1dwk
From Proteopedia
(Difference between revisions)
m (Protected "1dwk" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1dwk.png|left|200px]] | ||
| - | |||
| - | <!-- | ||
| - | The line below this paragraph, containing "STRUCTURE_1dwk", creates the "Structure Box" on the page. | ||
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet) | ||
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | ||
| - | or leave the SCENE parameter empty for the default display. | ||
| - | --> | ||
{{STRUCTURE_1dwk| PDB=1dwk | SCENE= }} | {{STRUCTURE_1dwk| PDB=1dwk | SCENE= }} | ||
| - | |||
===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== | |
| - | + | [[http://www.uniprot.org/uniprot/CYNS_ECOLI CYNS_ECOLI]] Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide. | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
==About this Structure== | ==About this Structure== | ||
| Line 22: | Line 10: | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:010801492</ref>< | + | <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
Contents |
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
- 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
