Structure analysis

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

X-ray diffraction
2.3Å resolution
Source organism: Shigella flexneri
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 8225.22 Å2
Buried surface area: 4692.7 Å2
Dissociation area: 2,305.37 Å2
Dissociation energy (ΔGdiss): 34.06 kcal/mol
Dissociation entropy (TΔSdiss): 11.21 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-141011
Assembly 2
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Multimeric state: homo dimer
Accessible surface area: 7956.85 Å2
Buried surface area: 4971.74 Å2
Dissociation area: 2,358.44 Å2
Dissociation energy (ΔGdiss): 28.36 kcal/mol
Dissociation entropy (TΔSdiss): 11.55 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-141011

Macromolecules

Chains: A, B, C, D
Length: 86 amino acids
Theoretical weight: 9.88 KDa
Source organism: Shigella flexneri
Expression system: Escherichia coli B
UniProt:
  • Canonical: P0A1K9 (Residues: 208-293; Coverage: 29%)
Gene names: CP0152, spa33, spaO
Pfam: Type III flagellar switch regulator (C-ring) FliN C-term
InterPro:
CATH: SpoA-like

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