Research workbench
AlphaFold monomer V2.0 prediction for ribitol-5-phosphate xylosyltransferase 1 (Q08CD5)
Analyse AlphaFold monomer V2.0 prediction for ribitol-5-phosphate xylosyltransferase 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q08CD5
- Type
- protein
- Length
- 434 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb21d88281e0c9D3f5b75d07D0eaDbB86e28d89D2
- Molecule
- Ribitol-5-phosphate xylosyltransferase 1
- UniProt
- Q08CD5
- Pockets
- 2 · best druggability 0.75
Structure
1 distinct chain · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribitol-5-phosphate xylosyltransferase 1 | protein | 434 | 43% helix, 17% strand | Q08CD5 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 533 | 0.75 | 0.83 | 56 | empty |
| 2 | 81 | 0.38 | 0.77 | 15 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 Q08CD5
- Elsewhere: UniProt Q08CD5 · AlphaFold DB Q08CD5
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