Reaction Details |
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Target | RAC-alpha serine/threonine-protein kinase |
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Ligand | BDBM50278532 |
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Substrate/Competitor | n/a |
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Meas. Tech. | ChEMBL_763185 (CHEMBL1820096) |
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IC50 | 190±n/a nM |
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Citation | Bamborough, P; Brown, MJ; Christopher, JA; Chung, CW; Mellor, GW Selectivity of kinase inhibitor fragments. J Med Chem54:5131-43 (2011) [PubMed] Article |
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More Info.: | Get all data from this article, Assay Method |
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RAC-alpha serine/threonine-protein kinase |
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Name: | RAC-alpha serine/threonine-protein kinase |
Synonyms: | AKT phosphorylation (p-AKT) | AKT1 | AKT1/PPP1CA | AKT1_HUMAN | C-AKT | PKB | PKB alpha | Protein kinase Akt-1 | Protein kinase B | Protein kinase B (AKT1) | Protein kinase B (Akt 1) | Protein kinase B (Akt) | Protein kinase B alpha | Protein kinase B alpha (AKT1) | Proto-oncogene Akt (Akt1) | Proto-oncogene c-Akt (AKT) | Proto-oncogene c-Akt (AKT1) | RAC | RAC-PK-alpha | RAC-alpha serine/threonine-protein kinase (AKT) | RAC-alpha serine/threonine-protein kinase (AKT1) | RAC-alpha serine/threonine-protein kinase (pAKT) |
Type: | Enzyme |
Mol. Mass.: | 55681.25 |
Organism: | Homo sapiens (Human) |
Description: | P31749 |
Residue: | 480 |
Sequence: | MSDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVDQREAPLNNFSVAQC
QLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGLKKQEEEEMDF
RSGSPSDNSGAEEMEVSLAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKI
LKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLS
RERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGI
KDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFEL
ILMEEIRFPRTLGPEAKSLLSGLLKKDPKQRLGGGSEDAKEIMQHRFFAGIVWQHVYEKK
LSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMECVDSERRPHFPQFSYSASGTA
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BDBM50278532 |
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n/a |
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Name | BDBM50278532 |
Synonyms: | CHEMBL471034 | N-(2-amino-1-phenylethyl)-5-(1H-pyrrolo[2,3-b]pyridin-4-yl)thiophene-2-carboxamide |
Type | Small organic molecule |
Emp. Form. | C20H18N4OS |
Mol. Mass. | 362.448 |
SMILES | NCC(NC(=O)c1ccc(s1)-c1ccnc2[nH]ccc12)c1ccccc1 |
Structure |
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