4jir: Difference between revisions

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'''Unreleased structure'''
{{STRUCTURE_4jir|  PDB=4jir  |  SCENE=  }}
===Crystal Structure Of Aldose Reductase (AKR1B1) Complexed With NADP+ And Epalrestat===
{{ABSTRACT_PUBMED_24100137}}


The entry 4jir is ON HOLD  until 00 0001
==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.


Authors: Zhang, L., Zheng, X., Zhang, H.., Zhao, Y., Chen, K., Zhai, J., Hu, X.
==About this Structure==
[[4jir]] 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=4JIR OCA].  


Description: Crystal Structure Of Aldose Reductase (AKR1B1) Complexed With NADP+ And Epalrestat
==Reference==
<ref group="xtra">PMID:024100137</ref><references group="xtra"/><references/>
[[Category: Aldehyde reductase]]
[[Category: Homo sapiens]]
[[Category: Chen, K.]]
[[Category: Hu, X.]]
[[Category: Zhai, J.]]
[[Category: Zhang, H..]]
[[Category: Zhang, L.]]
[[Category: Zhao, Y.]]
[[Category: Zheng, X.]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase-oxidoreductase inhibitor complex]]
[[Category: Tim barrel]]

Revision as of 06:48, 23 October 2013

Template:STRUCTURE 4jir

Crystal Structure Of Aldose Reductase (AKR1B1) Complexed With NADP+ And Epalrestat

Template:ABSTRACT PUBMED 24100137

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

4jir is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  1. Zhang L, Zhang H, Zhao Y, Li Z, Chen S, Zhai J, Chen Y, Xie W, Wang Z, Li Q, Zheng X, Hu X. Inhibitor selectivity between aldo-keto reductase superfamily members AKR1B10 and AKR1B1: Role of Trp112 (Trp111). FEBS Lett. 2013 Oct 4. pii: S0014-5793(13)00726-6. doi:, 10.1016/j.febslet.2013.09.031. PMID:24100137 doi:https://dx.doi.org/10.1016/j.febslet.2013.09.031

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