1N2N
Crystal structure of cyanide complex of the oxygenase domain of inducible nitric oxide synthase.
Summary for 1N2N
| Entry DOI | 10.2210/pdb1n2n/pdb |
| Descriptor | Inducible Nitric Oxide Synthase, CYANIDE ION, ZINC ION, ... (7 entities in total) |
| Functional Keywords | nitric oxide synthase, cyanide complex, oxygen complex analogue, oxidoreductase |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 2 |
| Total formula weight | 99219.06 |
| Authors | Fedorov, R.,Ghosh, D.K.,Schlichting, I. (deposition date: 2002-10-23, release date: 2003-02-11, Last modification date: 2023-10-25) |
| Primary citation | Fedorov, R.,Ghosh, D.K.,Schlichting, I. Crystal structures of cyanide complexes of P450cam and the oxygenase domain of inducible nitric oxide synthase-structural models of the short-lived oxygen complexes Arch.Biochem.Biophys., 409:25-31, 2003 Cited by PubMed Abstract: 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. PubMed: 12464241DOI: 10.1016/S0003-9861(02)00555-6 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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