› 3k5r

X-ray diffraction
2Å resolution

Crystal Structure of mouse T-cadherin EC1 EC2

Released:
DOI: 10.2210/pdb3k5r/pdb
PDB entry 3k5r coloured by chain, front view.
PDB entry 3k5r coloured by chain, side view.
PDB entry 3k5r coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
T-cadherin structures reveal a novel adhesive binding mechanism.
Ciatto C, Bahna F, Zampieri N, VanSteenhouse HC, Katsamba PS, Ahlsen G, Harrison OJ, Brasch J, Jin X, Posy S, Vendome J, Ranscht B, Jessell TM, Honig B, Shapiro L
Nat Struct Mol Biol 17 339-47 (2010)
PMID: 20190755

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194381 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cadherin-13 Chains: A, B
Molecule details ›
Chains: A, B
Length: 218 amino acids
Theoretical weight: 23.9 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WTR5 (Residues: 140-355; Coverage: 31%)
Gene name: Cdh13
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: APS BEAMLINE 31-ID
Spacegroup: R32
Unit cell:
a: 107.716Å b: 107.716Å c: 226.698Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.215 0.213 0.259
Expression system: Escherichia coli

Quick links

Citations

15 review citations

Thinking outside the cell: how cadherins drive adhesion.
Brasch et al. (2012)
14 more

1 mention without citation

T-cadherin structures reveal a novel adhesive binding mechanism.
Ciatto et al. (2010)