2H6D
Protein Kinase Domain of the Human 5'-AMP-activated protein kinase catalytic subunit alpha-2 (AMPK alpha-2 chain)
Summary for 2H6D
Entry DOI | 10.2210/pdb2h6d/pdb |
Related | 2F15 |
Descriptor | 5'-AMP-activated protein kinase catalytic subunit alpha-2 (2 entities in total) |
Functional Keywords | 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, signaling protein, transferase |
Biological source | Homo sapiens (human) |
Cellular location | Cytoplasm : P54646 |
Total number of polymer chains | 1 |
Total formula weight | 31557.75 |
Authors | Littler, D.R.,Walker, J.R.,Wybenga-Groot, L.,Newman, E.M.,Butler-Cole, C.,Mackenzie, F.,Finerty, P.J.,Weigelt, J.,Sundstrom, M.,Arrowsmith, C.H.,Edwards, A.M.,Bochkarev, A.,Dhe-Paganon, S.,Structural Genomics Consortium (SGC) (deposition date: 2006-05-31, release date: 2006-06-27, Last modification date: 2023-08-30) |
Primary citation | Littler, D.R.,Walker, J.R.,Davis, T.,Wybenga-Groot, L.E.,Finerty, P.J.,Newman, E.,Mackenzie, F.,Dhe-Paganon, S. A conserved mechanism of autoinhibition for the AMPK kinase domain: ATP-binding site and catalytic loop refolding as a means of regulation. Acta Crystallogr.,Sect.F, 66:143-151, 2010 Cited by PubMed: 20124709DOI: 10.1107/S1744309109052543 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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