CATH Classification

Domain Context

CATH Clusters

Superfamily Nitric Oxide Synthase; Chain A, domain 1
Functional Family

Enzyme Information

1.14.13.39
Nitric-oxide synthase (NADPH).
based on mapping to UniProt P29477
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)

P29477
NOS2_MOUSE
Mus musculus
Nitric oxide synthase, inducible

PDB Structure

PDB 2Y37
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
The Discovery of Novel, Potent and Highly Selective Inhibitors of Inducible Nitric Oxide Synthase (Inos).
Cheshire, D.R., Berg, A., Andersson, G.M., Andrews, G., Beaton, H.G., Birkinshaw, T.N., Boughton-Smith, N., Connolly, S., Cook, T.R., Cooper, A., Cooper, S.L., Cox, D., Dixon, J., Gensmantel, N., Hamley, P.J., Harrison, R., Hartopp, P., Kack, H., Leeson, P.D., Luker, T., Mete, A., Millichip, I., Nicholls, D.J., Pimm, A.D., St-Gallay, S.A., Wallace, A.V.
Bioorg.Med.Chem.Lett.
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