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TitleAkt Kinase Activation Mechanisms Revealed Using Protein Semisynthesis.
Journal, issue, pagesCell, Vol. 174, Page 897-907.e14, Year 2018
Publish dateDec 11, 2017 (structure data deposition date)
AuthorsChu, N. / Salguero, A.L. / Liu, A.Z. / Chen, Z. / Dempsey, D.R. / Ficarro, S.B. / Alexander, W.M. / Marto, J.A. / Li, Y. / Amzel, L.M. ...Chu, N. / Salguero, A.L. / Liu, A.Z. / Chen, Z. / Dempsey, D.R. / Ficarro, S.B. / Alexander, W.M. / Marto, J.A. / Li, Y. / Amzel, L.M. / Gabelli, S.B. / Cole, P.A.
External linksCell / PubMed:30078705
MethodsX-ray diffraction
Resolution2.12 - 2.4 Å
Structure data

PDB-6buu:
Crystal structure of AKT1 (aa 144-480) with a bisubstrate
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-6npz:
Crystal structure of Akt1 (aa 123-480) kinase with a bisubstrate
Method: X-RAY DIFFRACTION / Resolution: 2.12 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-MN:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-PGE:
TRIETHYLENE GLYCOL

ChemComp-GOL:
GLYCEROL

ChemComp-VO4:
VANADATE ION

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / AKT1 / RAC-alpha serine/theronine-protein kinase / kinase / phosphorylated tail / semi-synthesis / bisubstrate

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