› 1ff5

X-ray diffraction
2.93Å resolution

STRUCTURE OF E-CADHERIN DOUBLE DOMAIN

Released:
DOI: 10.2210/pdb1ff5/pdb
PDB entry 1ff5 coloured by chain, front view.
PDB entry 1ff5 coloured by chain, side view.
PDB entry 1ff5 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
A new crystal structure, Ca2+ dependence and mutational analysis reveal molecular details of E-cadherin homoassociation.
Pertz O, Bozic D, Koch AW, Fauser C, Brancaccio A, Engel J
EMBO J 18 1738-47 (1999)
PMID: 10202138

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140757 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cadherin-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 219 amino acids
Theoretical weight: 23.92 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P09803 (Residues: 157-374; Coverage: 25%)
Gene name: Cdh1
Sequence domains: Cadherin domain
Structure domains: Cadherins

Ligands and Environments

1 bound ligand:
Ligand CA 6 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELLIOTT GX-20
Spacegroup: P21
Unit cell:
a: 122.5Å b: 80.56Å c: 73.44Å
α: 90° β: 113.98° γ: 90°
R-values:
R R work R free
0.199 not available not available
Expression system: Escherichia coli

Quick links

Citations

56 review citations

Regulation of cadherin-mediated adhesion in morphogenesis.
Gumbiner BM. (2005)
55 more

20 mentions without citation

Proteolytic E-cadherin activation followed by solution NMR and X-ray crystallography.
Häussinger et al. (2004)
19 more