2we4

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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:20188742</ref><ref group="xtra">PMID:10211841</ref><ref group="xtra">PMID:10860751</ref><references group="xtra"/>
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<ref group="xtra">PMID:10211841</ref><ref group="xtra">PMID:10860751</ref><references group="xtra"/>
[[Category: Carbamate kinase]]
[[Category: Carbamate kinase]]
[[Category: Enterococcus faecalis]]
[[Category: Enterococcus faecalis]]
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[[Category: Transferase]]
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Revision as of 07:10, 7 April 2010

Image:2we4.png

Template:STRUCTURE 2we4

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 chains structure with sequences 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

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