| Reaction Details |
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 | Report a problem with these data |
| Target | Histone deacetylase 4 [653-1084,H976Y] |
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| Ligand | BDBM25150 |
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| Substrate/Competitor | BDBM25143 |
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| Meas. Tech. | HDAC Activity Assay |
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| pH | 7.5±n/a |
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| Temperature | 310.15±n/a K |
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| IC50 | 24±n/a nM |
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| Citation |  Jones, P; Altamura, S; De Francesco, R; Gallinari, P; Lahm, A; Neddermann, P; Rowley, M; Serafini, S; Steinkühler, C Probing the elusive catalytic activity of vertebrate class IIa histone deacetylases. Bioorg Med Chem Lett18:1814-9 (2008) [PubMed] Article |
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| More Info.: | Get all data from this article, Inhibition_Run data, Solution Info, Assay Method |
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| Histone deacetylase 4 [653-1084,H976Y] |
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| Name: | Histone deacetylase 4 [653-1084,H976Y] |
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| Synonyms: | HDAC4 | HDAC4_HUMAN | Histone Deacetylase 4 (HDAC4) Mutant (H976Y) | Histone deacetylase 4 gain of function (GOF) mutant | KIAA0288 |
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| Type: | Catalytic domain |
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| Mol. Mass.: | 46476.72 |
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| Organism: | Homo sapiens (Human) |
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| Description: | His-tagged HDAC4 GOF(gain of function, H976Y) catalytic domains (T653-L1084) was expressed in E.coli and purified by Nickel-Chelation affinity chromatography and anion exchange (MonoQ) chromatography. |
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| Residue: | 432 |
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| Sequence: | TTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQ
TVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAAR
LAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVS
KILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNM
AFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARC
FGYLTKQLMGLAGGRIVLALEGGYDLTAICDASEACVSALLGNELDPLPEKVLQQRPNAN
AVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKR
PDEEPMEEEPPL
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| BDBM25150 |
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| BDBM25143 |
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| Name | BDBM25150 |
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| Synonyms: | (2E)-N-hydroxy-3-[3-(phenylsulfamoyl)phenyl]prop-2-enamide | Belinosta | Belinostat | PXD-101 | PXD101 |
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| Type | Small organic molecule |
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| Emp. Form. | C15H14N2O4S |
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| Mol. Mass. | 318.348 |
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| SMILES | ONC(=O)\C=C\c1cccc(c1)S(=O)(=O)Nc1ccccc1 |
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| Structure | 
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