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TitleA conserved mechanism of autoinhibition for the AMPK kinase domain: ATP-binding site and catalytic loop refolding as a means of regulation.
Journal, issue, pagesActa Crystallogr. ,Sect. F, Vol. 66, Page 143-151, Year 2010
Publish dateMay 31, 2006 (structure data deposition date)
AuthorsLittler, D.R. / Walker, J.R. / Davis, T. / Wybenga-Groot, L.E. / Finerty, P.J. / Newman, E. / Mackenzie, F. / Dhe-Paganon, S.
External linksActa Crystallogr. ,Sect. F / PubMed:20124709
MethodsX-ray diffraction
Resolution1.85 Å
Structure data

PDB-2h6d:
Protein Kinase Domain of the Human 5'-AMP-activated protein kinase catalytic subunit alpha-2 (AMPK alpha-2 chain)
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsSIGNALING PROTEIN / TRANSFERASE / ATP-binding; Cholesterol biosynthesis; Fatty acid biosynthesis;Kinase; Lipid synthesis; Nucleotide-binding; Phosphorylation; Serine/threonine-protein kinase; Steroid biosynthesis; Sterol biosynthesis; Transferase / Structural Genomics / Structural Genomics Consortium / SGC

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