Research workbench
AlphaFold monomer V2.0 prediction for xylose repressor (P27159)
Analyse AlphaFold monomer V2.0 prediction for xylose repressor (P27159) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P27159
- Type
- protein
- Length
- 383 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x429aA010A80A47FF4a2777bB34A2bba144d19df2
- Molecule
- Xylose repressor
- UniProt
- P27159
- Pockets
- 6 · best druggability 0.60
Structure
1 distinct chain · 40% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Xylose repressor | protein | 383 | 40% helix, 24% strand | P27159 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 78 | 0.60 | 0.89 | 22 | empty |
| 2 | 267 | 0.53 | 0.76 | 25 | empty |
| 3 | 129 | 0.52 | 0.80 | 19 | empty |
| 4 | 125 | 0.48 | 0.79 | 24 | empty |
| 5 | 60 | 0.41 | 0.82 | 17 | 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 P27159
- Elsewhere: UniProt P27159 · AlphaFold DB P27159
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