Research workbench
AlphaFold monomer V2.0 prediction for putative thymidine phosphorylase (Q1GQ92)
Analyse AlphaFold monomer V2.0 prediction for putative thymidine phosphorylase (Q1GQ92) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q1GQ92
- Type
- protein
- Length
- 514 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xAFeA37bDaDABc4D574f7966CCC7435f7649E0287
- Molecule
- Putative thymidine phosphorylase
- UniProt
- Q1GQ92
- Pockets
- 4 · best druggability 0.78
Structure
1 distinct chain · 41% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative thymidine phosphorylase | protein | 514 | 41% helix, 20% strand | Q1GQ92 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 786 | 0.78 | 0.82 | 82 | empty |
| 2 | 94 | 0.40 | 0.76 | 14 | empty |
| 3 | 50 | 0.32 | 0.77 | 12 | empty |
| 4 | 55 | 0.28 | 0.74 | 12 | empty |
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 Q1GQ92
- Elsewhere: UniProt Q1GQ92 · AlphaFold DB Q1GQ92
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