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2agt

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[[Image:2agt.png|left|200px]]
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{{STRUCTURE_2agt| PDB=2agt | SCENE= }}
{{STRUCTURE_2agt| PDB=2agt | SCENE= }}
===Aldose Reductase Mutant Leu 300 Pro complexed with Fidarestat===
===Aldose Reductase Mutant Leu 300 Pro complexed with Fidarestat===
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{{ABSTRACT_PUBMED_16134934}}
{{ABSTRACT_PUBMED_16134934}}
==About this Structure==
==About this Structure==
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2AGT is a 1 chain structure of 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=2AGT OCA].
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[[2agt]] is a 1 chain structure of [[Aldose Reductase]] 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=2AGT OCA].
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==See Also==
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*[[Aldose Reductase|Aldose Reductase]]
==Reference==
==Reference==
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<ref group="xtra">PMID:16134934</ref><references group="xtra"/>
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<ref group="xtra">PMID:016134934</ref><references group="xtra"/>
[[Category: Aldehyde reductase]]
[[Category: Aldehyde reductase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Nadp]]
[[Category: Nadp]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 12:51:47 2009''
 

Revision as of 17:35, 26 July 2012

Template:STRUCTURE 2agt

Contents

Aldose Reductase Mutant Leu 300 Pro complexed with Fidarestat

Template:ABSTRACT PUBMED 16134934

About this Structure

2agt is a 1 chain structure of Aldose Reductase with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

Reference

  • Petrova T, Steuber H, Hazemann I, Cousido-Siah A, Mitschler A, Chung R, Oka M, Klebe G, El-Kabbani O, Joachimiak A, Podjarny A. Factorizing selectivity determinants of inhibitor binding toward aldose and aldehyde reductases: structural and thermodynamic properties of the aldose reductase mutant Leu300Pro-fidarestat complex. J Med Chem. 2005 Sep 8;48(18):5659-65. PMID:16134934 doi:10.1021/jm050424+

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