3hpr
From Proteopedia
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{{STRUCTURE_3hpr| PDB=3hpr | SCENE= }} | {{STRUCTURE_3hpr| PDB=3hpr | SCENE= }} | ||
===Crystal structure of V148G adenylate kinase from E. coli, in complex with Ap5A=== | ===Crystal structure of V148G adenylate kinase from E. coli, in complex with Ap5A=== | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | [[3hpr]] is a 2 chain structure of [[Adenylate kinase]] with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HPR OCA]. | |
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| + | ==See Also== | ||
| + | *[[Adenylate kinase|Adenylate kinase]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:019805185</ref><references group="xtra"/> |
[[Category: Adenylate kinase]] | [[Category: Adenylate kinase]] | ||
| - | [[Category: Escherichia coli | + | [[Category: Escherichia coli]] |
[[Category: Bolen, D W.]] | [[Category: Bolen, D W.]] | ||
[[Category: Hilser, V J.]] | [[Category: Hilser, V J.]] | ||
[[Category: Travis, T P.]] | [[Category: Travis, T P.]] | ||
| - | [[Category: Acetylation]] | ||
[[Category: Atp-binding]] | [[Category: Atp-binding]] | ||
| - | [[Category: Cytoplasm]] | ||
[[Category: Enzyme inhibitor complex]] | [[Category: Enzyme inhibitor complex]] | ||
[[Category: Kinase]] | [[Category: Kinase]] | ||
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[[Category: Nucleotide-binding]] | [[Category: Nucleotide-binding]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov 4 10:57:01 2009'' | ||
Revision as of 12:41, 25 July 2012
Contents |
Crystal structure of V148G adenylate kinase from E. coli, in complex with Ap5A
Template:ABSTRACT PUBMED 19805185
About this Structure
3hpr is a 2 chain structure of Adenylate kinase with sequence from Escherichia coli. Full crystallographic information is available from OCA.
See Also
Reference
- Schrank TP, Bolen DW, Hilser VJ. Rational modulation of conformational fluctuations in adenylate kinase reveals a local unfolding mechanism for allostery and functional adaptation in proteins. Proc Natl Acad Sci U S A. 2009 Oct 6;106(40):16984-9. Epub 2009 Sep 21. PMID:19805185
