| Reaction Details |
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 | Report a problem with these data |
| Target | Histone acetyltransferase KAT2B |
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| Ligand | BDBM50012070 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | ChEMBL_1904719 (CHEMBL4407077) |
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| IC50 | >50000±n/a nM |
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| Citation |  Huang, M; Huang, J; Zheng, Y; Sun, Q Histone acetyltransferase inhibitors: An overview in synthesis, structure-activity relationship and molecular mechanism. Eur J Med Chem178:259-286 (2019) [PubMed] Article |
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| More Info.: | Get all data from this article, Assay Method |
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| Histone acetyltransferase KAT2B |
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| Name: | Histone acetyltransferase KAT2B |
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| Synonyms: | Histone acetyltransferase KAT2A/KAT2B | Histone acetyltransferase PCAF | KAT2B | KAT2B_HUMAN | PCAF |
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| Type: | PROTEIN |
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| Mol. Mass.: | 93045.76 |
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| Organism: | Homo sapiens (Human) |
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| Description: | ChEMBL_1502838 |
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| Residue: | 832 |
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| Sequence: | MSEAGGAGPGGCGAGAGAGAGPGALPPQPAALPPAPPQGSPCAAAAGGSGACGPATAVAA
AGTAEGPGGGGSARIAVKKAQLRSAPRAKKLEKLGVYSACKAEESCKCNGWKNPNPSPTP
PRADLQQIIVSLTESCRSCSHALAAHVSHLENVSEEEMNRLLGIVLDVEYLFTCVHKEED
ADTKQVYFYLFKLLRKSILQRGKPVVEGSLEKKPPFEKPSIEQGVNNFVQYKFSHLPAKE
RQTIVELAKMFLNRINYWHLEAPSQRRLRSPNDDISGYKENYTRWLCYCNVPQFCDSLPR
YETTQVFGRTLLRSVFTVMRRQLLEQARQEKDKLPLEKRTLILTHFPKFLSMLEEEVYSQ
NSPIWDQDFLSASSRTSQLGIQTVINPPPVAGTISYNSTSSSLEQPNAGSSSPACKASSG
LEANPGEKRKMTDSHVLEEAKKPRVMGDIPMELINEVMSTITDPAAMLGPETNFLSAHSA
RDEAARLEERRGVIEFHVVGNSLNQKPNKKILMWLVGLQNVFSHQLPRMPKEYITRLVFD
PKHKTLALIKDGRVIGGICFRMFPSQGFTEIVFCAVTSNEQVKGYGTHLMNHLKEYHIKH
DILNFLTYADEYAIGYFKKQGFSKEIKIPKTKYVGYIKDYEGATLMGCELNPRIPYTEFS
VIIKKQKEIIKKLIERKQAQIRKVYPGLSCFKDGVRQIPIESIPGIRETGWKPSGKEKSK
EPRDPDQLYSTLKSILQQVKSHQSAWPFMEPVKRTEAPGYYEVIRFPMDLKTMSERLKNR
YYVSKKLFMADLQRVFTNCKEYNPPESEYYKCANILEKFFFSKIKEAGLIDK
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| BDBM50012070 |
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| n/a |
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| Name | BDBM50012070 |
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| Synonyms: | 5-Hydroxy-2-methyl-[1,4]naphthoquinone | 5-hydroxy-2-methylnaphthalene-1,4-dione | CHEMBL295316 | Plum-bagin | Plumbagin (6b) | Pumbagin | plumbagin |
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| Type | Small organic molecule |
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| Emp. Form. | C11H8O3 |
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| Mol. Mass. | 188.1794 |
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| SMILES | CC1=CC(=O)c2c(O)cccc2C1=O |t:1| |
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| Structure | 
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