CATH Classification

Domain Context

CATH Clusters

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

Enzyme Information

1.14.13.39
Nitric-oxide synthase (NADPH).
based on mapping to UniProt P29473
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)

P29473
NOS3_BOVIN
Bos taurus
Nitric oxide synthase, endothelial

PDB Structure

PDB 1DMK
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Structural basis for pterin antagonism in nitric-oxide synthase. Development of novel 4-oxo-pteridine antagonists of (6R)-5,6,7,8-tetrahydrobiopterin
Kotsonis, P., Frohlich, L.G., Raman, C.S., Li, H., Berg, M., Gerwig, R., Groehn, V., Kang, Y., Al-Masoudi, N., Taghavi-Moghadam, S., Mohr, D., Munch, U., Schnabel, J., Martasek, P., Masters, B.S., Strobel, H., Poulos, T., Matter, H., Pfleiderer, W., Schmidt, H.H.
J.Biol.Chem.
CATH-Gene3D is a Global Biodata Core Resource Learn more...