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2h6d
From Proteopedia
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[[Image:2h6d.png|left|200px]] | [[Image:2h6d.png|left|200px]] | ||
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{{STRUCTURE_2h6d| PDB=2h6d | SCENE= }} | {{STRUCTURE_2h6d| PDB=2h6d | SCENE= }} | ||
===Protein Kinase Domain of the Human 5'-AMP-activated protein kinase catalytic subunit alpha-2 (AMPK alpha-2 chain)=== | ===Protein Kinase Domain of the Human 5'-AMP-activated protein kinase catalytic subunit alpha-2 (AMPK alpha-2 chain)=== | ||
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{{ABSTRACT_PUBMED_20124709}} | {{ABSTRACT_PUBMED_20124709}} | ||
==About this Structure== | ==About this Structure== | ||
| - | + | [[2h6d]] is a 1 chain structure of [[AMP-activated protein kinase]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H6D OCA]. | |
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| + | ==See Also== | ||
| + | *[[AMP-activated protein kinase|AMP-activated protein kinase]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:020124709</ref><references group="xtra"/> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Non-specific serine/threonine protein kinase]] | [[Category: Non-specific serine/threonine protein kinase]] | ||
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[[Category: Structural genomics consortium]] | [[Category: Structural genomics consortium]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 17 09:51:29 2010'' | ||
Revision as of 14:26, 25 July 2012
Contents |
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
Categories: 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
