X-ray diffraction
2.72Å resolution

Human vinculin (head domain, Vh1, residues 1-258) in complex with Shigella's IpaA vinculin binding site (residues 602-633)

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

Function and Biology Details

Structure analysis Details

Assemblies composition:
Non-polymer only dimer (preferred)
Non-polymer only dodecamer
Non-polymer only hexamer
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
  • Canonical: P18206 (Residues: 1-258; Coverage: 23%)
Gene name: VCL
Structure domains: Alpha-catenin/vinculin-like
Invasin IpaA Chain: B
Molecule details ›
Chain: B
Length: 30 amino acids
Theoretical weight: 3.31 KDa
Source organism: Shigella flexneri
Expression system: Escherichia coli
  • Canonical: P18010 (Residues: 602-631; Coverage: 5%)
Gene names: CP0125, ipaA
Sequence domains: SipA vinculin binding site

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: I4132
Unit cell:
a: 151.31Å b: 151.31Å c: 151.31Å
α: 90° β: 90° γ: 90°
R R work R free
0.232 0.229 0.291
Expression system: Escherichia coli