› 1m9j

X-ray diffraction
2.43Å resolution

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:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151512 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nitric oxide synthase 3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 415 amino acids
Theoretical weight: 46.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P29474 (Residues: 67-481; Coverage: 35%)
Gene name: NOS3
Sequence domains: Nitric oxide synthase, oxygenase domain
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM
2 bound ligands:
Ligand ZN 1 x ZN
Ligand CLW 2 x CLW
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P212121
Unit cell:
a: 71.071Å b: 89.891Å c: 155.833Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.216 0.272
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Developing master keys to brain pathology, cancer and aging from the structural biology of proteins controlling reactive oxygen species and DNA repair.
Perry et al. (2007)
3 more

11 mentions without citation

Statistical analysis of interface similarity in crystals of homologous proteins.
Xu et al. (2008)
10 more