Research workbench
AlphaFold monomer V2.0 prediction for xylose import ATP-binding protein xylg (Q48J74)
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
- Q48J74
- Type
- protein
- Length
- 518 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd91633319BDB0a92cbC4f08DeA734Bf74C030064
- Molecule
- Xylose import ATP-binding protein xylg
- UniProt
- Q48J74
- Pockets
- 4 · best druggability 0.54
Structure
1 distinct chain · 36% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Xylose import ATP-binding protein xylg | protein | 518 | 36% helix, 26% strand | Q48J74 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 276 | 0.54 | 0.76 | 33 | empty |
| 2 | 113 | 0.41 | 0.77 | 23 | empty |
| 3 | 91 | 0.37 | 0.75 | 16 | empty |
| 4 | 57 | 0.27 | 0.74 | 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 Q48J74
- Elsewhere: UniProt Q48J74 · AlphaFold DB Q48J74
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