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1mi3

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[[Image:1mi3.png|left|200px]]
 
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{{STRUCTURE_1mi3| PDB=1mi3 | SCENE= }}
{{STRUCTURE_1mi3| PDB=1mi3 | SCENE= }}
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===1.8 Angstrom structure of xylose reductase from Candida tenuis in complex with NAD===
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{{ABSTRACT_PUBMED_12733986}}
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===1.8 Angstrom structure of xylose reductase from Candida tenuis in complex with NADH===
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==Function==
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[[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.
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{{ABSTRACT_PUBMED_12733986}}
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==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].
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==See Also==
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*[[Group:SMART:2010 Pingry SMART Team Models|SMART:2010 Pingry SMART Team Models]]
==Reference==
==Reference==
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<ref group="xtra">PMID:012733986</ref><references group="xtra"/>
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<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

Contents

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

  • 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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