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4e1q
From Proteopedia
(Difference between revisions)
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{{STRUCTURE_4e1q| PDB=4e1q | SCENE= }} | {{STRUCTURE_4e1q| PDB=4e1q | SCENE= }} | ||
===Crystal structure of Wheat Cyclophilin A at 1.25 A resolution=== | ===Crystal structure of Wheat Cyclophilin A at 1.25 A resolution=== | ||
| + | {{ABSTRACT_PUBMED_23519664}} | ||
==Function== | ==Function== | ||
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==About this Structure== | ==About this Structure== | ||
[[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]. | [[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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| + | ==Reference== | ||
| + | <ref group="xtra">PMID:023519664</ref><references group="xtra"/><references/> | ||
[[Category: Peptidylprolyl isomerase]] | [[Category: Peptidylprolyl isomerase]] | ||
[[Category: Triticum aestivum]] | [[Category: Triticum aestivum]] | ||
Revision as of 11:15, 24 July 2013
Contents |
Crystal structure of Wheat Cyclophilin A at 1.25 A resolution
Template:ABSTRACT PUBMED 23519664
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.
Reference
- Sekhon SS, Kaur H, Dutta T, Singh K, Kumari S, Kang S, Park SG, Park BC, Jeong DG, Pareek A, Woo EJ, Singh P, Yoon TS. Structural and biochemical characterization of the cytosolic wheat cyclophilin TaCypA-1. Acta Crystallogr D Biol Crystallogr. 2013 Apr;69(Pt 4):555-63. doi:, 10.1107/S0907444912051529. Epub 2013 Mar 9. PMID:23519664 doi:10.1107/S0907444912051529
