1n2n: Difference between revisions

Revision as of 12:12, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1n2n.png

Template:STRUCTURE 1n2n

Crystal structure of cyanide complex of the oxygenase domain of inducible nitric oxide synthase.Crystal structure of cyanide complex of the oxygenase domain of inducible nitric oxide synthase.

Template:ABSTRACT PUBMED 12464241

About this StructureAbout this Structure

1N2N is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of cyanide complexes of P450cam and the oxygenase domain of inducible nitric oxide synthase-structural models of the short-lived oxygen complexes., Fedorov R, Ghosh DK, Schlichting I, Arch Biochem Biophys. 2003 Jan 1;409(1):25-31. PMID:12464241

Page seeded by OCA on Mon Jul 28 12:12:38 2008

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

OCA

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-'''Crystal structure of cyanide complex of the oxygenase domain of inducible nitric oxide synthase.'''
+===Crystal structure of cyanide complex of the oxygenase domain of inducible nitric oxide synthase.===
-==Overview==
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-The crystal structure of the ternary cyanide complex of P450cam and camphor was determined to 1.8A resolution and found to be identical with the structure of the active oxygen complex [I. Schlichting et al., 2000, Science 287, 1615]. Notably, cyanide binds in a bent mode and induces the active conformation that is characterized by the presence of two water molecules and a flip of the carbonyl of the conserved Asp251. The structure of the ternary complex of cyanide, L-arginine, and the oxygenase domain of inducible nitric oxide synthase was determined to 2.4A resolution. Cyanide binds essentially linearly, interacts with L-Arg, and induces the binding of a water molecule at the active site. This water is positioned by backbone interactions, located 2.8A from the nitrogen atom of cyanide, and could provide a proton required for O-O bond scission in the hydroxylation reaction of nitric oxide synthase.
+The line below this paragraph, {{ABSTRACT_PUBMED_12464241}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_12464241}}
 ==About this Structure==
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 [[Category: Nitric oxide synthase]]
 [[Category: Oxygen complex analogue]]
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