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3rx3
From Proteopedia
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| - | [[Image:3rx3.png|left|200px]] | ||
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{{STRUCTURE_3rx3| PDB=3rx3 | SCENE= }} | {{STRUCTURE_3rx3| PDB=3rx3 | SCENE= }} | ||
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===Crystal Structure of Human Aldose Reductase Complexed with Sulindac=== | ===Crystal Structure of Human Aldose Reductase Complexed with Sulindac=== | ||
| + | {{ABSTRACT_PUBMED_22155003}} | ||
| + | ==Function== | ||
| + | [[http://www.uniprot.org/uniprot/ALDR_HUMAN ALDR_HUMAN]] Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. | ||
==About this Structure== | ==About this Structure== | ||
[[3rx3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RX3 OCA]. | [[3rx3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RX3 OCA]. | ||
| - | == | + | ==Reference== |
| - | + | <ref group="xtra">PMID:022155003</ref><references group="xtra"/><references/> | |
[[Category: Aldehyde reductase]] | [[Category: Aldehyde reductase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
Revision as of 10:16, 3 July 2013
Contents |
Crystal Structure of Human Aldose Reductase Complexed with Sulindac
Template:ABSTRACT PUBMED 22155003
Function
[ALDR_HUMAN] Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
About this Structure
3rx3 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Zheng X, Zhang L, Zhai J, Chen Y, Luo H, Hu X. The molecular basis for inhibition of sulindac and its metabolites towards human aldose reductase. FEBS Lett. 2012 Jan 2;586(1):55-9. Epub 2011 Dec 8. PMID:22155003 doi:10.1016/j.febslet.2011.11.023
