› 3e7s

X-ray diffraction
2.5Å 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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151509 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Nitric oxide synthase 3 Chain: A
Molecule details ›
Chain: A
Length: 431 amino acids
Theoretical weight: 48.39 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: P29473 (Residues: 57-487; Coverage: 36%)
Gene name: NOS3
Sequence domains: Nitric oxide synthase, oxygenase domain
Structure domains:
Nitric oxide synthase 3 Chain: B
Molecule details ›
Chain: B
Length: 431 amino acids
Theoretical weight: 48.5 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: P29473 (Residues: 57-487; Coverage: 36%)
Gene name: NOS3
Sequence domains: Nitric oxide synthase, oxygenase domain
Structure domains:

Ligands and Environments


Cofactor: Ligand HEC 2 x HEC
2 bound ligands:
Ligand ZN 1 x ZN
Ligand AT2 4 x AT2
1 modified residue:
Ligand CAS 1 x CAS

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P212121
Unit cell:
a: 58.93Å b: 104.37Å c: 156.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.212 0.254
Expression system: Escherichia coli

Quick links

Citations

15 review citations

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

3 mentions without citation

Nitric oxide synthase and structure-based inhibitor design.
Poulos et al. (2017)
2 more