3hpr
From Proteopedia
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- | The | + | <!-- |
+ | The line below this paragraph, containing "STRUCTURE_3hpr", creates the "Structure Box" on the page. | ||
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+ | {{STRUCTURE_3hpr| PDB=3hpr | SCENE= }} | ||
- | + | ===Crystal structure of V148G adenylate kinase from E. coli, in complex with Ap5A=== | |
- | Description: Crystal structure of V148G adenylate kinase from E. coli, in complex with Ap5A | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed | + | <!-- |
+ | The line below this paragraph, {{ABSTRACT_PUBMED_19805185}}, adds the Publication Abstract to the page | ||
+ | (as it appears on PubMed at http://www.pubmed.gov), where 19805185 is the PubMed ID number. | ||
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+ | {{ABSTRACT_PUBMED_19805185}} | ||
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+ | ==About this Structure== | ||
+ | 3HPR is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HPR OCA]. | ||
+ | |||
+ | ==Reference== | ||
+ | <ref group="xtra">PMID:19805185</ref><references group="xtra"/> | ||
+ | [[Category: Adenylate kinase]] | ||
+ | [[Category: Escherichia coli k-12]] | ||
+ | [[Category: Bolen, D W.]] | ||
+ | [[Category: Hilser, V J.]] | ||
+ | [[Category: Travis, T P.]] | ||
+ | [[Category: Acetylation]] | ||
+ | [[Category: Atp-binding]] | ||
+ | [[Category: Cytoplasm]] | ||
+ | [[Category: Enzyme inhibitor complex]] | ||
+ | [[Category: Kinase]] | ||
+ | [[Category: Nucleotide biosynthesis]] | ||
+ | [[Category: Nucleotide-binding]] | ||
+ | [[Category: Transferase]] | ||
+ | |||
+ | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov 4 10:57:01 2009'' |
Revision as of 08:57, 4 November 2009
Crystal structure of V148G adenylate kinase from E. coli, in complex with Ap5A
Template:ABSTRACT PUBMED 19805185
About this Structure
3HPR is a 2 chains structure of sequences from Escherichia coli k-12. Full crystallographic information is available from OCA.
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
Page seeded by OCA on Wed Nov 4 10:57:01 2009