11,13H2,1H3,(H,20,22) FKCQAJYTZWXNQB-UHFFFAOYSA-N 50637793 CHEMBL5559821 Histone deacetylase 3 Human 20 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637793 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=50637793&enzyme=Histone+deacetylase+3&column=ki&startPg=0&Increment=50&submit=Search 169092096 519658196 1 MAKTVAYFYDPDVGNFHYGAGHPMKPHRLALTHSLVLHYGLYKKMIVFKPYQASQHDMCRFHSEDYIDFLQRVSPTNMQGFTKSLNAFNVGDDCPVFPGLFEFCSRYTGASLQGATQLNNKICDIAINWAGGLHHAKKFEASGFCYVNDIVIGILELLKYHPRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYKHLFQPVINQVVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEYVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVEEAISEELPYSEYFEYFAPDFTLHPDVSTRIENQNSRQYLDQIRQTIFENLKMLNHAPSVQIHDVPADLLTYDRTDEADAEERGPEENYSRPEAPNEFYDGDHDNDKESDVEI 4A69 Histone deacetylase 3 HDAC3_HUMAN O15379 D3DQE1 O43268 Q9UEI5 Q9UEV0 51584665 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 44 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University 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 7SGG,3C0Z,9GKX,9GKV,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,9GN6,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 CHEMBL98 DB02546 1 MAKTVAYFYDPDVGNFHYGAGHPMKPHRLALTHSLVLHYGLYKKMIVFKPYQASQHDMCRFHSEDYIDFLQRVSPTNMQGFTKSLNAFNVGDDCPVFPGLFEFCSRYTGASLQGATQLNNKICDIAINWAGGLHHAKKFEASGFCYVNDIVIGILELLKYHPRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYKHLFQPVINQVVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEYVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVEEAISEELPYSEYFEYFAPDFTLHPDVSTRIENQNSRQYLDQIRQTIFENLKMLNHAPSVQIHDVPADLLTYDRTDEADAEERGPEENYSRPEAPNEFYDGDHDNDKESDVEI 4A69 Histone deacetylase 3 HDAC3_HUMAN O15379 D3DQE1 O43268 Q9UEI5 Q9UEV0 51584666 Nc1cc(F)ccc1NC(=O)c1ccc(CNC(=O)\C=C\c2cccnc2)cc1 InChI=1S/C22H19FN4O2/c23-18-8-9-20(19(24)12-18)27-22(29)17-6-3-16(4-7-17)14-26-21(28)10-5-15-2-1-11-25-13-15/h1-13H,14,24H2,(H,26,28)(H,27,29) SZMJVTADHFNAIS-UHFFFAOYSA-N 50457079 CS-055::CS055::Chidamide::Epidaza in China::HBI-8000::Tucidinostat::US11377423, HUYA::US11672788, Compound Chidamide Histone deacetylase 3 Homo sapiens 590 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50457079 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=50457079&enzyme=Histone+deacetylase+3&column=ki&startPg=0&Increment=50&submit=Search 12136798 433924346 1 MAKTVAYFYDPDVGNFHYGAGHPMKPHRLALTHSLVLHYGLYKKMIVFKPYQASQHDMCRFHSEDYIDFLQRVSPTNMQGFTKSLNAFNVGDDCPVFPGLFEFCSRYTGASLQGATQLNNKICDIAINWAGGLHHAKKFEASGFCYVNDIVIGILELLKYHPRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYKHLFQPVINQVVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEYVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVEEAISEELPYSEYFEYFAPDFTLHPDVSTRIENQNSRQYLDQIRQTIFENLKMLNHAPSVQIHDVPADLLTYDRTDEADAEERGPEENYSRPEAPNEFYDGDHDNDKESDVEI 4A69 Histone deacetylase 3 HDAC3_HUMAN O15379 D3DQE1 O43268 Q9UEI5 Q9UEV0 51584667 COc1ccccc1/C=C1\CC(=O)N(CCCCCCC(=O)NO)C1=O InChI=1S/C19H24N2O5/c1-26-16-9-6-5-8-14(16)12-15-13-18(23)21(19(15)24)11-7-3-2-4-10-17(22)20-25/h5-6,8-9,12,25H,2-4,7,10-11,13H2,1H3,(H,20,22) FKCQAJYTZWXNQB-UHFFFAOYSA-N 50637793 CHEMBL5559821 Histone deacetylase 4 Human >5000 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637793 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=50637793&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 169092096 519658196 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51584668 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 4 Homo sapiens >5000 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University 