4NOS
HUMAN INDUCIBLE NITRIC OXIDE SYNTHASE WITH INHIBITOR
Summary for 4NOS
| Entry DOI | 10.2210/pdb4nos/pdb |
| Related | 3NOS |
| Descriptor | INDUCIBLE NITRIC OXIDE SYNTHASE, ZINC ION, PROTOPORPHYRIN IX CONTAINING FE, ... (7 entities in total) |
| Functional Keywords | l-arginine monooxygenase, nitric oxide, human, zns4, oxidoreductase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 4 |
| Total formula weight | 201821.90 |
| Authors | Fischmann, T.O.,Weber, P.C. (deposition date: 1999-02-03, release date: 2000-02-04, Last modification date: 2023-12-27) |
| Primary citation | Fischmann, T.O.,Hruza, A.,Niu, X.D.,Fossetta, J.D.,Lunn, C.A.,Dolphin, E.,Prongay, A.J.,Reichert, P.,Lundell, D.J.,Narula, S.K.,Weber, P.C. Structural characterization of nitric oxide synthase isoforms reveals striking active-site conservation. Nat.Struct.Biol., 6:233-242, 1999 Cited by PubMed Abstract: Crystal structures of human endothelial nitric oxide synthase (eNOS) and human inducible NOS (iNOS) catalytic domains were solved in complex with the arginine substrate and an inhibitor S-ethylisothiourea (SEITU), respectively. The small molecules bind in a narrow cleft within the larger active-site cavity containing heme and tetrahydrobiopterin. Both are hydrogen-bonded to a conserved glutamate (eNOS E361, iNOS E377). The active-site residues of iNOS and eNOS are nearly identical. Nevertheless, structural comparisons provide a basis for design of isozyme-selective inhibitors. The high-resolution, refined structures of eNOS (2.4 A resolution) and iNOS (2.25 A resolution) reveal an unexpected structural zinc situated at the intermolecular interface and coordinated by four cysteines, two from each monomer. PubMed: 10074942DOI: 10.1038/6675 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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