PDBe 2hsq

X-ray diffraction
3.97Å resolution

Human vinculin (head domain, Vh1, residues 1-258) in complex with Shigella's IpaA vinculin binding site 2 (residues 565-587)

Released:
Source organisms:
Primary publication:
Shigella applies molecular mimicry to subvert vinculin and invade host cells.
OpenAccess logo J. Cell Biol. 175 465-75 (2006)
PMID: 17088427

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero 48-mer
hetero 12-mer
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Vinculin Chain: A
Molecule details ›
Chain: A
Length: 266 amino acids
Theoretical weight: 30.03 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P18206 (Residues: 1-258; Coverage: 23%)
Gene name: VCL
Structure domains: Four Helix Bundle (Hemerythrin (Met), subunit A)
Invasin Chain: B
Molecule details ›
Chain: B
Length: 23 amino acids
Theoretical weight: 2.5 KDa
Source organism: Shigella flexneri
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6XVZ2 (Residues: 565-587; Coverage: 4%)
Gene names: CBW45_05635, ipaA

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: I432
Unit cell:
a: 203.17Å b: 203.17Å c: 203.17Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.289 0.286 0.316
Expression system: Escherichia coli