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2c5a
From Proteopedia
(Difference between revisions)
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[[Image:2c5a.png|left|200px]] | [[Image:2c5a.png|left|200px]] | ||
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{{STRUCTURE_2c5a| PDB=2c5a | SCENE= }} | {{STRUCTURE_2c5a| PDB=2c5a | SCENE= }} | ||
| - | ===GDP-MANNOSE-3', 5'-EPIMERASE (ARABIDOPSIS THALIANA), Y174F, WITH GDP-BETA-L-GALACTOSE BOUND IN THE ACTIVE SITE=== | + | ===GDP-MANNOSE-3', 5' -EPIMERASE (ARABIDOPSIS THALIANA), Y174F, WITH GDP-BETA-L-GALACTOSE BOUND IN THE ACTIVE SITE=== |
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| - | (as it appears on PubMed at http://www.pubmed.gov), where 16366586 is the PubMed ID number. | ||
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{{ABSTRACT_PUBMED_16366586}} | {{ABSTRACT_PUBMED_16366586}} | ||
==About this Structure== | ==About this Structure== | ||
| - | + | [[2c5a]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C5A OCA]. | |
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| + | ==See Also== | ||
| + | *[[Temperature value vs. resolution|Temperature value vs. resolution]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:016366586</ref><references group="xtra"/> |
[[Category: Arabidopsis thaliana]] | [[Category: Arabidopsis thaliana]] | ||
[[Category: GDP-mannose 3,5-epimerase]] | [[Category: GDP-mannose 3,5-epimerase]] | ||
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[[Category: Short chain dehydratase/reductase]] | [[Category: Short chain dehydratase/reductase]] | ||
[[Category: Vitamin c]] | [[Category: Vitamin c]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 11:46:05 2009'' | ||
Revision as of 10:42, 6 January 2013
Contents |
GDP-MANNOSE-3', 5' -EPIMERASE (ARABIDOPSIS THALIANA), Y174F, WITH GDP-BETA-L-GALACTOSE BOUND IN THE ACTIVE SITE
Template:ABSTRACT PUBMED 16366586
About this Structure
2c5a is a 2 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.
See Also
Reference
- Major LL, Wolucka BA, Naismith JH. Structure and function of GDP-mannose-3',5'-epimerase: an enzyme which performs three chemical reactions at the same active site. J Am Chem Soc. 2005 Dec 28;127(51):18309-20. PMID:16366586 doi:10.1021/ja056490i
