6mjn

X-ray diffraction
1.75Å resolution

Crystal structure of an organic hydroperoxide resistance protein OsmC, predicted redox protein, regulator of sulfide bond formation from Legionella pneumophila

Released:
Source organism: Legionella pneumophila
Entry authors: Seattle Structural Genomics Center for Infectious Disease, Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-178638 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Organic hydroperoxide resistance protein OsmC, predicted redox protein, regulator of sulfide bond formation Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 147 amino acids
Theoretical weight: 15.75 KDa
Source organism: Legionella pneumophila
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5ZU37 (Residues: 1-139; Coverage: 100%)
Gene name: lpg1971
Sequence domains: OsmC-like protein
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P21
Unit cell:
a: 76.55Å b: 51.4Å c: 82.34Å
α: 90° β: 110.09° γ: 90°
R-values:
R R work R free
0.183 0.181 0.209
Expression system: Escherichia coli