4fsk: Difference between revisions

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'''Unreleased structure'''
{{STRUCTURE_4fsk|  PDB=4fsk  |  SCENE=  }}
===Urate oxidase-azide complex in anaerobic conditions===
{{ABSTRACT_PUBMED_18638417}}


The entry 4fsk is ON HOLD  until Paper Publication
==Function==
[[http://www.uniprot.org/uniprot/URIC_ASPFL URIC_ASPFL]] Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.


Authors: Gabison, L., Colloc'H, N., El Hajji, M., Castro, B., Chiadmi, M., Prange, T.
==About this Structure==
[[4fsk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspergillus_flavus Aspergillus flavus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FSK OCA].  


Description: Urate oxidase-azide complex in anaerobic conditions
==Reference==
<ref group="xtra">PMID:018638417</ref><references group="xtra"/><references/>
[[Category: Aspergillus flavus]]
[[Category: Factor independent urate hydroxylase]]
[[Category: Castro, B.]]
[[Category: Chiadmi, M.]]
[[Category: Gabison, L.]]
[[Category: H, N Colloc.]]
[[Category: Hajji, M El.]]
[[Category: Prange, T.]]
[[Category: Degradation mechanism]]
[[Category: Homotetramer]]
[[Category: Inhibition]]
[[Category: Oxidoreductase]]
[[Category: Oxygen binding]]
[[Category: Peroxisome]]
[[Category: Purine metabolism]]

Revision as of 14:15, 3 July 2013

Template:STRUCTURE 4fsk

Urate oxidase-azide complex in anaerobic conditions

Template:ABSTRACT PUBMED 18638417

Function

[URIC_ASPFL] Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.

About this Structure

4fsk is a 1 chain structure with sequence from Aspergillus flavus. Full crystallographic information is available from OCA.

Reference

  1. Gabison L, Prange T, Colloc'h N, El Hajji M, Castro B, Chiadmi M. Structural analysis of urate oxidase in complex with its natural substrate inhibited by cyanide: mechanistic implications. BMC Struct Biol. 2008 Jul 20;8:32. PMID:18638417 doi:10.1186/1472-6807-8-32

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