| Reaction Details |
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 | Report a problem with these data |
| Target | Histone-lysine N-methyltransferase PRDM9 [195-385] |
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| Ligand | BDBM228651 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | Radioactivity-Based Assay |
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| pH | 8.5±n/a |
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| Temperature | 296.15±n/a K |
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| Kd | 4.1e+3±n/a nM |
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| Comments | extracted |
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| Citation |  Eram, MS; Bustos, SP; Lima-Fernandes, E; Siarheyeva, A; Senisterra, G; Hajian, T; Chau, I; Duan, S; Wu, H; Dombrovski, L; Schapira, M; Arrowsmith, CH; Vedadi, M Trimethylation of histone H3 lysine 36 by human methyltransferase PRDM9 protein. J Biol Chem289:12177-88 (2014) [PubMed] Article |
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| More Info.: | Get all data from this article, Assay Method |
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| |
| Histone-lysine N-methyltransferase PRDM9 [195-385] |
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| Name: | Histone-lysine N-methyltransferase PRDM9 [195-385] |
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| Synonyms: | PFM6 | PR domain-containing protein 9 (PRDM9) | PRDM9 | PRDM9_HUMAN |
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| Type: | Protein |
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| Mol. Mass.: | 21772.09 |
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| Organism: | Homo sapiens (Human) |
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| Description: | Human PRDM9 truncation (195-385 aa) |
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| Residue: | 191 |
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| Sequence: | SEPQDDDYLYCEMCQNFFIDSCAAHGPPTFVKDSAVDKGHPNRSALSLPPGLRIGPSGIP
QAGLGVWNEASDLPLGLHFGPYEGRITEDEEAANNGYSWLITKGRNCYEYVDGKDKSWAN
WMRYVNCARDDEEQNLVAFQYHRQIFYRTCRVIRPGCELLVWYGDEYGQELGIKWGSKWK
KELMAGREPKP
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| BDBM228651 |
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| n/a |
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| Name | BDBM228651 |
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| Synonyms: | H3 (21-44) K36me1 | LATKAARKSAPSTGGVKKPHRYRP |
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| Type | Small organic molecule |
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| Emp. Form. | C114H196N39O30 |
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| Mol. Mass. | 2593.0188 |
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| SMILES | C[NH2+]CCCC[C@H](NC(=O)[C@@H](NC(=O)CNC(=O)CNC(=O)[C@@H](NC(=O)[C@H](CO)NC(=O)[C@@H]1CCCN1C(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@@H](N)CC(C)C)[C@@H](C)O)[C@@H](C)O)C(C)C)C(=O)N[C@@H](CCCCN)C(=O)N1CCC[C@H]1C(=O)N[C@@H](Cc1cnc[nH]1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N1CCC[C@H]1C(O)=O |r| |
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| Structure | 
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