› 3ebd

X-ray diffraction
2.4Å 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-541982 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nitric oxide synthase, inducible Chains: A, B
Molecule details ›
Chains: A, B
Length: 433 amino acids
Theoretical weight: 50.12 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P29477 (Residues: 66-498; Coverage: 38%)
Gene names: Inosl, Nos2
Sequence domains: Nitric oxide synthase, oxygenase domain
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM
3 bound ligands:
Ligand H4B 2 x H4B
Ligand 329 2 x 329
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P6122
Unit cell:
a: 213.44Å b: 213.44Å c: 116.109Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.215 0.215 0.248
Expression system: Escherichia coli

Quick links

Citations

16 review citations

The structural biochemistry of the superoxide dismutases.
Perry et al. (2010)
15 more

2 mentions without citation

Anchored plasticity opens doors for selective inhibitor design in nitric oxide synthase.
Garcin et al. (2008)
1 more