MolNFT v1 · #81531 · protein
Crystal structure of a mouse tankyrase-axin complex
3UTM · Tankyrase-1: “Crystal structure of a mouse tankyrase-axin complex”. X-ray diffraction, 2 pockets (best druggability 0.69). MolNFT v1 #81531 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3UTM
- Type
- protein
- Length
- 659 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tankyrase-1; Axin-1
- EC
- 2.4.2.30
- UniProt
- Q6PFX9, O35625
- Pockets
- 2 · best druggability 0.69
Structure
x-ray diffraction · 3 distinct chains · 50% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tankyrase-1 (EC 2.4.2.30) | protein | 320 | 54% helix, 0% strand | Q6PFX9 |
| B | Tankyrase-1 (EC 2.4.2.30) | protein | 307 | 51% helix, 0% strand | Q6PFX9 |
| C | Axin-1 | protein | 32 | 0% helix, 6% strand | O35625 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 485 | 0.69 | 0.79 | 42 | empty |
| 2 | 127 | 0.38 | 0.74 | 17 | empty |
Interfaces
3 interfaces between chains.
- A–B · 2136 Ų buried · 10 hydrogen bonds · protein-protein
- B–C · 815 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 675 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 3UTM · Crystal structure of a mouse Tankyrase-Axin complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q6PFX9 · AlphaFold monomer V2.0 prediction for poly [ADP-ribose] polymerase tankyrase-1 (Q6PFX9) · a predicted model of the same protein · chain B against A, TM-score 0.69
- O35625 · AlphaFold monomer V2.0 prediction for axin-1 (O35625) · a predicted model of the same protein · chain C against A, TM-score 0.28
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 Q6PFX9
- Every structure of UniProt O35625
- Elsewhere: RCSB PDB 3UTM · PDBe 3UTM · UniProt Q6PFX9 · UniProt O35625
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