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1UNQ

High resolution crystal structure of the Pleckstrin Homology Domain Of Protein Kinase B/Akt Bound To Ins(1,3,4,5)-Tetrakisphophate

Summary for 1UNQ
Entry DOI10.2210/pdb1unq/pdb
Related1H10 1UNP 1UNR
DescriptorRAC-ALPHA SERINE/THREONINE KINASE, INOSITOL-(1,3,4,5)-TETRAKISPHOSPHATE (3 entities in total)
Functional Keywordstransferase, pleckstrin homology domain, pkb, akt, phosphoinositide, serine/threonine-protein kinase, atp-binding, phosphorylation, nuclear protein
Biological sourceHOMO SAPIENS (HUMAN)
Cellular locationCytoplasm: P31749
Total number of polymer chains1
Total formula weight15299.78
Authors
Milburn, C.C.,Deak, M.,Kelly, S.M.,Price, N.C.,Alessi, D.R.,van Aalten, D.M.F. (deposition date: 2003-09-12, release date: 2004-09-16, Last modification date: 2023-12-13)
Primary citationMilburn, C.C.,Deak, M.,Kelly, S.M.,Price, N.C.,Alessi, D.R.,Van Aalten, D.M.
Binding of phosphatidylinositol 3,4,5-trisphosphate to the pleckstrin homology domain of protein kinase B induces a conformational change.
Biochem. J., 375:531-538, 2003
Cited by
PubMed: 12964941
DOI: 10.1042/BJ20031229
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (0.98 Å)
Structure validation

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