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=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=19149&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,9GKX,9GKV,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,9GN6,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 CHEMBL98 DB02546 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51584669 Nc1cc(F)ccc1NC(=O)c1ccc(CNC(=O)\C=C\c2cccnc2)cc1 InChI=1S/C22H19FN4O2/c23-18-8-9-20(19(24)12-18)27-22(29)17-6-3-16(4-7-17)14-26-21(28)10-5-15-2-1-11-25-13-15/h1-13H,14,24H2,(H,26,28)(H,27,29) SZMJVTADHFNAIS-UHFFFAOYSA-N 50457079 CS-055::CS055::Chidamide::Epidaza in China::HBI-8000::Tucidinostat::US11377423, HUYA::US11672788, Compound Chidamide Histone deacetylase 4 Homo sapiens >5000 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50457079 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=50457079&enzyme=Histone+deacetylase+4&column=ki&startPg=0&Increment=50&submit=Search 12136798 433924346 1 MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL 2VQM,2VQJ,6FYZ,4CBT,7XUZ Histone deacetylase 4 HDAC4_HUMAN P56524 E9PGB9 F5GX36 Q86YH7 Q9UND6 51584670 COc1ccccc1/C=C1\CC(=O)N(CCCCCCC(=O)NO)C1=O InChI=1S/C19H24N2O5/c1-26-16-9-6-5-8-14(16)12-15-13-18(23)21(19(15)24)11-7-3-2-4-10-17(22)20-25/h5-6,8-9,12,25H,2-4,7,10-11,13H2,1H3,(H,20,22) FKCQAJYTZWXNQB-UHFFFAOYSA-N 50637793 CHEMBL5559821 Histone deacetylase 5 Human >5000 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637793 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=50637793&enzyme=Histone+deacetylase+5&column=ki&startPg=0&Increment=50&submit=Search 169092096 519658196 1 MNSPNESDGMSGREPSLEILPRTSLHSIPVTVEVKPVLPRAMPSSMGGGGGGSPSPVELRGALVGSVDPTLREQQLQQELLALKQQQQLQKQLLFAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKQQQEMLAAKRQQELEQQRQREQQRQEELEKQRLEQQLLILRNKEKSKESAIASTEVKLRLQEFLLSKSKEPTPGGLNHSLPQHPKCWGAHHASLDQSSPPQSGPPGTPPSYKLPLPGPYDSRDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGTVISTFKKRAVEITGAGPGASSVCNSAPGSGPSSPNSSHSTIAENGFTGSVPNIPTEMLPQHRALPLDSSPNQFSLYTSPSLPNISLGLQATVTVTNSHLTASPKLSTQQEAERQALQSLRQGGTLTGKFMSTSSIPGCLLGVALEGDGSPHGHASLLQHVLLLEQARQQSTLIAVPLHGQSPLVTGERVATSMRTVGKLPRHRPLSRTQSSPLPQSPQALQQLVMQQQHQQFLEKQKQQQLQLGKILTKTGELPRQPTTHPEETEEELTEQQEVLLGEGALTMPREGSTESESTQEDLEEEDEEDDGEEEEDCIQVKDEEGESGAEEGPDLEEPGAGYKKLFSDAQPLQPLQVYQAPLSLATVPHQALGRTQSSPAAPGGMKSPPDQPVKHLFTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLNRQKLDSKKLLGPISQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVGYNVNVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRVVLALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPNINAVATLEKVIEIQSKHWSCVQKFAAGLGRSLREAQAGETEEAETVSAMALLSVGAEQAQAAAAREHSPRPAEEPMEQEPAL Histone deacetylase 5 HDAC5_HUMAN Q9UQL6 C9JFV9 O60340 O60528 Q96DY4 51584671 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 5 Homo sapiens >5000 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University 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=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=19149&enzyme=Histone+deacetylase+5&column=ki&startPg=0&Increment=50&submit=Search SHH 5311 46519184 CHEMBL98 DB02546 1 