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4e1q

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'''Unreleased structure'''
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{{STRUCTURE_4e1q| PDB=4e1q | SCENE= }}
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===Crystal structure of Wheat Cyclophilin A at 1.25 A resolution===
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The entry 4e1q is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/Q93W25_WHEAT Q93W25_WHEAT]] PPIases accelerate the folding of proteins (By similarity).[RuleBase:RU000493] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).[RuleBase:RU004223]
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Authors: Sekhon, S.S., Jeong, D.G., Woo, E.J., Singh, P., Yoon, T.S.
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==About this Structure==
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[[4e1q]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E1Q OCA].
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Description: Crystal structure of Wheat Cyclophilin A at 1.25 A resolution
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[[Category: Peptidylprolyl isomerase]]
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[[Category: Triticum aestivum]]
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[[Category: Jeong, D G.]]
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[[Category: Sekhon, S S.]]
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[[Category: Singh, P.]]
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[[Category: Woo, E J.]]
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[[Category: Yoon, T S.]]
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[[Category: Isomerase]]

Revision as of 08:57, 27 March 2013

Template:STRUCTURE 4e1q

Crystal structure of Wheat Cyclophilin A at 1.25 A resolution

Function

[Q93W25_WHEAT] PPIases accelerate the folding of proteins (By similarity).[RuleBase:RU000493] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).[RuleBase:RU004223]

About this Structure

4e1q is a 1 chain structure with sequence from Triticum aestivum. Full crystallographic information is available from OCA.

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