1n2n
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Crystal structure of cyanide complex of the oxygenase domain of inducible nitric oxide synthase.
OverviewOverview
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.
About this StructureAbout this Structure
1N2N is a Single protein structure of sequence from Mus musculus with CYN, ZN, HEM, H4B and ARG as ligands. Active as Nitric-oxide synthase, with EC number 1.14.13.39 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
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