1mi3: Difference between revisions

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[[Image:1mi3.png|left|200px]]
{{STRUCTURE_1mi3|  PDB=1mi3  |  SCENE=  }}  
{{STRUCTURE_1mi3|  PDB=1mi3  |  SCENE=  }}  
===1.8 Angstrom structure of xylose reductase from Candida tenuis in complex with NAD===
{{ABSTRACT_PUBMED_12733986}}


===1.8 Angstrom structure of xylose reductase from Candida tenuis in complex with NADH===
==Function==
 
[[http://www.uniprot.org/uniprot/XYL1_CANTE XYL1_CANTE]] Reduces D-xylose into xylitol. Has a preference for NADPH, but can also utilize NADH as cosubstrate.
{{ABSTRACT_PUBMED_12733986}}


==About this Structure==
==About this Structure==
[[1mi3]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Candida_tenuis Candida tenuis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MI3 OCA].  
[[1mi3]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Candida_tenuis Candida tenuis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MI3 OCA].  
==See Also==
*[[Group:SMART:2010 Pingry SMART Team Models|SMART:2010 Pingry SMART Team Models]]


==Reference==
==Reference==
<ref group="xtra">PMID:012733986</ref><references group="xtra"/>
<ref group="xtra">PMID:012733986</ref><references group="xtra"/><references/>
[[Category: Aldehyde reductase]]
[[Category: Aldehyde reductase]]
[[Category: Candida tenuis]]
[[Category: Candida tenuis]]

Revision as of 06:30, 6 November 2013

Template:STRUCTURE 1mi3

1.8 Angstrom structure of xylose reductase from Candida tenuis in complex with NAD

Template:ABSTRACT PUBMED 12733986

Function

[XYL1_CANTE] Reduces D-xylose into xylitol. Has a preference for NADPH, but can also utilize NADH as cosubstrate.

About this Structure

1mi3 is a 4 chain structure with sequence from Candida tenuis. Full crystallographic information is available from OCA.

See Also

Reference

  1. Kavanagh KL, Klimacek M, Nidetzky B, Wilson DK. Structure of xylose reductase bound to NAD+ and the basis for single and dual co-substrate specificity in family 2 aldo-keto reductases. Biochem J. 2003 Jul 15;373(Pt 2):319-26. PMID:12733986 doi:10.1042/BJ20030286

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