Reaction Details |
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Target | Protein kinase C epsilon type |
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Ligand | BDBM50012921 |
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Substrate/Competitor | n/a |
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Meas. Tech. | ChEMBL_1352186 (CHEMBL3268159) |
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IC50 | 25500±n/a nM |
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Citation | Rechfeld, F; Gruber, P; Kirchmair, J; Boehler, M; Hauser, N; Hechenberger, G; Garczarczyk, D; Lapa, GB; Preobrazhenskaya, MN; Goekjian, P; Langer, T; Hofmann, J Thienoquinolines as novel disruptors of the PKCe/RACK2 protein-protein interaction. J Med Chem57:3235-46 (2014) [PubMed] Article |
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More Info.: | Get all data from this article, Assay Method |
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Protein kinase C epsilon type |
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Name: | Protein kinase C epsilon type |
Synonyms: | KPCE_HUMAN | PKC epsilon | PKCE | PRKCE | Protein kinase C epsilon | Protein kinase C epsilon type | Protein kinase C, PKC; classical/novel | Protein kinase C, epsilon | nPKC-epsilon |
Type: | Enzyme |
Mol. Mass.: | 83680.45 |
Organism: | Homo sapiens (Human) |
Description: | The recombinant human PKC enzymes were
produced using a baculovirus expression system in SF9 cells |
Residue: | 737 |
Sequence: | MVVFNGLLKIKICEAVSLKPTAWSLRHAVGPRPQTFLLDPYIALNVDDSRIGQTATKQKT
NSPAWHDEFVTDVCNGRKIELAVFHDAPIGYDDFVANCTIQFEELLQNGSRHFEDWIDLE
PEGRVYVIIDLSGSSGEAPKDNEERVFRERMRPRKRQGAVRRRVHQVNGHKFMATYLRQP
TYCSHCRDFIWGVIGKQGYQCQVCTCVVHKRCHELIITKCAGLKKQETPDQVGSQRFSVN
MPHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVDARGIA
KVLADLGVTPDKITNSGQRRKKLIAGAESPQPASGSSPSEEDRSKSAPTSPCDQEIKELE
NNIRKALSFDNRGEEHRAASSPDGQLMSPGENGEVRQGQAKRLGLDEFNFIKVLGKGSFG
KVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKD
RLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILL
DAEGHCKLADFGMCKEGILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEM
MAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRLGCVASQNGED
AIKQHPFFKEIDWVLLEQKKIKPPFKPRIKTKRDVNNFDQDFTREEPVLTLVDEAIVKQI
NQEEFKGFSYFGEDLMP
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BDBM50012921 |
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n/a |
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Name | BDBM50012921 |
Synonyms: | CHEMBL3261337 |
Type | Small organic molecule |
Emp. Form. | C22H18N4O3S2 |
Mol. Mass. | 450.533 |
SMILES | CCOc1ccc2nc(NC(=O)c3sc4nc5cc(OC)ccc5cc4c3N)sc2c1 |
Structure |
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