Research workbench
AlphaFold monomer V2.0 prediction for xylose import ATP-binding protein xylg (Q1R528)
Analyse AlphaFold monomer V2.0 prediction for xylose import ATP-binding protein xylg… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q1R528
- Type
- protein
- Length
- 513 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xE978529ba527BfA750887e738022a7611e695635
- Molecule
- Xylose import ATP-binding protein xylg
- UniProt
- Q1R528
- Pockets
- 6 · best druggability 0.60
Structure
1 distinct chain · 35% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Xylose import ATP-binding protein xylg | protein | 513 | 35% helix, 27% strand | Q1R528 |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 523 | 0.60 | 0.74 | 54 | empty |
| 2 | 123 | 0.42 | 0.76 | 22 | empty |
| 3 | 53 | 0.39 | 0.81 | 12 | empty |
| 4 | 64 | 0.38 | 0.79 | 12 | empty |
| 5 | 56 | 0.31 | 0.76 | 12 | 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 Q1R528
- Elsewhere: UniProt Q1R528 · AlphaFold DB Q1R528
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