1Q1P: E-Cadherin activation

E-Cadherin activation. Determined by X-ray diffraction at 3.2 Å resolution. Released 20 Apr 2004.

Method
X-ray diffraction
Resolution
3.2 Å
Organism
Mus musculus
Chains
1
Atoms
1,864
Mol. weight
23.27 kDa
Ligands
CA
Released
20 Apr 2004

Explore 1Q1P in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1Q1P contains 3 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: 3 helices, 19 β-strands

ElementResiduesLengthSheet
β-strand7-1041
β-strand19-2352
β-strand34-3961
β-strand5112
β-strand59-6242
β-strand73-82101
β-strand86-8721
α-helix90-912
β-strand92-9981
β-strand107-10823
β-strand112-11544
β-strand11815
β-strand126-12946
β-strand132-13323
α-helix142-1443
β-strand148-15254
β-strand163-16536
β-strand171-17446
β-strand188-19474
α-helix195-1984
β-strand202-20984
β-strand21215

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Epithelial-cadherinAprotein212Mus musculusP09803 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1Q1P_1 Epithelial-cadherin (chains A)
WVIPPISCPENEKGEFPKNLVQIKSNRDKETKVFYSITGQGADKPPVGVFIIERETGWLK
VTQPLDREAIAKYILYSHAVSSNGEAVEDPMEIVITVTDQNDNRPEFTQEVFEGSVAEGA
VPGTSVMKVSATDADDDVNTYNAAIAYTIVSQDPELPHKNMFTVNRDTGVISVLTSGLDR
ESYPTYTLVVQAADLQGEGLSTTAKAVITVKD

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa3

Primary citation

Proteolytic E-cadherin activation followed by solution NMR and X-ray crystallography. Haussinger, D., Ahrens, T., Aberle, T. et al. EMBO J (2004) 23:1699-1708. DOI 10.1038/sj.emboj.7600192 · PubMed

Other PDB entries of the same protein (UniProt P09803 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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