MNSPNESDGMSGREPSLEILPRTSLHSIPVTVEVKPVLPRAMPSSMGGGGGGSPSPVELRGALVGSVDPTLREQQLQQELLALKQQQQLQKQLLFAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKQQQEMLAAKRQQELEQQRQREQQRQEELEKQRLEQQLLILRNKEKSKESAIASTEVKLRLQEFLLSKSKEPTPGGLNHSLPQHPKCWGAHHASLDQSSPPQSGPPGTPPSYKLPLPGPYDSRDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGTVISTFKKRAVEITGAGPGASSVCNSAPGSGPSSPNSSHSTIAENGFTGSVPNIPTEMLPQHRALPLDSSPNQFSLYTSPSLPNISLGLQATVTVTNSHLTASPKLSTQQEAERQALQSLRQGGTLTGKFMSTSSIPGCLLGVALEGDGSPHGHASLLQHVLLLEQARQQSTLIAVPLHGQSPLVTGERVATSMRTVGKLPRHRPLSRTQSSPLPQSPQALQQLVMQQQHQQFLEKQKQQQLQLGKILTKTGELPRQPTTHPEETEEELTEQQEVLLGEGALTMPREGSTESESTQEDLEEEDEEDDGEEEEDCIQVKDEEGESGAEEGPDLEEPGAGYKKLFSDAQPLQPLQVYQAPLSLATVPHQALGRTQSSPAAPGGMKSPPDQPVKHLFTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLNRQKLDSKKLLGPISQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVGYNVNVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRVVLALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPNINAVATLEKVIEIQSKHWSCVQKFAAGLGRSLREAQAGETEEAETVSAMALLSVGAEQAQAAAAREHSPRPAEEPMEQEPAL Histone deacetylase 5 HDAC5_HUMAN Q9UQL6 C9JFV9 O60340 O60528 Q96DY4 51584672 Nc1cc(F)ccc1NC(=O)c1ccc(CNC(=O)\C=C\c2cccnc2)cc1 InChI=1S/C22H19FN4O2/c23-18-8-9-20(19(24)12-18)27-22(29)17-6-3-16(4-7-17)14-26-21(28)10-5-15-2-1-11-25-13-15/h1-13H,14,24H2,(H,26,28)(H,27,29) SZMJVTADHFNAIS-UHFFFAOYSA-N 50457079 CS-055::CS055::Chidamide::Epidaza in China::HBI-8000::Tucidinostat::US11377423, HUYA::US11672788, Compound Chidamide Histone deacetylase 5 Homo sapiens >5000 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50457079 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=50457079&enzyme=Histone+deacetylase+5&column=ki&startPg=0&Increment=50&submit=Search 12136798 433924346 1 MNSPNESDGMSGREPSLEILPRTSLHSIPVTVEVKPVLPRAMPSSMGGGGGGSPSPVELRGALVGSVDPTLREQQLQQELLALKQQQQLQKQLLFAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKQQQEMLAAKRQQELEQQRQREQQRQEELEKQRLEQQLLILRNKEKSKESAIASTEVKLRLQEFLLSKSKEPTPGGLNHSLPQHPKCWGAHHASLDQSSPPQSGPPGTPPSYKLPLPGPYDSRDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGTVISTFKKRAVEITGAGPGASSVCNSAPGSGPSSPNSSHSTIAENGFTGSVPNIPTEMLPQHRALPLDSSPNQFSLYTSPSLPNISLGLQATVTVTNSHLTASPKLSTQQEAERQALQSLRQGGTLTGKFMSTSSIPGCLLGVALEGDGSPHGHASLLQHVLLLEQARQQSTLIAVPLHGQSPLVTGERVATSMRTVGKLPRHRPLSRTQSSPLPQSPQALQQLVMQQQHQQFLEKQKQQQLQLGKILTKTGELPRQPTTHPEETEEELTEQQEVLLGEGALTMPREGSTESESTQEDLEEEDEEDDGEEEEDCIQVKDEEGESGAEEGPDLEEPGAGYKKLFSDAQPLQPLQVYQAPLSLATVPHQALGRTQSSPAAPGGMKSPPDQPVKHLFTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLNRQKLDSKKLLGPISQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVGYNVNVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRVVLALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPNINAVATLEKVIEIQSKHWSCVQKFAAGLGRSLREAQAGETEEAETVSAMALLSVGAEQAQAAAAREHSPRPAEEPMEQEPAL Histone deacetylase 5 HDAC5_HUMAN Q9UQL6 C9JFV9 O60340 O60528 Q96DY4 51584673 COc1ccccc1/C=C1\CC(=O)N(CCCCCCC(=O)NO)C1=O InChI=1S/C19H24N2O5/c1-26-16-9-6-5-8-14(16)12-15-13-18(23)21(19(15)24)11-7-3-2-4-10-17(22)20-25/h5-6,8-9,12,25H,2-4,7,10-11,13H2,1H3,(H,20,22) FKCQAJYTZWXNQB-UHFFFAOYSA-N 50637793 CHEMBL5559821 Histone deacetylase 6 Human 3.0 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637793 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=50637793&enzyme=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search 169092096 519658196 1 MTSTGQDSTTTRQRRSRQNPQSPPQDSSVTSKRNIKKGAVPRSIPNLAEVKKKGKMKKLGQAMEEDLIVGLQGMDLNLEAEALAGTGLVLDEQLNEFHCLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCRSAQASVSCALEALEPFWEVLVRSTETVERDNMEEDNVEESEEEGPWEPPVLPILTWPVLQSRTGLVYDQNMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQTISGHALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLSGALASITETIQVHRRYWRSLRVMKVEDREGPSSSKLVTKKAPQPAKPRLAERMTTREKKVLEAGMGKVTSASFGEESTPGQTNSETAVVALTQDQPSEAATGGATLAQTISEAAIGGAMLGQTTSEEAVGGATPDQTTSEETVGGAILDQTTSEDAVGGATLGQTTSEEAVGGATLAQTTSEAAMEGATLDQTTSEEAPGGTELIQTPLASSTDHQTPPTSPVQGTTPQISPSTLIGSLRTLELGSESQGASESQAPGEENLLGEAAGGQDMADSMLMQGSRGLTDQAIFYAVTPLPWCPHLVAVCPIPAAGLDVTQPCGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHGNSGHPLVLSYIDLSAWCYYCQAYVHHQALLDVKNIAHQNKFGEDMPHPH 