Reaction Details |
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Target | E3 ubiquitin-protein ligase Mdm2 |
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Ligand | BDBM50397771 |
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Substrate/Competitor | n/a |
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Meas. Tech. | ChEMBL_874354 (CHEMBL2182652) |
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Kd | 1±n/a nM |
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Citation | Rew, Y; Sun, D; Gonzalez-Lopez De Turiso, F; Bartberger, MD; Beck, HP; Canon, J; Chen, A; Chow, D; Deignan, J; Fox, BM; Gustin, D; Huang, X; Jiang, M; Jiao, X; Jin, L; Kayser, F; Kopecky, DJ; Li, Y; Lo, MC; Long, AM; Michelsen, K; Oliner, JD; Osgood, T; Ragains, M; Saiki, AY; Schneider, S; Toteva, M; Yakowec, P; Yan, X; Ye, Q; Yu, D; Zhao, X; Zhou, J; Medina, JC; Olson, SH Structure-based design of novel inhibitors of the MDM2-p53 interaction. J Med Chem55:4936-54 (2012) [PubMed] Article |
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More Info.: | Get all data from this article, Assay Method |
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E3 ubiquitin-protein ligase Mdm2 |
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Name: | E3 ubiquitin-protein ligase Mdm2 |
Synonyms: | Double minute 2 protein | Double minute 2 protein (HDM2) | E3 ubiquitin-protein ligase Mdm2 (p53-binding protein Mdm2) | Hdm2 | Human Double Minute 2 (HDM2) | MDM2 | MDM2-MDMX | MDM2_HUMAN | p53-Binding Protein MDM2 | p53-binding protein |
Type: | Oncoprotein |
Mol. Mass.: | 55196.54 |
Organism: | Homo sapiens (Human) |
Description: | Q00987 |
Residue: | 491 |
Sequence: | MCNTNMSVPTDGAVTTSQIPASEQETLVRPKPLLLKLLKSVGAQKDTYTMKEVLFYLGQY
IMTKRLYDEKQQHIVYCSNDLLGDLFGVPSFSVKEHRKIYTMIYRNLVVVNQQESSDSGT
SVSENRCHLEGGSDQKDLVQELQEEKPSSSHLVSRPSTSSRRRAISETEENSDELSGERQ
RKRHKSDSISLSFDESLALCVIREICCERSSSSESTGTPSNPDLDAGVSEHSGDWLDQDS
VSDQFSVEFEVESLDSEDYSLSEEGQELSDEDDEVYQVTVYQAGESDTDSFEEDPEISLA
DYWKCTSCNEMNPPLPSHCNRCWALRENWLPEDKGKDKGEISEKAKLENSTQAEEGFDVP
DCKKTIVNDSRESCVEENDDKITQASQSQESEDYSQPSTSSSIIYSSQEDVKEFEREETQ
DKEESVESSLPLNAIEPCVICQGRPKNGCIVHGKTGHLMACFTCAKKLKKRNKPCPVCRQ
PIQMIVLTYFP
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BDBM50397771 |
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n/a |
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Name | BDBM50397771 |
Synonyms: | CHEMBL2059300 | US9593129, Example 67 |
Type | Small organic molecule |
Emp. Form. | C28H33Cl2NO5 |
Mol. Mass. | 534.471 |
SMILES | CC[C@H](N1[C@@H]([C@H](C[C@](C)(CC(O)=O)C1=O)c1cccc(Cl)c1)c1ccc(Cl)cc1)C(=O)OC(C)(C)C |r| |
Structure |
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