CATH Classification

Domain Context

CATH Clusters

Superfamily Nitric Oxide Synthase; Chain A, domain 3
Functional Family Nitric oxide synthase, brain

Enzyme Information

1.14.13.39
Nitric-oxide synthase (NADPH).
based on mapping to UniProt P29474
2 L-arginine + 3 NADPH + 4 O(2) = 2 L-citrulline + 2 nitric oxide + 3 NADP(+) + 4 H(2)O.
-!- The enzyme consists of linked oxygenase and reductase domains. -!- The eukaryotic enzyme binds FAD, FMN, heme (iron protoporphyrin IX) and tetrahydrobiopterin, and its two domains are linked via a regulatory calmodulin-binding domain. -!- Upon calcium-induced calmodulin binding, the reductase and oxygenase domains form a complex, allowing electrons to flow from NADPH via FAD and FMN to the active center. -!- The reductase domain of the enzyme from the bacterium Sorangium cellulosum utilizes a [2Fe-2S] cluster to transfer the electrons from NADPH to the active center. -!- Cf. EC 1.14.14.47.

UniProtKB Entries (1)

P29474
NOS3_HUMAN
Homo sapiens
Nitric oxide synthase, endothelial

PDB Structure

PDB 3EAH
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Anchored plasticity opens doors for selective inhibitor design in nitric oxide synthase.
Garcin, E.D., Arvai, A.S., Rosenfeld, R.J., Kroeger, M.D., Crane, B.R., Andersson, G., Andrews, G., Hamley, P.J., Mallinder, P.R., Nicholls, D.J., St-Gallay, S.A., Tinker, A.C., Gensmantel, N.P., Mete, A., Cheshire, D.R., Connolly, S., Stuehr, D.J., Aberg, A., Wallace, A.V., Tainer, J.A., Getzoff, E.D.
Nat.Chem.Biol.