X-ray diffraction
2.14Å resolution

Structure of Nitric Oxide Synthase Heme Protein from Bacillus Subtilis with N-Hydroxy-Arginine and Tetrahydrofolate Bound

Source organism: Bacillus subtilis
Primary publication:
Structure of a nitric oxide synthase heme protein from Bacillus subtilis.
Biochemistry 41 11071-9 (2002)
PMID: 12220171

Function and Biology Details

Reaction catalysed:
(1a) 2 L-arginine + 2 reduced flavodoxin + 2 O(2) = 2 N(omega)-hydroxy-L-arginine + 2 oxidized flavodoxin + 2 H(2)O
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Nitric oxide synthase oxygenase Chain: A
Molecule details ›
Chain: A
Length: 361 amino acids
Theoretical weight: 41.9 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21(DE3)
  • Canonical: O34453 (Residues: 5-363; Coverage: 98%)
Gene names: BSU07630, nos, yflM
Structure domains:

Ligands and Environments

Cofactor: Ligand THG 1 x THG

Cofactor: Ligand HEM 1 x HEM
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P21212
Unit cell:
a: 81.085Å b: 93.068Å c: 62.769Å
α: 90° β: 90° γ: 90°
R R work R free
0.212 0.212 0.239
Expression system: Escherichia coli BL21(DE3)