5EDU,7ZYU,3PHD,3GV4 Protein deacetylase HDAC6 HDAC6_HUMAN Q9UBN7 O94975 Q6NT75 Q7L3E5 Q96CY0 51584674 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 6.8 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University 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 7SGG,3C0Z,9GKX,9GKV,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,9GN6,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 CHEMBL98 DB02546 1 MTSTGQDSTTTRQRRSRQNPQSPPQDSSVTSKRNIKKGAVPRSIPNLAEVKKKGKMKKLGQAMEEDLIVGLQGMDLNLEAEALAGTGLVLDEQLNEFHCLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCRSAQASVSCALEALEPFWEVLVRSTETVERDNMEEDNVEESEEEGPWEPPVLPILTWPVLQSRTGLVYDQNMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQTISGHALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLSGALASITETIQVHRRYWRSLRVMKVEDREGPSSSKLVTKKAPQPAKPRLAERMTTREKKVLEAGMGKVTSASFGEESTPGQTNSETAVVALTQDQPSEAATGGATLAQTISEAAIGGAMLGQTTSEEAVGGATPDQTTSEETVGGAILDQTTSEDAVGGATLGQTTSEEAVGGATLAQTTSEAAMEGATLDQTTSEEAPGGTELIQTPLASSTDHQTPPTSPVQGTTPQISPSTLIGSLRTLELGSESQGASESQAPGEENLLGEAAGGQDMADSMLMQGSRGLTDQAIFYAVTPLPWCPHLVAVCPIPAAGLDVTQPCGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHGNSGHPLVLSYIDLSAWCYYCQAYVHHQALLDVKNIAHQNKFGEDMPHPH 5EDU,7ZYU,3PHD,3GV4 Protein deacetylase HDAC6 HDAC6_HUMAN Q9UBN7 O94975 Q6NT75 Q7L3E5 Q96CY0 51584675 Nc1cc(F)ccc1NC(=O)c1ccc(CNC(=O)\C=C\c2cccnc2)cc1 InChI=1S/C22H19FN4O2/c23-18-8-9-20(19(24)12-18)27-22(29)17-6-3-16(4-7-17)14-26-21(28)10-5-15-2-1-11-25-13-15/h1-13H,14,24H2,(H,26,28)(H,27,29) SZMJVTADHFNAIS-UHFFFAOYSA-N 50457079 CS-055::CS055::Chidamide::Epidaza in China::HBI-8000::Tucidinostat::US11377423, HUYA::US11672788, Compound Chidamide Histone deacetylase 6 Homo sapiens >5000 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50457079 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=50457079&enzyme=Histone+deacetylase+6&column=ki&startPg=0&Increment=50&submit=Search 12136798 433924346 1 MTSTGQDSTTTRQRRSRQNPQSPPQDSSVTSKRNIKKGAVPRSIPNLAEVKKKGKMKKLGQAMEEDLIVGLQGMDLNLEAEALAGTGLVLDEQLNEFHCLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCRSAQASVSCALEALEPFWEVLVRSTETVERDNMEEDNVEESEEEGPWEPPVLPILTWPVLQSRTGLVYDQNMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQTISGHALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLSGALASITETIQVHRRYWRSLRVMKVEDREGPSSSKLVTKKAPQPAKPRLAERMTTREKKVLEAGMGKVTSASFGEESTPGQTNSETAVVALTQDQPSEAATGGATLAQTISEAAIGGAMLGQTTSEEAVGGATPDQTTSEETVGGAILDQTTSEDAVGGATLGQTTSEEAVGGATLAQTTSEAAMEGATLDQTTSEEAPGGTELIQTPLASSTDHQTPPTSPVQGTTPQISPSTLIGSLRTLELGSESQGASESQAPGEENLLGEAAGGQDMADSMLMQGSRGLTDQAIFYAVTPLPWCPHLVAVCPIPAAGLDVTQPCGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHGNSGHPLVLSYIDLSAWCYYCQAYVHHQALLDVKNIAHQNKFGEDMPHPH 5EDU,7ZYU,3PHD,3GV4 Protein deacetylase HDAC6 HDAC6_HUMAN Q9UBN7 O94975 Q6NT75 Q7L3E5 Q96CY0 51584676 COc1ccccc1/C=C1\CC(=O)N(CCCCCCC(=O)NO)C1=O InChI=1S/C19H24N2O5/c1-26-16-9-6-5-8-14(16)12-15-13-18(23)21(19(15)24)11-7-3-2-4-10-17(22)20-25/h5-6,8-9,12,25H,2-4,7,10-11,13H2,1H3,(H,20,22) FKCQAJYTZWXNQB-UHFFFAOYSA-N 50637793 CHEMBL5559821 Histone deacetylase 7 Human >5000 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637793 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=50637793&enzyme=Histone+deacetylase+7&column=ki&startPg=0&Increment=50&submit=Search 169092096 519658196 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 51584677 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 7 Homo sapiens >5000 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University 