Research workbench
AlphaFold monomer V2.0 prediction for glucose-1-phosphate thymidylyltransferase (P95778)
Analyse AlphaFold monomer V2.0 prediction for glucose-1-phosphate thymidylyltransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P95778
- Type
- protein
- Length
- 289 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3F68E74Da58A02eCfd34cED79740EF24407440ed
- Molecule
- Glucose-1-phosphate thymidylyltransferase
- UniProt
- P95778
- Pockets
- 4 · best druggability 0.71
Structure
1 distinct chain · 39% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucose-1-phosphate thymidylyltransferase | protein | 289 | 39% helix, 23% strand | P95778 |
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 | 415 | 0.71 | 0.83 | 38 | empty |
| 2 | 158 | 0.49 | 0.77 | 23 | empty |
| 3 | 105 | 0.37 | 0.74 | 15 | empty |
| 4 | 67 | 0.31 | 0.74 | 13 | 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 P95778
- Elsewhere: UniProt P95778 · AlphaFold DB P95778
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