| Reaction Details |
|---|
 | Report a problem with these data |
| Target | RAC-alpha serine/threonine-protein kinase [E49C,C296S,C310S,C344S] |
|---|
| Ligand | BDBM25013 |
|---|
| Substrate/Competitor | n/a |
|---|
| Meas. Tech. | KinEASE Assay |
|---|
| IC50 | 0.4± 0.2 nM |
|---|
| Citation |  Fang, Z; Simard, JR; Plenker, D; Nguyen, HD; Phan, T; Wolle, P; Baumeister, S; Rauh, D Discovery of inter-domain stabilizers-a novel assay system for allosteric akt inhibitors. ACS Chem Biol10:279-88 (2015) [PubMed] Article |
|---|
| More Info.: | Get all data from this article, Assay Method |
|---|
| |
| RAC-alpha serine/threonine-protein kinase [E49C,C296S,C310S,C344S] |
|---|
| Name: | RAC-alpha serine/threonine-protein kinase [E49C,C296S,C310S,C344S] |
|---|
| Synonyms: | AKT1 | AKT1_HUMAN | PKB | Protein kinase B (Akt1 E49C, C296S, C310S and C344S ) | RAC |
|---|
| Type: | Protein |
|---|
| Mol. Mass.: | 55608.09 |
|---|
| Organism: | Homo sapiens (Human) |
|---|
| Description: | Human Akt1 containing mutations E49C, C296S, C310S and C344S |
|---|
| Residue: | 480 |
|---|
| Sequence: | MSDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVDQRCAPLNNFSVAQC
QLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGLKKQEEEEMDF
RSGSPSDNSGAEEMEVSLAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKI
LKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLS
RERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLSKEGI
KDGATMKTFSGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMSGRLPFYNQDHEKLFEL
ILMEEIRFPRTLGPEAKSLLSGLLKKDPKQRLGGGSEDAKEIMQHRFFAGIVWQHVYEKK
LSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMECVDSERRPHFPQFSYSASGTA
|
|
|
|---|
| BDBM25013 |
|---|
| n/a |
|---|
| Name | BDBM25013 |
|---|
| Synonyms: | 4-[2-(4-amino-1,2,5-oxadiazol-3-yl)-1-ethyl-7-[(3S)-piperidin-3-ylmethoxy]-1H-imidazo[4,5-c]pyridin-4-yl]-2-methylbut-3-yn-2-ol | GSK-690693 | GSK690693 | US10550114, Compound GSK690693 |
|---|
| Type | Small organic molecule |
|---|
| Emp. Form. | C21H27N7O3 |
|---|
| Mol. Mass. | 425.4842 |
|---|
| SMILES | CCn1c(nc2c(ncc(OC[C@H]3CCCNC3)c12)C#CC(C)(C)O)-c1nonc1N |r| |
|---|
| Structure | 
|
|---|
Search and Browse
