3NOS

HUMAN ENDOTHELIAL NITRIC OXIDE SYNTHASE WITH ARGININE SUBSTRATE

Summary for 3NOS

• Entry DOI: 10.2210/pdb3nos/pdb
• Related: 4NOS
• Descriptor: ENDOTHELIAL NITRIC-OXIDE SYNTHASE, ZINC ION, N-OMEGA-HYDROXY-L-ARGININE, ... (6 entities in total)
• Functional Keywords: l-arginine monooxygenase, nitric oxide, human, zns4, oxidoreductase
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane: P29474
• Total number of polymer chains: 2
• Total formula weight: 98200.07

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

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: 10074942
DOI: 10.1038/6675

Experimental method

X-RAY DIFFRACTION (2.4 Å)