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  Domain Name: Nitric_oxide_synthas
The ferredoxin-reductase (FNR) like C-terminal domain of the nitric oxide synthase (NOS) fuses with a heme-containing N-terminal oxidase domain. The reductase portion is similar in structure to NADPH dependent cytochrome-450 reductase (CYPOR), having an inserted connecting sub-domain within the FAD binding portion of FNR. NOS differs from CYPOR in a requirement for the cofactor tetrahydrobiopterin and unlike most CYPOR is dimeric. Nitric oxide synthase produces nitric oxide in the conversion of L-arginine to L-citruline. NOS has been implicated in a variety of processes including cytotoxicity, anti-inflamation, neurotransmission, and vascular smooth muscle relaxation.
No pairwise interactions are available for this conserved domain.

Total Mutations Found: 32
Total Disease Mutations Found: 11
This domain occurred 6 times on human genes (17 proteins).



  ANTLEY-BIXLER SYNDROME WITH GENITAL ANOMALIES AND DISORDERED STEROIDOGENESIS
  DISORDERED STEROIDOGENESIS DUE TO CYTOCHRO
  DISORDERED STEROIDOGENESIS DUE TO CYTOCHROME P450 OXIDOREDUCTASE DEFICIENCY
  HOMOCYSTINURIA-MEGALOBLASTIC ANEMIA, CBLE COMPLEMENTATION TYPE


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Range on the Protein:  

   Protein ID            Protein Position

Domain Position:  


Feature Name:Total Found:
FAD binding pocket
NAD binding pocket
dimerization interface
catalytic residues
FAD binding motif
phosphate binding motif
beta-alpha-beta structure



















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Please Cite: Peterson, T.A., Adadey, A., Santana-Cruz ,I., Sun, Y., Winder A, Kann, M.G., (2010) DMDM: Domain Mapping of Disease Mutations. Bioinformatics 26 (19), 2458-2459.

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