Research workbench
Crystal structure of full-length mouse alphae-catenin
Analyse Crystal structure of full-length mouse alphae-catenin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4K1N
- Type
- protein
- Length
- 1,040 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Catenin alpha-1
- UniProt
- P26231
- Pockets
- 11 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Catenin alpha-1 | protein | 520 | 78% helix, 0% strand | P26231 |
Pockets
11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 725 | 0.79 | 0.83 | 102 | empty |
| 2 | 589 | 0.73 | 0.81 | 72 | empty |
| 3 | 215 | 0.65 | 0.84 | 42 | empty |
| 4 | 99 | 0.62 | 0.88 | 21 | empty |
| 5 | 510 | 0.61 | 0.75 | 46 | empty |
Interfaces
1 interface between chains.
- A–B · 1477 Ų buried · 6 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 4K1N · PDBe 4K1N · UniProt P26231
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.