› 2fc1

X-ray diffraction
2Å resolution

Heme NO Complex in NOS

Released:
DOI: 10.2210/pdb2fc1/pdb
PDB entry 2fc1 coloured by chain, front view.
PDB entry 2fc1 coloured by chain, side view.
PDB entry 2fc1 coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Nitrosyl-heme structures of Bacillus subtilis nitric oxide synthase have implications for understanding substrate oxidation.
Pant K, Crane BR
Biochemistry 45 2537-44 (2006)
PMID: 16489746

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 domain:

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: 361 amino acids
Theoretical weight: 41.9 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: O34453 (Residues: 5-363; Coverage: 98%)
Gene names: BSU07630, nos, yflM
Sequence domains: Nitric oxide synthase, oxygenase domain
Structure domains:

Ligands and Environments


Cofactor: Ligand HBI 1 x HBI

Cofactor: Ligand HEM 1 x HEM
2 bound ligands:
Ligand NO 1 x NO
Ligand ARG 1 x ARG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P21212
Unit cell:
a: 80.009Å b: 93.517Å c: 62.768Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.26 0.232 0.26
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Bacterial nitric oxide synthases.
Crane et al. (2010)
5 more

3 mentions without citation

Active intermediates in heme monooxygenase reactions as revealed by cryoreduction/annealing, EPR/ENDOR studies.
Davydov et al. (2011)
2 more