X-ray diffraction
2.3Å resolution

Structure of the C-terminal SpoA domain of Shigella flexneri Spa33


Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Surface presentation of antigens protein SpaO Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 86 amino acids
Theoretical weight: 9.88 KDa
Source organism: Shigella flexneri
Expression system: Escherichia coli B
  • Canonical: P0A1K9 (Residues: 208-293; Coverage: 29%)
Gene names: CP0152, spa33, spaO
Sequence domains: Type III flagellar switch regulator (C-ring) FliN C-term
Structure domains: SpoA-like

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P21
Unit cell:
a: 51.3Å b: 27.82Å c: 104.44Å
α: 90° β: 90.03° γ: 90°
R R work R free
0.177 0.174 0.21
Expression system: Escherichia coli B