Research workbench
AlphaFold monomer V2.0 prediction for glucose-1-phosphate thymidylyltransferase (B0RVK9)
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
- B0RVK9
- Type
- protein
- Length
- 295 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf23FAc8E9E29c5e2e2c0614b611FB353464fD274
- Molecule
- Glucose-1-phosphate thymidylyltransferase
- UniProt
- B0RVK9
- Pockets
- 3 · best druggability 0.72
Structure
1 distinct chain · 39% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucose-1-phosphate thymidylyltransferase | protein | 295 | 39% helix, 23% strand | B0RVK9 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 338 | 0.72 | 0.84 | 37 | empty |
| 2 | 360 | 0.65 | 0.79 | 26 | empty |
| 3 | 84 | 0.33 | 0.74 | 16 | 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 B0RVK9
- Elsewhere: UniProt B0RVK9 · AlphaFold DB B0RVK9
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