1ank
From Proteopedia
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[[Image:1ank.png|left|200px]] | [[Image:1ank.png|left|200px]] | ||
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{{STRUCTURE_1ank| PDB=1ank | SCENE= }} | {{STRUCTURE_1ank| PDB=1ank | SCENE= }} | ||
===THE CLOSED CONFORMATION OF A HIGHLY FLEXIBLE PROTEIN: THE STRUCTURE OF E. COLI ADENYLATE KINASE WITH BOUND AMP AND AMPPNP=== | ===THE CLOSED CONFORMATION OF A HIGHLY FLEXIBLE PROTEIN: THE STRUCTURE OF E. COLI ADENYLATE KINASE WITH BOUND AMP AND AMPPNP=== | ||
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==See Also== | ==See Also== | ||
| - | *[[Adenylate kinase]] | + | *[[Adenylate kinase|Adenylate kinase]] |
==Reference== | ==Reference== | ||
Revision as of 22:53, 26 July 2012
Contents |
THE CLOSED CONFORMATION OF A HIGHLY FLEXIBLE PROTEIN: THE STRUCTURE OF E. COLI ADENYLATE KINASE WITH BOUND AMP AND AMPPNP
Template:ABSTRACT PUBMED 7937733
About this Structure
1ank is a 2 chain structure of Adenylate kinase with sequence from Escherichia coli. Full crystallographic information is available from OCA.
See Also
Reference
- Berry MB, Meador B, Bilderback T, Liang P, Glaser M, Phillips GN Jr. The closed conformation of a highly flexible protein: the structure of E. coli adenylate kinase with bound AMP and AMPPNP. Proteins. 1994 Jul;19(3):183-98. PMID:7937733 doi:http://dx.doi.org/10.1002/prot.340190304
- Haney P, Konisky J, Koretke KK, Luthey-Schulten Z, Wolynes PG. Structural basis for thermostability and identification of potential active site residues for adenylate kinases from the archaeal genus Methanococcus. Proteins. 1997 May;28(1):117-30. PMID:9144797
