2rcm: Difference between revisions

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==About this Structure==
==About this Structure==
2RCM is a [[Single protein]] structure of 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=2RCM OCA].  
2RCM is a 2 chains structure of 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=2RCM OCA].  


==Reference==
==Reference==
Structural insights into the evolutionary paths of oxylipin biosynthetic enzymes., Lee DS, Nioche P, Hamberg M, Raman CS, Nature. 2008 Sep 18;455(7211):363-8. Epub 2008 Aug 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18716621 18716621]
<ref group="xtra">PMID:18716621</ref><references group="xtra"/>
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
[[Category: Hydroperoxide dehydratase]]
[[Category: Hydroperoxide dehydratase]]
[[Category: Single protein]]
[[Category: Lee, D S.]]
[[Category: Lee, D S.]]
[[Category: Nioche, P.]]
[[Category: Nioche, P.]]
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[[Category: Transit peptide]]
[[Category: Transit peptide]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct  1 21:40:55 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 21:09:08 2009''

Revision as of 22:09, 16 February 2009

File:2rcm.png

Template:STRUCTURE 2rcm

Crystal Structure of Arabidopsis thaliana Allene Oxide Synthase variant (F137L) (At-AOS(F137L), cytochrome P450 74A) at 1.73 A ResolutionCrystal Structure of Arabidopsis thaliana Allene Oxide Synthase variant (F137L) (At-AOS(F137L), cytochrome P450 74A) at 1.73 A Resolution

Template:ABSTRACT PUBMED 18716621

About this StructureAbout this Structure

2RCM is a 2 chains structure of sequences from Arabidopsis thaliana. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1]

  1. Lee DS, Nioche P, Hamberg M, Raman CS. Structural insights into the evolutionary paths of oxylipin biosynthetic enzymes. Nature. 2008 Sep 18;455(7211):363-8. Epub 2008 Aug 20. PMID:18716621 doi:10.1038/nature07307

Page seeded by OCA on Mon Feb 16 21:09:08 2009

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