› 1f20

X-ray diffraction
1.9Å resolution

CRYSTAL STRUCTURE OF RAT NEURONAL NITRIC-OXIDE SYNTHASE FAD/NADP+ DOMAIN AT 1.9A RESOLUTION.

Released:
DOI: 10.2210/pdb1f20/pdb
PDB entry 1f20 coloured by chain, front view.
PDB entry 1f20 coloured by chain, side view.
PDB entry 1f20 coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Crystal structure of the FAD/NADPH-binding domain of rat neuronal nitric-oxide synthase. Comparisons with NADPH-cytochrome P450 oxidoreductase.
Zhang J, Martàsek P, Paschke R, Shea T, Siler Masters BS, Kim JJ
J Biol Chem 276 37506-13 (2001)
PMID: 11473123

Function and Biology Details

Reaction catalysed: 
(1a) 2 L-arginine + 2 NADPH + 2 O(2) = 2 N(omega)-hydroxy-L-arginine + 2 NADP(+) + 2 H(2)O
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151516 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nitric oxide synthase 1 Chain: A
Molecule details ›
Chain: A
Length: 435 amino acids
Theoretical weight: 49.73 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P29476 (Residues: 963-1397; Coverage: 30%)
Gene names: Bnos, Nos1
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAP 1 x NAP
3 bound ligands:
Ligand FAD 1 x FAD
Ligand GOL 5 x GOL
Ligand FMT 3 x FMT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P212121
Unit cell:
a: 59.07Å b: 64.37Å c: 159.43Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.186 0.206
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Structural and mechanistic aspects of flavoproteins: electron transfer through the nitric oxide synthase flavoprotein domain.
Stuehr et al. (2009)
10 more

11 mentions without citation

S-glutathionylation reshapes our understanding of endothelial nitric oxide synthase uncoupling and nitric oxide/reactive oxygen species-mediated signaling.
Zweier et al. (2011)
10 more