E-Cadherin activation. Determined by X-ray diffraction at 3.2 Å resolution. Released 20 Apr 2004.
Explore 1Q1P in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7-10 | 4 | 1 |
| β-strand | 19-23 | 5 | 2 |
| β-strand | 34-39 | 6 | 1 |
| β-strand | 51 | 1 | 2 |
| β-strand | 59-62 | 4 | 2 |
| β-strand | 73-82 | 10 | 1 |
| β-strand | 86-87 | 2 | 1 |
| α-helix | 90-91 | 2 | |
| β-strand | 92-99 | 8 | 1 |
| β-strand | 107-108 | 2 | 3 |
| β-strand | 112-115 | 4 | 4 |
| β-strand | 118 | 1 | 5 |
| β-strand | 126-129 | 4 | 6 |
| β-strand | 132-133 | 2 | 3 |
| α-helix | 142-144 | 3 | |
| β-strand | 148-152 | 5 | 4 |
| β-strand | 163-165 | 3 | 6 |
| β-strand | 171-174 | 4 | 6 |
| β-strand | 188-194 | 7 | 4 |
| α-helix | 195-198 | 4 | |
| β-strand | 202-209 | 8 | 4 |
| β-strand | 212 | 1 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Epithelial-cadherin | A | protein | 212 | Mus musculus | P09803 (AlphaFold model) |
>1Q1P_1 Epithelial-cadherin (chains A) WVIPPISCPENEKGEFPKNLVQIKSNRDKETKVFYSITGQGADKPPVGVFIIERETGWLK VTQPLDREAIAKYILYSHAVSSNGEAVEDPMEIVITVTDQNDNRPEFTQEVFEGSVAEGA VPGTSVMKVSATDADDDVNTYNAAIAYTIVSQDPELPHKNMFTVNRDTGVISVLTSGLDR ESYPTYTLVVQAADLQGEGLSTTAKAVITVKD
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 3 |
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:
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