1m7v

X-ray diffraction
1.95Å resolution

STRUCTURE OF A NITRIC OXIDE SYNTHASE HEME PROTEIN FROM BACILLUS SUBTILIS WITH TETRAHYDROFOLATE AND ARGININE BOUND

Released:
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)
PDBe Complex ID:
PDB-CPX-128541 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nitric oxide synthase oxygenase Chain: A
Molecule details ›
Chain: A
Length: 363 amino acids
Theoretical weight: 42.1 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O34453 (Residues: 5-363; Coverage: 99%)
Gene names: BSU07630, nos, yflM
Sequence domains: Nitric oxide synthase, oxygenase domain
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 1 x HEM

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

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P21212
Unit cell:
a: 81.155Å b: 92.553Å c: 62.939Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.225 0.225 0.239
Expression system: Escherichia coli BL21(DE3)