1QW5
Murine inducible nitric oxide synthase oxygenase domain in complex with W1400 inhibitor.
Summary for 1QW5
| Entry DOI | 10.2210/pdb1qw5/pdb |
| Related | 1NOD 1QW4 1QW6 |
| Descriptor | Nitric oxide synthase, inducible, ZINC ION, PROTOPORPHYRIN IX CONTAINING FE, ... (6 entities in total) |
| Functional Keywords | murine inosoxy inhibitor complex, oxidoreductase |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 2 |
| Total formula weight | 99197.11 |
| Authors | Fedorov, R.,Hartmann, E.,Ghosh, D.K.,Schlichting, I. (deposition date: 2003-08-31, release date: 2003-12-09, Last modification date: 2023-08-16) |
| Primary citation | Fedorov, R.,Hartmann, E.,Ghosh, D.K.,Schlichting, I. Structural basis for the specificity of the nitric-oxide synthase inhibitors W1400 and Nomega-propyl-L-Arg for the inducible and neuronal isoforms. J.Biol.Chem., 278:45818-45825, 2003 Cited by PubMed Abstract: The high level of amino acid conservation and structural similarity in the immediate vicinity of the substrate binding sites of the oxygenase domains of the nitric-oxide synthase (NOS) isoforms (eNOSoxy, iNOSoxy, and nNOSoxy) make the interpretation of the structural basis of inhibitor isoform specificity a challenge and provide few clues for the design of new selective compounds. Crystal structures of iNOSoxy and nNOSoxy complexed with the inhibitors W1400 and Nomega-propyl-l-arginine provide a rationale for their isoform specificity. It involves differences outside the immediate active site as well as a conformational flexibility in the active site that allows the adoption of distinct conformations in response to interactions with the inhibitors. This flexibility is determined by isoform-specific residues outside the active site. PubMed: 12954642DOI: 10.1074/jbc.M306030200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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