MolNFT v1 · #61345 · protein
C-terminal beta-catenin bound tip-1 structure
3DIW · TAX1-binding protein 3: “C-terminal beta-catenin bound tip-1 structure”. X-ray diffraction, 2 pockets (best druggability 0.35). MolNFT v1 #61345 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3DIW
- Type
- protein
- Length
- 232 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- TAX1-binding protein 3; Decameric peptide form catenin beta-1
- UniProt
- Q9DBG9, P35222
- Pockets
- 2 · best druggability 0.35
Structure
x-ray diffraction · 3 distinct chains · 16% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TAX1-binding protein 3 | protein | 108 | 15% helix, 40% strand | Q9DBG9 |
| B | TAX1-binding protein 3 | protein | 106 | 18% helix, 37% strand | Q9DBG9 |
| C, D | Decameric peptide form catenin beta-1 | protein | 9 | 0% helix, 33% strand | P35222 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 104 | 0.35 | 0.74 | 22 | empty |
| 2 | 75 | 0.35 | 0.76 | 18 | empty |
Interfaces
3 interfaces between chains.
- A–C · 663 Ų buried · 17 hydrogen bonds · protein-protein
- B–D · 587 Ų buried · 15 hydrogen bonds · protein-protein
- A–B · 454 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 3DIW · c-terminal beta-catenin bound TIP-1 structure · the same entry in another collection · chain D against D, TM-score 1.00
- Q9DBG9 · AlphaFold monomer V2.0 prediction for TAX1-binding protein 3 (Q9DBG9) · a predicted model of the same protein · chain B against A, TM-score 0.97
- P35222 · AlphaFold monomer V2.0 prediction for catenin beta-1 (P35222) · a predicted model of the same protein · chain C against A, TM-score 0.46
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 Q9DBG9
- Every structure of UniProt P35222
- Elsewhere: RCSB PDB 3DIW · PDBe 3DIW · UniProt Q9DBG9 · UniProt P35222
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