› 3eah

X-ray diffraction
2.44Å 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: 427 amino acids
Theoretical weight: 48.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P29474 (Residues: 66-492; Coverage: 36%)
Gene name: NOS3
Sequence domains: Nitric oxide synthase, oxygenase domain
Structure domains:

Ligands and Environments


Cofactor: Ligand HEC 2 x HEC
4 bound ligands:
Ligand ZN 1 x ZN
Ligand 327 2 x 327
Ligand MPD 4 x MPD
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P212121
Unit cell:
a: 71.09Å b: 90.15Å c: 156.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.213 0.258
Expression system: Escherichia coli

Quick links

Citations

16 review citations

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

7 mentions without citation

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