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Full-length human alpha-catenin crystal structure
Analyse Full-length human alpha-catenin crystal structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4IGG
- Type
- protein
- Length
- 1,521 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Catenin alpha-1
- UniProt
- P35221
- Ligands
- PO4
- Pockets
- 20 · best druggability 0.88
Structure
x-ray diffraction · 2 distinct chains · 77% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Catenin alpha-1 | protein | 750 | 78% helix, 0% strand | P35221 |
| B | Catenin alpha-1 | protein | 771 | 76% helix, 1% strand | P35221 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1165 | 0.88 | 0.90 | 158 | empty |
| 2 | 478 | 0.84 | 0.91 | 86 | empty |
| 3 | 334 | 0.78 | 0.89 | 38 | empty |
| 4 | 351 | 0.76 | 0.87 | 38 | empty |
| 5 | 502 | 0.71 | 0.81 | 61 | empty |
Interfaces
1 interface between chains.
- A–B · 5020 Ų buried · 43 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 P35221
- Elsewhere: RCSB PDB 4IGG · PDBe 4IGG · UniProt P35221
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