Research workbench
Crystal structure of the alpha-E-catenin actin-binding domain
Analyse Crystal structure of the alpha-E-catenin actin-binding domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6DV1
- Type
- protein
- Length
- 389 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Catenin alpha-1
- UniProt
- P26231
- Ligands
- BR, SO4
- Pockets
- 6 · best druggability 0.50
Structure
x-ray diffraction · 2 distinct chains · 69% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Catenin alpha-1 | protein | 194 | 68% helix, 7% strand | P26231 |
| B | Catenin alpha-1 | protein | 195 | 69% helix, 8% strand | P26231 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 62 | 0.50 | 0.86 | 19 | empty |
| 2 | 83 | 0.35 | 0.75 | 14 | empty |
| 3 | 67 | 0.35 | 0.77 | 17 | empty |
| 4 | 52 | 0.33 | 0.78 | 15 | empty |
| 5 | 50 | 0.32 | 0.78 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 507 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
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 P26231
- Elsewhere: RCSB PDB 6DV1 · PDBe 6DV1 · UniProt P26231
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