PDBe 5jro

X-ray diffraction
2.54Å resolution

The crystal structure of azoreductase from Yersinia pestis CO92 in its Apo form

Released:
Source organism: Yersinia pestis CO92
Entry authors: Tan K, Gu M, Kwon K, Anderson WF, Joachimiak A, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
FMN-dependent NADH-azoreductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 204 amino acids
Theoretical weight: 21.89 KDa
Source organism: Yersinia pestis CO92
Expression system: Escherichia coli
UniProt:
  • Canonical: NEW Q8ZE60 (Residues: 1-201; Coverage: 100%)
Gene names: YPO2323, YP_2110, azoR, y2010
Sequence domains: Flavodoxin-like fold
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2
Unit cell:
a: 124.257Å b: 45.135Å c: 72.699Å
α: 90° β: 112.84° γ: 90°
R-values:
R R work R free
0.202 0.2 0.249
Expression system: Escherichia coli