| Reaction Details |
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 | Report a problem with these data |
| Target | Histone-lysine N-methyltransferase EZH2 |
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| Ligand | BDBM50536589 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | ChEMBL_1933810 (CHEMBL4479462) |
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| IC50 | <10.0±n/a nM |
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| Citation |  Yang, X; Li, F; Konze, KD; Meslamani, J; Ma, A; Brown, PJ; Zhou, MM; Arrowsmith, CH; Kaniskan, HÜ; Vedadi, M; Jin, J Structure-Activity Relationship Studies for Enhancer of Zeste Homologue 2 (EZH2) and Enhancer of Zeste Homologue 1 (EZH1) Inhibitors. J Med Chem59:7617-33 (2016) [PubMed] Article |
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| More Info.: | Get all data from this article, Assay Method |
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| Histone-lysine N-methyltransferase EZH2 |
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| Name: | Histone-lysine N-methyltransferase EZH2 |
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| Synonyms: | ENX-1 | EZH2 | EZH2_HUMAN | Enhancer of zeste homolog 2 (EZH2) | Histone-lysine N-methyltransferase EZH2 | KMT6 | Lysine N-methyltransferase 6 |
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| Type: | Protein |
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| Mol. Mass.: | 85367.84 |
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| Organism: | Homo sapiens (Human) |
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| Description: | Q15910 |
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| Residue: | 746 |
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| Sequence: | MGQTGKKSEKGPVCWRKRVKSEYMRLRQLKRFRRADEVKSMFSSNRQKILERTEILNQEW
KQRRIQPVHILTSVSSLRGTRECSVTSDLDFPTQVIPLKTLNAVASVPIMYSWSPLQQNF
MVEDETVLHNIPYMGDEVLDQDGTFIEELIKNYDGKVHGDRECGFINDEIFVELVNALGQ
YNDDDDDDDGDDPEEREEKQKDLEDHRDDKESRPPRKFPSDKIFEAISSMFPDKGTAEEL
KEKYKELTEQQLPGALPPECTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFH
ATPNTYKRKNTETALDNKPCGPQCYQHLEGAKEFAAALTAERIKTPPKRPGGRRRGRLPN
NSSRPSTPTINVLESKDTDSDREAGTETGGENNDKEEEEKKDETSSSSEANSRCQTPIKM
KPNIEPPENVEWSGAEASMFRVLIGTYYDNFCAIARLIGTKTCRQVYEFRVKESSIIAPA
PAEDVDTPPRKKKRKHRLWAAHCRKIQLKKDGSSNHVYNYQPCDHPRQPCDSSCPCVIAQ
NFCEKFCQCSSECQNRFPGCRCKAQCNTKQCPCYLAVRECDPDLCLTCGAADHWDSKNVS
CKNCSIQRGSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYDK
YMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGE
ELFFDYRYSQADALKYVGIEREMEIP
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| BDBM50536589 |
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| n/a |
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| Name | BDBM50536589 |
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| Synonyms: | CHEMBL4545986 |
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| Type | Small organic molecule |
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| Emp. Form. | C35H47N7O2 |
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| Mol. Mass. | 597.7934 |
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| SMILES | CCCc1cc(C)[nH]c(=O)c1CNC(=O)c1cc(cc2n(ncc12)C(CC)CC)-c1ccc(nc1)N1CCN(CC1)C(C)C |
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| Structure | 
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