| Reaction Details |
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 | Report a problem with these data |
| Target | Histone deacetylase 3 |
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| Ligand | BDBM50314136 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | ChEMBL_623893 (CHEMBL1105416) |
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| IC50 | 58±n/a nM |
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| Citation |  Oger, F; Lecorgne, A; Sala, E; Nardese, V; Demay, F; Chevance, S; Desravines, DC; Aleksandrova, N; Le Guével, R; Lorenzi, S; Beccari, AR; Barath, P; Hart, DJ; Bondon, A; Carettoni, D; Simonneaux, G; Salbert, G Biological and biophysical properties of the histone deacetylase inhibitor suberoylanilide hydroxamic acid are affected by the presence of short alkyl groups on the phenyl ring. J Med Chem53:1937-50 (2010) [PubMed] Article |
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| More Info.: | Get all data from this article, Assay Method |
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| Histone deacetylase 3 |
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| Name: | Histone deacetylase 3 |
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| Synonyms: | HD3 | HDAC3 | HDAC3_HUMAN | Histone deacetylase 3 (HDAC3) | Human HDAC3 | RPD3-2 | SMAP45 |
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| Type: | Enzyme |
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| Mol. Mass.: | 48829.55 |
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| Organism: | Homo sapiens (Human) |
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| Description: | O15379 |
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| Residue: | 428 |
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| Sequence: | MAKTVAYFYDPDVGNFHYGAGHPMKPHRLALTHSLVLHYGLYKKMIVFKPYQASQHDMCR
FHSEDYIDFLQRVSPTNMQGFTKSLNAFNVGDDCPVFPGLFEFCSRYTGASLQGATQLNN
KICDIAINWAGGLHHAKKFEASGFCYVNDIVIGILELLKYHPRVLYIDIDIHHGDGVQEA
FYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYKHLFQPVI
NQVVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEYVKSFNIPLLVLGGGGYTV
RNVARCWTYETSLLVEEAISEELPYSEYFEYFAPDFTLHPDVSTRIENQNSRQYLDQIRQ
TIFENLKMLNHAPSVQIHDVPADLLTYDRTDEADAEERGPEENYSRPEAPNEFYDGDHDN
DKESDVEI
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| BDBM50314136 |
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| n/a |
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| Name | BDBM50314136 |
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| Synonyms: | CHEMBL1089339 | N-Hydroxy-N'-(3-methylphenyl)octanediamide |
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| Type | Small organic molecule |
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| Emp. Form. | C13H18N2O3 |
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| Mol. Mass. | 250.2936 |
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| SMILES | Cc1cccc(NC(=O)CCCCC(=O)NO)c1 |
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| Structure | 
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