Research workbench
Alpha-E-catenin is an autoinhibited molecule that co-activates vinculin
Analyse Alpha-E-catenin is an autoinhibited molecule that co-activates vinculin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4E17
- Type
- protein
- Length
- 274 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vinculin; Catenin alpha-1
- UniProt
- P12003, P26231
- Pockets
- 3 · best druggability 0.49
Structure
x-ray diffraction · 2 distinct chains · 84% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vinculin | protein | 246 | 83% helix, 1% strand | P12003 |
| B | Catenin alpha-1 | protein | 28 | 89% helix, 0% strand | P26231 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 147 | 0.49 | 0.78 | 15 | empty |
| 2 | 84 | 0.43 | 0.80 | 19 | empty |
| 3 | 50 | 0.32 | 0.78 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 1491 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 4E17 · Alpha-E-catenin is an autoinhibited molecule that co-activates vinculin · the same entry in another collection · chain A against A, TM-score 1.00
- P26231 · AlphaFold monomer V2.0 prediction for catenin alpha-1 (P26231) · a predicted model of the same protein · chain B against A, TM-score 0.88
- P12003 · AlphaFold monomer V2.0 prediction for vinculin (P12003) · a predicted model of the same protein · chain A against A, TM-score 0.88
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P12003
- Every structure of UniProt P26231
- Elsewhere: RCSB PDB 4E17 · PDBe 4E17 · UniProt P12003 · UniProt P26231
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