› 1q1p

X-ray diffraction
3.2Å resolution

E-Cadherin activation

Released:
DOI: 10.2210/pdb1q1p/pdb
PDB entry 1q1p coloured by chain, front view.
PDB entry 1q1p coloured by chain, side view.
PDB entry 1q1p coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Proteolytic E-cadherin activation followed by solution NMR and X-ray crystallography.
Häussinger D, Ahrens T, Aberle T, Engel J, Stetefeld J, Grzesiek S
EMBO J 23 1699-708 (2004)
PMID: 15071499

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-140753 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cadherin-1 Chain: A
Molecule details ›
Chain: A
Length: 212 amino acids
Theoretical weight: 23.15 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P09803 (Residues: 158-369; Coverage: 25%)
Gene name: Cdh1
Sequence domains: Cadherin domain
Structure domains: Cadherins

Ligands and Environments

1 bound ligand:
Ligand CA 3 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELLIOTT GX-21
Spacegroup: C2
Unit cell:
a: 129.204Å b: 48.601Å c: 58.669Å
α: 90° β: 113.93° γ: 90°
R-values:
R R work R free
0.262 0.259 0.305
Expression system: Escherichia coli

Quick links

Citations

27 review citations

Structure and biochemistry of cadherins and catenins.
Shapiro et al. (2009)
26 more

18 mentions without citation

Protein crystallography for non-crystallographers, or how to get the best (but not more) from published macromolecular structures.
Wlodawer et al. (2008)
17 more