Research workbench
AlphaFold monomer V2.0 prediction for thymidine phosphorylase (Q99N42)
Analyse AlphaFold monomer V2.0 prediction for thymidine phosphorylase (Q99N42) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q99N42
- Type
- protein
- Length
- 471 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7a1388B6Aad67B04634A32f63b8A6D6005eab86c
- Molecule
- Thymidine phosphorylase
- UniProt
- Q99N42
- Pockets
- 5 · best druggability 0.76
Structure
1 distinct chain · 44% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thymidine phosphorylase | protein | 471 | 44% helix, 15% strand | Q99N42 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 105 | 0.76 | 0.97 | 28 | empty |
| 2 | 167 | 0.59 | 0.83 | 24 | empty |
| 3 | 97 | 0.44 | 0.79 | 18 | empty |
| 4 | 86 | 0.40 | 0.78 | 14 | empty |
| 5 | 62 | 0.29 | 0.74 | 15 | 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 Q99N42
- Elsewhere: UniProt Q99N42 · AlphaFold DB Q99N42
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