2O72: Crystal Structure Analysis of human E-cadherin

Crystal Structure Analysis of human E-cadherin (1-213). Determined by X-ray diffraction at 2.0 Å resolution. Released 9 Oct 2007.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Homo sapiens
Chains
1
Atoms
1,877
Mol. weight
23.34 kDa
Ligands
CA
Released
9 Oct 2007

Explore 2O72 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2O72 contains 4 α-helices and 19 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 4 helices, 19 β-strands

ElementResiduesLengthSheet
α-helix4-63
β-strand7-1041
β-strand19-2352
α-helix27-304
β-strand34-3961
β-strand4113
β-strand4513
β-strand51-5332
β-strand59-6242
β-strand73-82101
β-strand8711
β-strand92-9981
α-helix1001
β-strand107-10824
β-strand112-11875
α-helix121-1222
β-strand126-12946
β-strand132-13324
β-strand147-15485
β-strand163-16536
β-strand171-17446
β-strand186-19495
β-strand202-212115

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Epithelial-cadherinAprotein213Homo sapiensP12830 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2O72_1 Epithelial-cadherin (chains A)
DWVIPPISSPENEKGPFPKNLVQIKSNKDKEGKVFYSITGQGADTPPVGVFIIERETGWL
KVTEPLDRERIATYTLFSHAVSSNGNAVEDPMEILITVTDQNDNKPEFTQEVFKGSVMEG
ALPGTSVMEVTATDADDDVNTYNAAIAYTILSQDPELPDKNMFTINRNTGVISVVTTGLD
RESFPTYTLVVQAADLQGEGLSTTATAVITVTD

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa5

Primary citation

The Crystal Structure of Human E-cadherin Domains 1 and 2, and Comparison with other Cadherins in the Context of Adhesion Mechanism. Parisini, E., Higgins, J.M.G., Liu, J.-H. et al. J Mol Biol (2007) 373:401-411. DOI 10.1016/j.jmb.2007.08.011 · PubMed

Other PDB entries of the same protein (UniProt P12830 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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