Research workbench
Crystal structure of mouse catenin beta-59 in 5.6M urea
Analyse Crystal structure of mouse catenin beta-59 in 5.6M urea in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4EVA
- Type
- protein
- Length
- 979 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Catenin beta-1
- UniProt
- Q02248
- Ligands
- URE
- Pockets
- 6 · best druggability 0.47
Structure
x-ray diffraction · 2 distinct chains · 75% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Catenin beta-1 | protein | 491 | 74% helix, 0% strand | Q02248 |
| C | Catenin beta-1 | protein | 488 | 75% helix, 0% strand | Q02248 |
Ligands and binding sites
- URE · Urea · ligand · 72 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 188 | 0.47 | 0.75 | 23 | URE |
| 2 | 179 | 0.45 | 0.75 | 25 | URE |
| 3 | 128 | 0.40 | 0.75 | 16 | URE |
| 4 | 141 | 0.39 | 0.73 | 20 | URE |
| 5 | 79 | 0.35 | 0.75 | 16 | empty |
Interfaces
1 interface between chains.
- A–C · 144 Ų buried · 1 hydrogen bond · 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 Q02248
- Elsewhere: RCSB PDB 4EVA · PDBe 4EVA · UniProt Q02248
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