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; PubMed: 20124709; DOI: 10.1107/S1744309109052543

Experimental method

X-RAY DIFFRACTION (1.85 Å)