PDBe 1niw

X-ray diffraction
2.05Å resolution

Crystal structure of endothelial nitric oxide synthase peptide bound to calmodulin

Released:

Function and Biology Details

Reaction catalysed:
2 L-arginine + 3 NADPH + 4 O(2) = 2 L-citrulline + 2 nitric oxide + 3 NADP(+) + 4 H(2)O. 

Structure analysis Details

Assemblies composition:
hetero dimer
hetero octamer
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Calmodulin-1 Chains: A, C, E, G
Molecule details ›
Chains: A, C, E, G
Length: 148 amino acids
Theoretical weight: 17.14 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P0DP29 (Residues: 2-149; Coverage: 99%)
Gene names: CaMI, Calm, Calm1, Cam, Cam1
Structure domains: EF-hand
Nitric oxide synthase, endothelial Chains: B, D, F, H
Molecule details ›
Chains: B, D, F, H
Length: 20 amino acids
Theoretical weight: 2.18 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P29474 (Residues: 492-511; Coverage: 2%)
Gene name: NOS3

Ligands and Environments

3 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P21
Unit cell:
a: 68.521Å b: 73.952Å c: 71.142Å
α: 90° β: 111.4° γ: 90°
R-values:
R R work R free
0.223 0.223 0.249
Expression systems:
  • Escherichia coli
  • Not provided