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=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=19149&enzyme=Histone+deacetylase+7&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,9GKX,9GKV,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,9GN6,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 CHEMBL98 DB02546 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 51584678 Nc1cc(F)ccc1NC(=O)c1ccc(CNC(=O)\C=C\c2cccnc2)cc1 InChI=1S/C22H19FN4O2/c23-18-8-9-20(19(24)12-18)27-22(29)17-6-3-16(4-7-17)14-26-21(28)10-5-15-2-1-11-25-13-15/h1-13H,14,24H2,(H,26,28)(H,27,29) SZMJVTADHFNAIS-UHFFFAOYSA-N 50457079 CS-055::CS055::Chidamide::Epidaza in China::HBI-8000::Tucidinostat::US11377423, HUYA::US11672788, Compound Chidamide Histone deacetylase 7 Homo sapiens >5000 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50457079 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=50457079&enzyme=Histone+deacetylase+7&column=ki&startPg=0&Increment=50&submit=Search 12136798 433924346 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 51584679 COc1ccccc1/C=C1\CC(=O)N(CCCCCCC(=O)NO)C1=O InChI=1S/C19H24N2O5/c1-26-16-9-6-5-8-14(16)12-15-13-18(23)21(19(15)24)11-7-3-2-4-10-17(22)20-25/h5-6,8-9,12,25H,2-4,7,10-11,13H2,1H3,(H,20,22) FKCQAJYTZWXNQB-UHFFFAOYSA-N 50637793 CHEMBL5559821 Histone deacetylase 8 Human 566 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637793 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=50637793&enzyme=Histone+deacetylase+8&column=ki&startPg=0&Increment=50&submit=Search 169092096 519658196 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 51584680 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 8 Homo sapiens 461 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University 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=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=19149&enzyme=Histone+deacetylase+8&column=ki&startPg=0&Increment=50&submit=Search SHH 7SGG,3C0Z,9GKX,9GKV,8BPC,4LXZ,5EEI,1ZZ1,1T69,4R7L,9GN6,7JVU,4QA0,4BZ6,1C3S,4QA2,7ZZS 5311 46519184 CHEMBL98 DB02546 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 51584681 Nc1cc(F)ccc1NC(=O)c1ccc(CNC(=O)\C=C\c2cccnc2)cc1 InChI=1S/C22H19FN4O2/c23-18-8-9-20(19(24)12-18)27-22(29)17-6-3-16(4-7-17)14-26-21(28)10-5-15-2-1-11-25-13-15/h1-13H,14,24H2,(H,26,28)(H,27,29) SZMJVTADHFNAIS-UHFFFAOYSA-N 50457079 CS-055::CS055::Chidamide::Epidaza in China::HBI-8000::Tucidinostat::US11377423, HUYA::US11672788, Compound Chidamide Histone deacetylase 8 Homo sapiens >5000 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50457079 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=50457079&enzyme=Histone+deacetylase+8&column=ki&startPg=0&Increment=50&submit=Search 12136798 433924346 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 51584682 COc1ccccc1/C=C1\CC(=O)N(CCCCCCC(=O)NO)C1=O InChI=1S/C19H24N2O5/c1-26-16-9-6-5-8-14(16)12-15-13-18(23)21(19(15)24)11-7-3-2-4-10-17(22)20-25/h5-6,8-9,12,25H,2-4,7,10-11,13H2,1H3,(H,20,22) FKCQAJYTZWXNQB-UHFFFAOYSA-N 50637793 CHEMBL5559821 Histone deacetylase 9 Human >5000 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637793 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=50637793&enzyme=Histone+deacetylase+9&column=ki&startPg=0&Increment=50&submit=Search 169092096 519658196 1 