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1q5m

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[[Image:1q5m.png|left|200px]]
 
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{{STRUCTURE_1q5m| PDB=1q5m | SCENE= }}
{{STRUCTURE_1q5m| PDB=1q5m | SCENE= }}
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===Binary complex of rabbit 20alpha-hydroxysteroid dehydrogenase with NADPH===
===Binary complex of rabbit 20alpha-hydroxysteroid dehydrogenase with NADPH===
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{{ABSTRACT_PUBMED_15123423}}
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{{ABSTRACT_PUBMED_15123423}}
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==Function==
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[[http://www.uniprot.org/uniprot/PE2R_RABIT PE2R_RABIT]] Can convert prostaglandin E2 to prostaglandin F2-alpha.
==About this Structure==
==About this Structure==
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[[1q5m]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q5M OCA].
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[[1q5m]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q5M OCA].
==See Also==
==See Also==
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==Reference==
==Reference==
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<ref group="xtra">PMID:015123423</ref><references group="xtra"/>
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<ref group="xtra">PMID:015123423</ref><references group="xtra"/><references/>
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[[Category: Oryctolagus cuniculus]]
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[[Category: European rabbit]]
[[Category: Breton, R.]]
[[Category: Breton, R.]]
[[Category: Cantin, L.]]
[[Category: Cantin, L.]]

Revision as of 12:19, 20 November 2013

Template:STRUCTURE 1q5m

Contents

Binary complex of rabbit 20alpha-hydroxysteroid dehydrogenase with NADPH

Template:ABSTRACT PUBMED 15123423

Function

[PE2R_RABIT] Can convert prostaglandin E2 to prostaglandin F2-alpha.

About this Structure

1q5m is a 2 chain structure with sequence from European rabbit. Full crystallographic information is available from OCA.

See Also

Reference

  • Couture JF, Legrand P, Cantin L, Labrie F, Luu-The V, Breton R. Loop relaxation, a mechanism that explains the reduced specificity of rabbit 20alpha-hydroxysteroid dehydrogenase, a member of the aldo-keto reductase superfamily. J Mol Biol. 2004 May 21;339(1):89-102. PMID:15123423 doi:10.1016/j.jmb.2004.03.035

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