CATH Classification
| Level | CATH Code | Description | 
|---|---|---|
 
	 | 
    3 | Alpha Beta | 
 
	 | 
    3.90 | Alpha-Beta Complex | 
 
	 | 
    3.90.440 | Nitric Oxide Synthase;Heme Domain; Chain A, domain 2 | 
 
	 | 
    3.90.440.10 | Nitric Oxide Synthase;Heme Domain;Chain A domain 2 | 
Domain Context
CATH Clusters
| Superfamily | Nitric Oxide Synthase;Heme Domain;Chain A domain 2 | 
| Functional Family | Endothelial nitric oxide synthase | 
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 | 3NOS | 
| External Links | |
| Method | X-RAY DIFFRACTION | 
| Organism | Escherichia | 
| Primary Citation | 
					 Structural characterization of nitric oxide synthase isoforms reveals striking active-site conservation. 
					    
					    Nat.Struct.Biol. 
					    
					 | 
			