MHSMISSVDVKSEVPVGLEPISPLDLRTDLRMMMPVVDPVVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHIKELLAIKQQQELLEKEQKLEQQRQEQEVERHRREQQLPPLRGKDRGRERAVASTEVKQKLQEFLLSKSATKDTPTNGKNHSVSRHPKLWYTAAHHTSLDQSSPPLSGTSPSYKYTLPGAQDAKDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGNVVTSFKKRMFEVTESSVSSSSPGSGPSSPNNGPTGSVTENETSVLPPTPHAEQMVSQQRILIHEDSMNLLSLYTSPSLPNITLGLPAVPSQLNASNSLKEKQKCETQTLRQGVPLPGQYGGSIPASSSHPHVTLEGKPPNSSHQALLQHLLLKEQMRQQKLLVAGGVPLHPQSPLATKERISPGIRGTHKLPRHRPLNRTQSAPLPQSTLAQLVIQQQHQQFLEKQKQYQQQIHMNKLLSKSIEQLKQPGSHLEEAEEELQGDQAMQEDRAPSSGNSTRSDSSACVDDTLGQVGAVKVKEEPVDSDEDAQIQEMESGEQAAFMQQPFLEPTHTRALSVRQAPLAAVGMDGLEKHRLVSRTHSSPAASVLPHPAMDRPLQPGSATGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPLDGQKLDPRILLGDDSQKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMGFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGTGLGEGYNINIAWTGGLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLADGRVVLALEGGHDLTAICDASEACVNALLGNELEPLAEDILHQSPNMNAVISLQKIIEIQSMSLKFS Histone deacetylase 9 HDAC9_HUMAN Q9UKV0 A7E2F3 B7Z4I4 B7Z917 B7Z928 B7Z940 C9JS87 E7EX34 F8W9E0 O94845 O95028 Q2M2R6 Q86SL1 Q86US3 51584683 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 9 Homo sapiens >5000 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University 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=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=19149&enzyme=Histone+deacetylase+9&column=ki&startPg=0&Increment=50&submit=Search SHH 5311 46519184 CHEMBL98 DB02546 1 MHSMISSVDVKSEVPVGLEPISPLDLRTDLRMMMPVVDPVVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHIKELLAIKQQQELLEKEQKLEQQRQEQEVERHRREQQLPPLRGKDRGRERAVASTEVKQKLQEFLLSKSATKDTPTNGKNHSVSRHPKLWYTAAHHTSLDQSSPPLSGTSPSYKYTLPGAQDAKDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGNVVTSFKKRMFEVTESSVSSSSPGSGPSSPNNGPTGSVTENETSVLPPTPHAEQMVSQQRILIHEDSMNLLSLYTSPSLPNITLGLPAVPSQLNASNSLKEKQKCETQTLRQGVPLPGQYGGSIPASSSHPHVTLEGKPPNSSHQALLQHLLLKEQMRQQKLLVAGGVPLHPQSPLATKERISPGIRGTHKLPRHRPLNRTQSAPLPQSTLAQLVIQQQHQQFLEKQKQYQQQIHMNKLLSKSIEQLKQPGSHLEEAEEELQGDQAMQEDRAPSSGNSTRSDSSACVDDTLGQVGAVKVKEEPVDSDEDAQIQEMESGEQAAFMQQPFLEPTHTRALSVRQAPLAAVGMDGLEKHRLVSRTHSSPAASVLPHPAMDRPLQPGSATGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPLDGQKLDPRILLGDDSQKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMGFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGTGLGEGYNINIAWTGGLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLADGRVVLALEGGHDLTAICDASEACVNALLGNELEPLAEDILHQSPNMNAVISLQKIIEIQSMSLKFS Histone deacetylase 9 HDAC9_HUMAN Q9UKV0 A7E2F3 B7Z4I4 B7Z917 B7Z928 B7Z940 C9JS87 E7EX34 F8W9E0 O94845 O95028 Q2M2R6 Q86SL1 Q86US3 51584684 Nc1cc(F)ccc1NC(=O)c1ccc(CNC(=O)\C=C\c2cccnc2)cc1 InChI=1S/C22H19FN4O2/c23-18-8-9-20(19(24)12-18)27-22(29)17-6-3-16(4-7-17)14-26-21(28)10-5-15-2-1-11-25-13-15/h1-13H,14,24H2,(H,26,28)(H,27,29) SZMJVTADHFNAIS-UHFFFAOYSA-N 50457079 CS-055::CS055::Chidamide::Epidaza in China::HBI-8000::Tucidinostat::US11377423, HUYA::US11672788, Compound Chidamide Histone deacetylase 9 Homo sapiens >5000 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50457079 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=50457079&enzyme=Histone+deacetylase+9&column=ki&startPg=0&Increment=50&submit=Search 12136798 433924346 1 MHSMISSVDVKSEVPVGLEPISPLDLRTDLRMMMPVVDPVVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHIKELLAIKQQQELLEKEQKLEQQRQEQEVERHRREQQLPPLRGKDRGRERAVASTEVKQKLQEFLLSKSATKDTPTNGKNHSVSRHPKLWYTAAHHTSLDQSSPPLSGTSPSYKYTLPGAQDAKDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGNVVTSFKKRMFEVTESSVSSSSPGSGPSSPNNGPTGSVTENETSVLPPTPHAEQMVSQQRILIHEDSMNLLSLYTSPSLPNITLGLPAVPSQLNASNSLKEKQKCETQTLRQGVPLPGQYGGSIPASSSHPHVTLEGKPPNSSHQALLQHLLLKEQMRQQKLLVAGGVPLHPQSPLATKERISPGIRGTHKLPRHRPLNRTQSAPLPQSTLAQLVIQQQHQQFLEKQKQYQQQIHMNKLLSKSIEQLKQPGSHLEEAEEELQGDQAMQEDRAPSSGNSTRSDSSACVDDTLGQVGAVKVKEEPVDSDEDAQIQEMESGEQAAFMQQPFLEPTHTRALSVRQAPLAAVGMDGLEKHRLVSRTHSSPAASVLPHPAMDRPLQPGSATGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPLDGQKLDPRILLGDDSQKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMGFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGTGLGEGYNINIAWTGGLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLADGRVVLALEGGHDLTAICDASEACVNALLGNELEPLAEDILHQSPNMNAVISLQKIIEIQSMSLKFS