2we4
From Proteopedia
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[[Image:2we4.png|left|200px]] | [[Image:2we4.png|left|200px]] | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | [[2we4]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WE4 OCA]. | |
==Reference== | ==Reference== | ||
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[[Category: Phosphotransferase]] | [[Category: Phosphotransferase]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 7 10:10:35 2010'' | ||
Revision as of 22:02, 14 March 2011
CARBAMATE KINASE FROM ENTEROCOCCUS FAECALIS BOUND TO A SULFATE ION AND TWO WATER MOLECULES, WHICH MIMIC THE SUBSTRATE CARBAMYL PHOSPHATE
Template:ABSTRACT PUBMED 10211841
About this Structure
2we4 is a 4 chain structure with sequence from Enterococcus faecalis. Full crystallographic information is available from OCA.
Reference
- Marina A, Alzari PM, Bravo J, Uriarte M, Barcelona B, Fita I, Rubio V. Carbamate kinase: New structural machinery for making carbamoyl phosphate, the common precursor of pyrimidines and arginine. Protein Sci. 1999 Apr;8(4):934-40. PMID:10211841
- Ramon-Maiques S, Marina A, Uriarte M, Fita I, Rubio V. The 1.5 A resolution crystal structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic Archaeon pyrococcus furiosus, bound to ADP, confirms that this thermostable enzyme is a carbamate kinase, and provides insight into substrate binding and stability in carbamate kinases. J Mol Biol. 2000 Jun 2;299(2):463-76. PMID:10860751 doi:http://dx.doi.org/10.1006/jmbi.2000.3779
