Reaction Details |
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Target | RAC-alpha serine/threonine-protein kinase |
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Ligand | BDBM50428737 |
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Substrate/Competitor | n/a |
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Meas. Tech. | ChEMBL_947949 (CHEMBL2344170) |
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IC50 | 1900±n/a nM |
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Citation | Niemann, H; Lin, W; Müller, WE; Kubbutat, M; Lai, D; Proksch, P Trimeric hemibastadin congener from the marine sponge Ianthella basta. J Nat Prod76:121-5 (2013) [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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BDBM50428737 |
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n/a |
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Name | BDBM50428737 |
Synonyms: | BASTADIN 3 |
Type | Small organic molecule |
Emp. Form. | C34H30Br4N4O8 |
Mol. Mass. | 942.24 |
SMILES | Oc1ccc(CCNC(=O)C(Cc2cc(Br)c(O)c(c2)-c2cc(CC(N=O)C(=O)NCCc3ccc(O)c(Br)c3)cc(Br)c2O)N=O)cc1Br |
Structure |
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