1e19

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==About this Structure==
==About this Structure==
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1E19 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E19 OCA].
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1E19 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E19 OCA].
==Reference==
==Reference==
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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., Ramon-Maiques S, Marina A, Uriarte M, Fita I, Rubio V, J Mol Biol. 2000 Jun 2;299(2):463-76. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10860751 10860751]
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<ref group="xtra">PMID:10860751</ref><references group="xtra"/>
[[Category: Carbamate kinase]]
[[Category: Carbamate kinase]]
[[Category: Pyrococcus furiosus]]
[[Category: Pyrococcus furiosus]]
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[[Category: Single protein]]
 
[[Category: Fita, I.]]
[[Category: Fita, I.]]
[[Category: Marina, A.]]
[[Category: Marina, A.]]
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[[Category: Pyrococcus furiosus]]
[[Category: Pyrococcus furiosus]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:58:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 20:45:19 2009''

Revision as of 18:45, 17 February 2009

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

About this Structure

1E19 is a 2 chains structure of sequences from Pyrococcus furiosus. Full crystallographic information is available from OCA.

Reference

  • 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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