Research workbench
AlphaFold monomer V2.0 prediction for glucose-1-phosphate thymidylyltransferase (A0QPF9)
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
- A0QPF9
- Type
- protein
- Length
- 288 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xD65e9d6E89E7Ebb7c293A3b63fCda2B159ce6e3e
- Molecule
- Glucose-1-phosphate thymidylyltransferase
- UniProt
- A0QPF9
- Pockets
- 2 · best druggability 0.70
Structure
1 distinct chain · 40% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucose-1-phosphate thymidylyltransferase | protein | 288 | 40% helix, 22% strand | A0QPF9 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 341 | 0.70 | 0.83 | 37 | empty |
| 2 | 198 | 0.54 | 0.78 | 26 | 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 A0QPF9
- Elsewhere: UniProt A0QPF9 · AlphaFold DB A0QPF9
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