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Structure paper

TitleBinding of phosphatidylinositol 3,4,5-trisphosphate to the pleckstrin homology domain of protein kinase B induces a conformational change.
Journal, issue, pagesBiochem. J., Vol. 375, Page 531-538, Year 2003
Publish dateSep 12, 2003 (structure data deposition date)
AuthorsMilburn, C.C. / Deak, M. / Kelly, S.M. / Price, N.C. / Alessi, D.R. / Van Aalten, D.M.
External linksBiochem. J. / PubMed:12964941
MethodsX-ray diffraction
Resolution0.98 - 1.65 Å
Structure data

PDB-1unp:
Crystal structure of the pleckstrin homology domain of PKB alpha
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-1unq:
High resolution crystal structure of the Pleckstrin Homology Domain Of Protein Kinase B/Akt Bound To Ins(1,3,4,5)-Tetrakisphophate
Method: X-RAY DIFFRACTION / Resolution: 0.98 Å

PDB-1unr:
Crystal structure of the PH domain of PKB alpha in complex with a sulfate molecule
Method: X-RAY DIFFRACTION / Resolution: 1.25 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-4IP:
INOSITOL-(1,3,4,5)-TETRAKISPHOSPHATE

ChemComp-SO4:
SULFATE ION

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / PLECKSTRIN HOMOLOGY DOMAIN / PHOSPHOINOSITIDE / PKB / AKT / SERINE/THREONINE-PROTEIN KINASE / ATP-BINDING / PHOSPHORYLATION / NUCLEAR PROTEIN / PLECKSTRIN HOMOLOGY / PH / ATK

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