| Reaction Details |
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 | Report a problem with these data |
| Target | Protein arginine N-methyltransferase 5 |
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| Ligand | BDBM223126 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | In Vitro Enzymatic Assay |
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| Temperature | 298.15±n/a K |
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| IC50 | 7.2e+2±n/a nM |
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| Comments | extracted |
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| Citation |  Ji, S; Ma, S; Wang, WJ; Huang, SZ; Wang, TQ; Xiang, R; Hu, YG; Chen, Q; Li, LL; Yang, SY Discovery of selective protein arginine methyltransferase 5 inhibitors and biological evaluations. Chem Biol Drug Des89:585-598 (2017) [PubMed] Article |
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| More Info.: | Get all data from this article, Assay Method |
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| Protein arginine N-methyltransferase 5 |
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| Name: | Protein arginine N-methyltransferase 5 |
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| Synonyms: | 72 kDa ICln-binding protein | ANM5_HUMAN | HRMT1L5 | Histone-arginine N-methyltransferase PRMT5 | IBP72 | JBP1 | Jak-binding protein 1 | PRMT5 | PRMT5/MEP50 complex | Protein arginine N-methyltransferase 5 (PRMT5) | Protein arginine methyltransferase 5 (PRMT5) | SKB1 | SKB1 homolog | SKB1Hs | Shk1 kinase-binding protein 1 homolog |
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| Type: | Enzyme |
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| Mol. Mass.: | 72679.99 |
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| Organism: | Homo sapiens (Human) |
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| Description: | O14744 |
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| Residue: | 637 |
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| Sequence: | MAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVAKQGFDFLCMPVFHPRFKREFIQEPAK
NRPGPQTRSDLLLSGRDWNTLIVGKLSPWIRPDSKVEKIRRNSEAAMLQELNFGAYLGLP
AFLLPLNQEDNTNLARVLTNHIHTGHHSSMFWMRVPLVAPEDLRDDIIENAPTTHTEEYS
GEEKTWMWWHNFRTLCDYSKRIAVALEIGADLPSNHVIDRWLGEPIKAAILPTSIFLTNK
KGFPVLSKMHQRLIFRLLKLEVQFIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELF
AKGYEDYLQSPLQPLMDNLESQTYEVFEKDPIKYSQYQQAIYKCLLDRVPEEEKDTNVQV
LMVLGAGRGPLVNASLRAAKQADRRIKLYAVEKNPNAVVTLENWQFEEWGSQVTVVSSDM
REWVAPEKADIIVSELLGSFADNELSPECLDGAQHFLKDDGVSIPGEYTSFLAPISSSKL
YNEVRACREKDRDPEAQFEMPYVVRLHNFHQLSAPQPCFTFSHPNRDPMIDNNRYCTLEF
PVEVNTVLHGFAGYFETVLYQDITLSIRPETHSPGMFSWFPILFPIKQPITVREGQTICV
RFWRCSNSKKVWYEWAVTAPVCSAIHNPTGRSYTIGL
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| BDBM223126 |
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| n/a |
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| Name | BDBM223126 |
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| Synonyms: | P5i-7 |
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| Type | Small organic molecule |
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| Emp. Form. | C12H10ClN3OS |
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| Mol. Mass. | 279.745 |
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| SMILES | NC(=S)N\N=C\c1ccc(o1)-c1ccc(Cl)cc1 |
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| Structure | 
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