2h6d: Difference between revisions
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Revision as of 14:26, 25 July 2012
Protein Kinase Domain of the Human 5'-AMP-activated protein kinase catalytic subunit alpha-2 (AMPK alpha-2 chain)
Template:ABSTRACT PUBMED 20124709
About this Structure
2h6d is a 1 chain structure of AMP-activated protein kinase with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Littler DR, Walker JR, Davis T, Wybenga-Groot LE, Finerty PJ Jr, 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 Struct Biol Cryst Commun. 2010 Feb 1;66(Pt, 2):143-51. Epub 2010 Jan 27. PMID:20124709 doi:10.1107/S1744309109052543
Proteopedia Page Contributors and Editors (what is this?)
Categories:
- Pages with broken file links
- Homo sapiens
- Non-specific serine/threonine protein kinase
- Arrowsmith, C H.
- Bochkarev, A.
- Butler-Cole, C.
- Dhe-Paganon, S.
- Edwards, A M.
- Finerty, P J.
- Littler, D R.
- Mackenzie, F.
- Newman, E M.
- SGC, Structural Genomics Consortium.
- Sundstrom, M.
- Walker, J R.
- Weigelt, J.
- Wybenga-Groot, L.
- Atp-binding
- Cholesterol biosynthesis
- Fatty acid biosynthesis
- Kinase
- Lipid synthesis
- Nucleotide-binding
- Phosphorylation
- Serine/threonine-protein kinase
- Sgc
- Signaling protein
- Steroid biosynthesis
- Sterol biosynthesis
- Structural genomic
- Structural genomics consortium
- Transferase
