Crystal structure of the alpha-catenin dimerization domain. Determined by X-ray diffraction at 3.0 Å resolution. Released 12 Jul 2000.
Explore 1DOV in 3D Show helices and sheets RCSB PDB PDBe
1DOV contains 5 α-helices and 0 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 |
|---|---|---|---|
| α-helix | 85-113 | 29 | |
| α-helix | 118-165 | 48 | |
| α-helix | 170-197 | 28 | |
| α-helix | 201-230 | 30 | |
| α-helix | 235-259 | 25 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Alpha-catenin | A | protein | 181 | Mus musculus | P26231 (AlphaFold model) |
>1DOV_1 ALPHA-CATENIN (chains A) ESQFLKEELVVAVEDVRKQGDLMKSAAGEFADDPCSSVKRGNMVRAARALLSAVTRLLIL ADMADVYKLLVQLKVVEDGILKLRNAGNEQDLGIQYKALKPEVDKLNIMAAKRQQELKDV GNRDQMAAARGILQKNVPILYTASQACLQHPDVAAYKANRDLIYKQLQQAVTGISNAAQA T
Structure of the dimerization and beta-catenin-binding region of alpha-catenin. Pokutta, S., Weis, W.I. Mol Cell (2000) 5:533-543. DOI 10.1016/S1097-2765(00)80447-5 · PubMed
Other PDB entries of the same protein (UniProt P26231 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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