Research workbench
AlphaFold monomer V2.0 prediction for xylose import ATP-binding protein xylg (Q13RB6)
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
- Q13RB6
- Type
- protein
- Length
- 519 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x80D2ac0F5e3268bC5C1d28BBAA07E3169BB02b79
- Molecule
- Xylose import ATP-binding protein xylg
- UniProt
- Q13RB6
- Pockets
- 5 · best druggability 0.65
Structure
1 distinct chain · 35% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Xylose import ATP-binding protein xylg | protein | 519 | 35% helix, 26% strand | Q13RB6 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 692 | 0.65 | 0.75 | 69 | empty |
| 2 | 144 | 0.46 | 0.77 | 27 | empty |
| 3 | 78 | 0.40 | 0.78 | 15 | empty |
| 4 | 74 | 0.39 | 0.78 | 13 | empty |
| 5 | 93 | 0.38 | 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 Q13RB6
- Elsewhere: UniProt Q13RB6 · AlphaFold DB Q13RB6
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