3CQW

Crystal Structure of Akt-1 complexed with substrate peptide and inhibitor

Summary for 3CQW

Related3CQU
DescriptorRAC-alpha serine/threonine-protein kinase, Glycogen synthase kinase-3 beta, MANGANESE (II) ION, ... (5 entities in total)
Functional Keywordskinase, apoptosis, atp-binding, carbohydrate metabolism, cytoplasm, glucose metabolism, glycogen biosynthesis, glycogen metabolism, membrane, nucleotide-binding, nucleus, phosphoprotein, serine/threonine-protein kinase, sugar transport, transferase, translation regulation, transport, alternative splicing, wnt signaling pathway
Biological sourceHomo sapiens (human)
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Cellular locationCytoplasm P31749 P49841
Total number of polymer chains2
Total molecular weight41060.96
Authors
Pandit, J. (deposition date: 2008-04-03, release date: 2008-05-27, Last modification date: 2011-07-13)
Primary citation
Lippa, B.,Pan, G.,Corbett, M.,Li, C.,Kauffman, G.S.,Pandit, J.,Robinson, S.,Wei, L.,Kozina, E.,Marr, E.S.,Borzillo, G.,Knauth, E.,Barbacci-Tobin, E.G.,Vincent, P.,Troutman, M.,Baker, D.,Rajamohan, F.,Kakar, S.,Clark, T.,Morris, J.
Synthesis and structure based optimization of novel Akt inhibitors
Bioorg.Med.Chem.Lett., 18:3359-3363, 2008
PubMed: 18456494 (PDB entries with the same primary citation)
DOI: 10.1016/j.bmcl.2008.04.034
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers 0.26640 4.2% 4.0%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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PDB entries from 2020-10-21