CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.30 | Roll |
|
2.30.42 | Pdz3 Domain |
|
2.30.42.10 | PDZ domain |
Domain Context
CATH Clusters
| Superfamily | 2.30.42.10 |
| Functional Family | Nitric oxide synthase |
Enzyme Information
| 1.14.13.39 |
Nitric-oxide synthase (NADPH).
based on mapping to UniProt P29476
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 (2)
| Q61234 |
SNTA1_MOUSE
Mus musculus
Alpha-1-syntrophin
|
| P29476 |
NOS1_RAT
Rattus norvegicus
Nitric oxide synthase, brain
|
PDB Structure
| PDB | 4HOP |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Quantification of the transferability of a designed protein specificity switch reveals extensive epistasis in molecular recognition.
Proc.Natl.Acad.Sci.USA
|
