Research workbench
AlphaFold monomer V2.0 prediction for methylthioribose-1-phosphate isomerase (Q92TI2)
Analyse AlphaFold monomer V2.0 prediction for methylthioribose-1-phosphate isomerase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q92TI2
- Type
- protein
- Length
- 364 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBbA81fF34F47ba53f6581B08F2f97eb513cf6705
- Molecule
- Methylthioribose-1-phosphate isomerase
- UniProt
- Q92TI2
- Pockets
- 3 · best druggability 0.76
Structure
1 distinct chain · 42% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methylthioribose-1-phosphate isomerase | protein | 364 | 42% helix, 20% strand | Q92TI2 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 87 | 0.76 | 0.98 | 31 | empty |
| 2 | 130 | 0.49 | 0.79 | 22 | empty |
| 3 | 96 | 0.40 | 0.77 | 18 | 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 Q92TI2
- Elsewhere: UniProt Q92TI2 · AlphaFold DB Q92TI2
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