3agc

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[[Image:3agc.png|left|200px]]
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{{STRUCTURE_3agc| PDB=3agc | SCENE= }}
{{STRUCTURE_3agc| PDB=3agc | SCENE= }}
===F218V mutant of the substrate-bound red chlorophyll catabolite reductase from Arabidopsis thaliana===
===F218V mutant of the substrate-bound red chlorophyll catabolite reductase from Arabidopsis thaliana===
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{{ABSTRACT_PUBMED_20727901}}
{{ABSTRACT_PUBMED_20727901}}
==About this Structure==
==About this Structure==
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3AGC is a 2 chains structure with sequences 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=3AGC OCA].
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[[3agc]] 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=3AGC OCA].
==Reference==
==Reference==
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<ref group="xtra">PMID:20727901</ref><references group="xtra"/>
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<ref group="xtra">PMID:020727901</ref><references group="xtra"/>
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
[[Category: Red chlorophyll catabolite reductase]]
[[Category: Red chlorophyll catabolite reductase]]
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[[Category: Substrate-bound enzyme]]
[[Category: Substrate-bound enzyme]]
[[Category: Transit peptide]]
[[Category: Transit peptide]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 1 09:47:00 2010''
 

Revision as of 23:09, 7 January 2013

Template:STRUCTURE 3agc

F218V mutant of the substrate-bound red chlorophyll catabolite reductase from Arabidopsis thaliana

Template:ABSTRACT PUBMED 20727901

About this Structure

3agc is a 2 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.

Reference

  • Sugishima M, Okamoto Y, Noguchi M, Kohchi T, Tamiaki H, Fukuyama K. Crystal Structures of the Substrate-Bound Forms of Red Chlorophyll Catabolite Reductase: Implications for Site-Specific and Stereospecific Reaction. J Mol Biol. 2010 Aug 19. PMID:20727901 doi:10.1016/j.jmb.2010.08.021

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