Histone deacetylase 9 HDAC9_HUMAN Q9UKV0 A7E2F3 B7Z4I4 B7Z917 B7Z928 B7Z940 C9JS87 E7EX34 F8W9E0 O94845 O95028 Q2M2R6 Q86SL1 Q86US3 51584685 COc1ccccc1/C=C1\CC(=O)N(CCCCCCC(=O)NO)C1=O InChI=1S/C19H24N2O5/c1-26-16-9-6-5-8-14(16)12-15-13-18(23)21(19(15)24)11-7-3-2-4-10-17(22)20-25/h5-6,8-9,12,25H,2-4,7,10-11,13H2,1H3,(H,20,22) FKCQAJYTZWXNQB-UHFFFAOYSA-N 50637793 CHEMBL5559821 Polyamine deacetylase HDAC10 Human 72 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637793 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=50637793&enzyme=Polyamine+deacetylase+HDAC10&column=ki&startPg=0&Increment=50&submit=Search 169092096 519658196 1 MGTALVYHEDMTATRLLWDDPECEIERPERLTAALDRLRQRGLEQRCLRLSAREASEEELGLVHSPEYVSLVRETQVLGKEELQALSGQFDAIYFHPSTFHCARLAAGAGLQLVDAVLTGAVQNGLALVRPPGHHGQRAAANGFCVFNNVAIAAAHAKQKHGLHRILVVDWDVHHGQGIQYLFEDDPSVLYFSWHRYEHGRFWPFLRESDADAVGRGQGLGFTVNLPWNQVGMGNADYVAAFLHLLLPLAFEFDPELVLVSAGFDSAIGDPEGQMQATPECFAHLTQLLQVLAGGRVCAVLEGGYHLESLAESVCMTVQTLLGDPAPPLSGPMAPCQSALESIQSARAAQAPHWKSLQQQDVTAVPMSPSSHSPEGRPPPLLPGGPVCKAAASAPSSLLDQPCLCPAPSVRTAVALTTPDITLVLPPDVIQQEASALREETEAWARPHESLAREEALTALGKLLYLLDGMLDGQVNSGIAATPASAAAATLDVAVRRGLSHGAQRLLCVALGQLDRPPDLAHDGRSLWLNIRGKEAAALSMFHVSTPLPVMTGGFLSCILGLVLPLAYGFQPDLVLVALGPGHGLQGPHAALLAAMLRGLAGGRVLALLEENSTPQLAGILARVLNGEAPPSLGPSSVASPEDVQALMYLRGQLEPQWKMLQCHPHLVA Polyamine deacetylase HDAC10 HDA10_HUMAN Q969S8 Q08AP4 Q6STF9 Q96P77 Q96P78 Q9H028 Q9UGX1 Q9UGX2 51584686 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 Polyamine deacetylase HDAC10 Homo sapiens 100 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University 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=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=19149&enzyme=Polyamine+deacetylase+HDAC10&column=ki&startPg=0&Increment=50&submit=Search SHH 5311 46519184 CHEMBL98 DB02546 1 MGTALVYHEDMTATRLLWDDPECEIERPERLTAALDRLRQRGLEQRCLRLSAREASEEELGLVHSPEYVSLVRETQVLGKEELQALSGQFDAIYFHPSTFHCARLAAGAGLQLVDAVLTGAVQNGLALVRPPGHHGQRAAANGFCVFNNVAIAAAHAKQKHGLHRILVVDWDVHHGQGIQYLFEDDPSVLYFSWHRYEHGRFWPFLRESDADAVGRGQGLGFTVNLPWNQVGMGNADYVAAFLHLLLPLAFEFDPELVLVSAGFDSAIGDPEGQMQATPECFAHLTQLLQVLAGGRVCAVLEGGYHLESLAESVCMTVQTLLGDPAPPLSGPMAPCQSALESIQSARAAQAPHWKSLQQQDVTAVPMSPSSHSPEGRPPPLLPGGPVCKAAASAPSSLLDQPCLCPAPSVRTAVALTTPDITLVLPPDVIQQEASALREETEAWARPHESLAREEALTALGKLLYLLDGMLDGQVNSGIAATPASAAAATLDVAVRRGLSHGAQRLLCVALGQLDRPPDLAHDGRSLWLNIRGKEAAALSMFHVSTPLPVMTGGFLSCILGLVLPLAYGFQPDLVLVALGPGHGLQGPHAALLAAMLRGLAGGRVLALLEENSTPQLAGILARVLNGEAPPSLGPSSVASPEDVQALMYLRGQLEPQWKMLQCHPHLVA Polyamine deacetylase HDAC10 HDA10_HUMAN Q969S8 Q08AP4 Q6STF9 Q96P77 Q96P78 Q9H028 Q9UGX1 Q9UGX2 51584687 Nc1cc(F)ccc1NC(=O)c1ccc(CNC(=O)\C=C\c2cccnc2)cc1 InChI=1S/C22H19FN4O2/c23-18-8-9-20(19(24)12-18)27-22(29)17-6-3-16(4-7-17)14-26-21(28)10-5-15-2-1-11-25-13-15/h1-13H,14,24H2,(H,26,28)(H,27,29) SZMJVTADHFNAIS-UHFFFAOYSA-N 50457079 CS-055::CS055::Chidamide::Epidaza in China::HBI-8000::Tucidinostat::US11377423, HUYA::US11672788, Compound Chidamide Polyamine deacetylase HDAC10 Homo sapiens 456 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50457079 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=50457079&enzyme=Polyamine+deacetylase+HDAC10&column=ki&startPg=0&Increment=50&submit=Search 12136798 433924346 1 