1dwk: Difference between revisions

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[[Image:1dwk.png|left|200px]]
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{{STRUCTURE_1dwk|  PDB=1dwk  |  SCENE=  }}  
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===STRUCTURE OF CYANASE WITH THE DI-ANION OXALATE BOUND AT THE ENZYME ACTIVE SITE===
===STRUCTURE OF CYANASE WITH THE DI-ANION OXALATE BOUND AT THE ENZYME ACTIVE SITE===
{{ABSTRACT_PUBMED_10801492}}


 
==Function==
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[[http://www.uniprot.org/uniprot/CYNS_ECOLI CYNS_ECOLI]] Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.  
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{{ABSTRACT_PUBMED_10801492}}


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
<ref group="xtra">PMID:010801492</ref><ref group="xtra">PMID:002822670</ref><ref group="xtra">PMID:003518792</ref><ref group="xtra">PMID:003651424</ref><ref group="xtra">PMID:006994799</ref><references group="xtra"/>
<ref group="xtra">PMID:010801492</ref><references group="xtra"/><references/>
[[Category: Cyanase]]
[[Category: Cyanase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]

Revision as of 10:29, 16 April 2014

Template:STRUCTURE 1dwk

STRUCTURE OF CYANASE WITH THE DI-ANION OXALATE BOUND AT THE ENZYME ACTIVE SITE

Template:ABSTRACT PUBMED 10801492

Function

[CYNS_ECOLI] Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.

About this Structure

1dwk is a 10 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

  1. Walsh MA, Otwinowski Z, Perrakis A, Anderson PM, Joachimiak A. Structure of cyanase reveals that a novel dimeric and decameric arrangement of subunits is required for formation of the enzyme active site. Structure. 2000 May 15;8(5):505-14. PMID:10801492

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