1jfc: Difference between revisions

Revision as of 20:09, 1 July 2008

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File:1jfc.png

Template:STRUCTURE 1jfc

X-ray structure of nitric oxide reductase (cytochrome P450nor) in the ferrous CO state at atomic resolutionX-ray structure of nitric oxide reductase (cytochrome P450nor) in the ferrous CO state at atomic resolution

Template:ABSTRACT PUBMED 11752781

About this StructureAbout this Structure

1JFC is a Single protein structure of sequence from Fusarium oxysporum. Full crystallographic information is available from OCA.

ReferenceReference

X-ray structure of nitric oxide reductase (cytochrome P450nor) at atomic resolution., Shimizu H, Park SY, Shiro Y, Adachi S, Acta Crystallogr D Biol Crystallogr. 2002 Jan;58(Pt 1):81-9. Epub 2001 Dec, 21. PMID:11752781

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''X-ray structure of nitric oxide reductase (cytochrome P450nor) in the ferrous CO state at atomic resolution'''
+===X-ray structure of nitric oxide reductase (cytochrome P450nor) in the ferrous CO state at atomic resolution===
-==Overview==
+<!--
-Crystal structures of the nitric oxide reductase cytochrome P450nor (P450nor) in the ferric resting and the ferrous carbonmonoxy (CO) states have been determined at 1.00 and 1.05 A resolution, respectively. P450nor consists of 403 amino-acid residues (46 kDa) and is one of the largest proteins refined to this resolution so far. The final models have conventional R factors of 10.2% (ferric resting) and 11.7% (ferrous CO), with mean coordinate errors of 0.028 (ferric resting) and 0.030 A (ferrous CO) as calculated from inversion of the full positional least-squares matrix. Owing to the atomic resolution, novel features are found in the refined structures. Firstly, two orientations of the haem are observed both in the ferric resting and the ferrous CO states. Secondly, a disordered water molecule bound to the haem iron is found in the ferric resting state. In addition, the accurate structures at atomic resolution enabled the examination of general stereochemical parameters that are commonly used in refinement cycles of protein structures.
+The line below this paragraph, {{ABSTRACT_PUBMED_11752781}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_11752781}}
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 [[Category: Rsgi]]
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