PDBe 2omz

X-ray diffraction
1.6Å resolution

Crystal structure of InlA Y369A/hEC1 complex

Released:
Primary publication:
Thermodynamically reengineering the listerial invasion complex InlA/E-cadherin.
Proc. Natl. Acad. Sci. U.S.A. 104 13960-5 (2007)
PMID: 17715295

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Internalin-A Chain: A
Molecule details ›
Chain: A
Length: 466 amino acids
Theoretical weight: 50.13 KDa
Source organism: Listeria monocytogenes EGD-e
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P0DJM0 (Residues: 36-495; Coverage: 60%)
Gene names: inlA, lmo0433
Sequence domains:
Structure domains:
Cadherin-1 Chain: B
Molecule details ›
Chain: B
Length: 105 amino acids
Theoretical weight: 11.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P12830 (Residues: 156-254; Coverage: 12%)
Gene names: CDH1, CDHE, UVO
Sequence domains: Cadherin domain
Structure domains: Cadherins

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: P212121
Unit cell:
a: 55.323Å b: 84.741Å c: 108.416Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.155 0.153 0.186
Expression system: Escherichia coli BL21