CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.340 | Nitric Oxide Synthase; Chain A, domain 1 |
|
3.90.340.10 | Nitric Oxide Synthase; Chain A, domain 1 |
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 P35228
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)
| P35228 |
NOS2_HUMAN
Homo sapiens
Nitric oxide synthase, inducible
|
PDB Structure
| PDB | 1NSI |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structures of zinc-free and -bound heme domain of human inducible nitric-oxide synthase. Implications for dimer stability and comparison with endothelial nitric-oxide synthase.
J.Biol.Chem.
|
