PDBe 2omx

X-ray diffraction
1.7Å resolution

Crystal structure of InlA S192N G194S+S/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):
InlA Chain: A
Molecule details ›
Chain: A
Length: 462 amino acids
Theoretical weight: 49.97 KDa
Source organism: Listeria monocytogenes EGD-e
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: A4GWL5 (Residues: 36-195, 196-496; Coverage: 60%)
Gene name: inlA
Sequence domains:
Structure domains:
Cadherin-1 Chain: B
Molecule details ›
Chain: B
Length: 108 amino acids
Theoretical weight: 11.87 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P12830 (Residues: 156-258; Coverage: 12%)
Gene names: CDH1, CDHE, UVO
Sequence domains: Cadherin domain
Structure domains: Cadherins

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P1
Unit cell:
a: 44.887Å b: 54.16Å c: 68.811Å
α: 74.75° β: 80.69° γ: 67.71°
R-values:
R R work R free
0.17 0.167 0.223
Expression system: Escherichia coli BL21