MGTALVYHEDMTATRLLWDDPECEIERPERLTAALDRLRQRGLEQRCLRLSAREASEEELGLVHSPEYVSLVRETQVLGKEELQALSGQFDAIYFHPSTFHCARLAAGAGLQLVDAVLTGAVQNGLALVRPPGHHGQRAAANGFCVFNNVAIAAAHAKQKHGLHRILVVDWDVHHGQGIQYLFEDDPSVLYFSWHRYEHGRFWPFLRESDADAVGRGQGLGFTVNLPWNQVGMGNADYVAAFLHLLLPLAFEFDPELVLVSAGFDSAIGDPEGQMQATPECFAHLTQLLQVLAGGRVCAVLEGGYHLESLAESVCMTVQTLLGDPAPPLSGPMAPCQSALESIQSARAAQAPHWKSLQQQDVTAVPMSPSSHSPEGRPPPLLPGGPVCKAAASAPSSLLDQPCLCPAPSVRTAVALTTPDITLVLPPDVIQQEASALREETEAWARPHESLAREEALTALGKLLYLLDGMLDGQVNSGIAATPASAAAATLDVAVRRGLSHGAQRLLCVALGQLDRPPDLAHDGRSLWLNIRGKEAAALSMFHVSTPLPVMTGGFLSCILGLVLPLAYGFQPDLVLVALGPGHGLQGPHAALLAAMLRGLAGGRVLALLEENSTPQLAGILARVLNGEAPPSLGPSSVASPEDVQALMYLRGQLEPQWKMLQCHPHLVA Polyamine deacetylase HDAC10 HDA10_HUMAN Q969S8 Q08AP4 Q6STF9 Q96P77 Q96P78 Q9H028 Q9UGX1 Q9UGX2 51584688 COc1ccccc1/C=C1\CC(=O)N(CCCCCCC(=O)NO)C1=O InChI=1S/C19H24N2O5/c1-26-16-9-6-5-8-14(16)12-15-13-18(23)21(19(15)24)11-7-3-2-4-10-17(22)20-25/h5-6,8-9,12,25H,2-4,7,10-11,13H2,1H3,(H,20,22) FKCQAJYTZWXNQB-UHFFFAOYSA-N 50637793 CHEMBL5559821 Histone deacetylase 11 Human >5000 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50637793 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=50637793&enzyme=Histone+deacetylase+11&column=ki&startPg=0&Increment=50&submit=Search 169092096 519658196 1 MLHTTQLYQHVPETRWPIVYSPRYNITFMGLEKLHPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKWSFAVATITEIPPVIFLPNFLVQRKVLRPLRTQTGGTIMAGKLAVERGWAINVGGGFHHCSSDRGGGFCAYADITLAIKFLFERVEGISRATIIDLDAHQGNGHERDFMDDKRVYIMDVYNRHIYPGDRFAKQAIRRKVELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGIVKRDELVFRMVRGRRVPILMVTSGGYQKRTARIIADSILNLFGLGLIGPESPSVSAQNSDTPLLPPAVP Histone deacetylase 11 HDA11_HUMAN Q96DB2 B4DDK1 Q9H6I7 Q9H6X3 Q9NTC9 51584689 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 11 Homo sapiens >5000 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University 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=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=19149&enzyme=Histone+deacetylase+11&column=ki&startPg=0&Increment=50&submit=Search SHH 5311 46519184 CHEMBL98 DB02546 1 MLHTTQLYQHVPETRWPIVYSPRYNITFMGLEKLHPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKWSFAVATITEIPPVIFLPNFLVQRKVLRPLRTQTGGTIMAGKLAVERGWAINVGGGFHHCSSDRGGGFCAYADITLAIKFLFERVEGISRATIIDLDAHQGNGHERDFMDDKRVYIMDVYNRHIYPGDRFAKQAIRRKVELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGIVKRDELVFRMVRGRRVPILMVTSGGYQKRTARIIADSILNLFGLGLIGPESPSVSAQNSDTPLLPPAVP Histone deacetylase 11 HDA11_HUMAN Q96DB2 B4DDK1 Q9H6I7 Q9H6X3 Q9NTC9 51584690 Nc1cc(F)ccc1NC(=O)c1ccc(CNC(=O)\C=C\c2cccnc2)cc1 InChI=1S/C22H19FN4O2/c23-18-8-9-20(19(24)12-18)27-22(29)17-6-3-16(4-7-17)14-26-21(28)10-5-15-2-1-11-25-13-15/h1-13H,14,24H2,(H,26,28)(H,27,29) SZMJVTADHFNAIS-UHFFFAOYSA-N 50457079 CS-055::CS055::Chidamide::Epidaza in China::HBI-8000::Tucidinostat::US11377423, HUYA::US11672788, Compound Chidamide Histone deacetylase 11 Homo sapiens >5000 ChEMBL 10.7270/Q2P273R8 38503167 Jiang, Q; Tang, Y; Hu, Q; Wang, B; Ruan, X; Zhou, Q //0 10/11/2025 China Pharmaceutical University http://www.bindingdb.org/bind/chemsearch/marvin/MolStructure.jsp?monomerid=50457079 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=50457079&enzyme=Histone+deacetylase+11&column=ki&startPg=0&Increment=50&submit=Search 12136798 433924346 1 MLHTTQLYQHVPETRWPIVYSPRYNITFMGLEKLHPFDAGKWGKVINFLKEEKLLSDSMLVEAREASEEDLLVVHTRRYLNELKWSFAVATITEIPPVIFLPNFLVQRKVLRPLRTQTGGTIMAGKLAVERGWAINVGGGFHHCSSDRGGGFCAYADITLAIKFLFERVEGISRATIIDLDAHQGNGHERDFMDDKRVYIMDVYNRHIYPGDRFAKQAIRRKVELEWGTEDDEYLDKVERNIKKSLQEHLPDVVVYNAGTDILEGDRLGGLSISPAGIVKRDELVFRMVRGRRVPILMVTSGGYQKRTARIIADSILNLFGLGLIGPESPSVSAQNSDTPLLPPAVP Histone deacetylase 11 HDA11_HUMAN Q96DB2 B4DDK1 Q9H6I7 Q9H6X3 Q9NTC9