Research workbench
Crystal structure of human CTNNBL1(RESIDUES 33~563)
Analyse Crystal structure of human CTNNBL1(RESIDUES 33~563) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MFV
- Type
- protein
- Length
- 978 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-catenin-like protein 1
- UniProt
- Q8WYA6
- Pockets
- 12 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Beta-catenin-like protein 1 | protein | 489 | 76% helix, 0% strand | Q8WYA6 |
Pockets
12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 932 | 0.81 | 0.83 | 77 | empty |
| 2 | 420 | 0.63 | 0.78 | 37 | empty |
| 3 | 362 | 0.63 | 0.79 | 35 | empty |
| 4 | 407 | 0.63 | 0.77 | 59 | empty |
| 5 | 75 | 0.42 | 0.80 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1024 Ų buried · 5 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 Q8WYA6
- Elsewhere: RCSB PDB 4MFV · PDBe 4MFV · UniProt Q8WYA6
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