1mi3
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | [[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}} | ||
| - | === | + | ==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. | |
| - | + | ||
==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
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
