spacer Structure of rat neuronal nitric oxide synthase heme domain in complex with 6,6'-((5-(3-aminopropyl)-1,3-phenylene)bis(ethane-2,1-diyl))bis(4-methylpyridin-2-amine)
UniProt
Accession P29476search
Name NOS1_RAT
Keywords 3D-structure, Complete proteome, Oxidoreductase, Iron, Metal-binding, Flavoprotein, Cell membrane, NADP, Ubl conjugation, FMN, Membrane, FAD, Heme, Alternative splicing, Calmodulin-binding, Reference proteome, Cell projection, Direct protein sequencing
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Polymers A B
 
Enzyme nomenclature
EC number 1.14.13.39 ExPASy BRENDA search
Polymers B, A
Name nitric-oxide synthase, nitric-oxide synthase (NADPH dependent)
Comment The enzyme in brain, but not that induced in lung or liver by endotoxin, requires Ca2+. The stoichiometry is not clear, but may involve a two-electron and a one-electron oxidation step.
Binds FAD, FMN, heme (iron protoporphyrin IX) and tetrahydrobiopterin. This eukaryotic enzyme, which is found in plants and animals [1-3], consists of oxygenase and reductase domains that 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. May produce superoxide under certain conditions. cf. EC 1.14.13.165, nitric-oxide synthase [NAD(P)H dependent].
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