1e19: Difference between revisions

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[[Image:1e19.png|left|200px]]
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{{STRUCTURE_1e19|  PDB=1e19  |  SCENE=  }}  
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===Structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic archaeon Pyrococcus furiosus bound to ADP===
===Structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic archaeon Pyrococcus furiosus bound to ADP===
{{ABSTRACT_PUBMED_10860751}}


 
==Function==
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[[http://www.uniprot.org/uniprot/CPKA_PYRFU CPKA_PYRFU]] Carbamate kinase that plays a biosynthetic role in that it produces carbamoyl-phosphate.  
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{{ABSTRACT_PUBMED_10860751}}


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
<ref group="xtra">PMID:010860751</ref><references group="xtra"/>
<ref group="xtra">PMID:010860751</ref><references group="xtra"/><references/>
[[Category: Carbamate kinase]]
[[Category: Carbamate kinase]]
[[Category: Pyrococcus furiosus]]
[[Category: Pyrococcus furiosus]]

Revision as of 10:43, 16 April 2014

Template:STRUCTURE 1e19

Structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic archaeon Pyrococcus furiosus bound to ADP

Template:ABSTRACT PUBMED 10860751

Function

[CPKA_PYRFU] Carbamate kinase that plays a biosynthetic role in that it produces carbamoyl-phosphate.

About this Structure

1e19 is a 2 chain structure with sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA.

Reference

  1. 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:https://dx.doi.org/10.1006/jmbi.2000.3779

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