› 4uqs

X-ray diffraction
2.15Å resolution

Structure of Bacillus subtilis Nitric Oxide Synthase in complex with 3-Bromo-7-Nitroindazole

Released:
DOI: 10.2210/pdb4uqs/pdb
PDB entry 4uqs coloured by chain, front view.
PDB entry 4uqs coloured by chain, side view.
PDB entry 4uqs coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Identification of redox partners and development of a novel chimeric bacterial nitric oxide synthase for structure activity analyses.
Holden JK, Lim N, Poulos TL
J Biol Chem 289 29437-45 (2014)
PMID: 25194416

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:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
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: 41.79 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O34453 (Residues: 1-363; Coverage: 100%)
Gene names: BSU07630, nos, yflM
Sequence domains: Nitric oxide synthase, oxygenase domain
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 1 x HEM
3 bound ligands:
Ligand CL 1 x CL
Ligand INE 1 x INE
Ligand PEG 1 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: P21212
Unit cell:
a: 80.42Å b: 94.53Å c: 63.227Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.231 0.229 0.283
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 citation in other articles

Nitric Oxide Synthase as a Target for Methicillin-Resistant Staphylococcus aureus.
Holden et al. (2015)
4 more

2 mentions without citation

Identification of redox partners and development of a novel chimeric bacterial nitric oxide synthase for structure activity analyses.
Holden et al. (2014)
1 more