› 3nos

X-ray diffraction
2.4Å resolution

HUMAN ENDOTHELIAL NITRIC OXIDE SYNTHASE WITH ARGININE SUBSTRATE

Released:
DOI: 10.2210/pdb3nos/pdb
PDB entry 3nos coloured by chain, front view.
PDB entry 3nos coloured by chain, side view.
PDB entry 3nos coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural characterization of nitric oxide synthase isoforms reveals striking active-site conservation.
Fischmann TO, Hruza A, Niu XD, Fossetta JD, Lunn CA, Dolphin E, Prongay AJ, Reichert P, Lundell DJ, Narula SK, Weber PC
Nat Struct Biol 6 233-42 (1999)
PMID: 10074942

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 HEM 2 x HEM
3 bound ligands:
Ligand ZN 1 x ZN
Ligand HAR 2 x HAR
Ligand H4B 2 x H4B
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 68.859Å b: 93.264Å c: 156.117Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.193 0.308
Expression system: Escherichia coli

Quick links

Citations

50 review citations

Nitric oxide synthases: structure, function and inhibition.
Alderton et al. (2001)
49 more

29 mentions without citation

European contribution to the study of ROS: A summary of the findings and prospects for the future from the COST action BM1203 (EU-ROS).
Egea et al. (2017)
28 more