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 DOI | 10.2210/pdb1unq/pdb |
Related | 1H10 1UNP 1UNR |
Descriptor | RAC-ALPHA SERINE/THREONINE KINASE, INOSITOL-(1,3,4,5)-TETRAKISPHOSPHATE (3 entities in total) |
Functional Keywords | transferase, pleckstrin homology domain, pkb, akt, phosphoinositide, serine/threonine-protein kinase, atp-binding, phosphorylation, nuclear protein |
Biological source | HOMO SAPIENS (HUMAN) |
Cellular location | Cytoplasm: P31749 |
Total number of polymer chains | 1 |
Total formula weight | 15299.78 |
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 citation | Milburn, 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: 12964941DOI: 10.1042/BJ20031229 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (0.98 Å) |
Structure validation
Download full validation report