| Reaction Details |
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 | Report a problem with these data |
| Target | L-lactate dehydrogenase B chain |
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| Ligand | BDBM50597916 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | ChEMBL_2224766 (CHEMBL5138279) |
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| IC50 | 2.20±n/a nM |
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| Citation |  Wei, B; Robarge, K; Labadie, SS; Chen, J; Corson, LB; DiPasquale, A; Dragovich, PS; Eigenbrot, C; Evangelista, M; Fauber, BP; Hitz, A; Hong, R; Lai, KW; Liu, W; Ma, S; Malek, S; O'Brien, T; Pang, J; Peterson, D; Salphati, L; Sampath, D; Sideris, S; Ultsch, M; Xu, Z; Yen, I; Yu, D; Yue, Q; Zhou, A; Purkey, HE Structure-based optimization of hydroxylactam as potent, cell-active inhibitors of lactate dehydrogenase. Bioorg Med Chem Lett59:0 (2022) [PubMed] Article |
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| More Info.: | Get all data from this article, Assay Method |
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| L-lactate dehydrogenase B chain |
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| Name: | L-lactate dehydrogenase B chain |
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| Synonyms: | L-lactate dehydrogenase B | L-lactate dehydrogenase B chain | LDH heart subunit | LDH-B | LDH-H | LDHB | LDHB_HUMAN | Lactate dehydrogenase B (LDHB) | Renal carcinoma antigen NY-REN-46 |
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| Type: | Oxidoreductase; homotetramer |
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| Mol. Mass.: | 36635.55 |
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| Organism: | Homo sapiens (Human) |
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| Description: | n/a |
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| Residue: | 334 |
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| Sequence: | MATLKEKLIAPVAEEEATVPNNKITVVGVGQVGMACAISILGKSLADELALVDVLEDKLK
GEMMDLQHGSLFLQTPKIVADKDYSVTANSKIVVVTAGVRQQEGESRLNLVQRNVNVFKF
IIPQIVKYSPDCIIIVVSNPVDILTYVTWKLSGLPKHRVIGSGCNLDSARFRYLMAEKLG
IHPSSCHGWILGEHGDSSVAVWSGVNVAGVSLQELNPEMGTDNDSENWKEVHKMVVESAY
EVIKLKGYTNWAIGLSVADLIESMLKNLSRIHPVSTMVKGMYGIENEVFLSLPCILNARG
LTSVINQKLKDDEVAQLKKSADTLWDIQKDLKDL
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| BDBM50597916 |
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| n/a |
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| Name | BDBM50597916 |
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| Synonyms: | CHEMBL5201115 |
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| Type | Small organic molecule |
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| Emp. Form. | C32H27ClFN3O4S |
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| Mol. Mass. | 604.091 |
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| SMILES | OC1=C(Sc2ccccc2Cl)C(=O)NC(C1)(c1ccc(cc1)N1CCOCC1)c1cccc(Oc2ccc(F)cc2)n1 |c:1| |
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| Structure | 
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