Research workbench
AlphaFold monomer V2.0 prediction for xylose import ATP-binding protein xylg (Q5KYS1)
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
- Q5KYS1
- Type
- protein
- Length
- 504 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBc0D917FA4795675935BEf33e3A0671BBDb3ebf1
- Molecule
- Xylose import ATP-binding protein xylg
- UniProt
- Q5KYS1
- Pockets
- 5 · best druggability 0.55
Structure
1 distinct chain · 36% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Xylose import ATP-binding protein xylg | protein | 504 | 36% helix, 29% strand | Q5KYS1 |
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 | 201 | 0.55 | 0.79 | 28 | empty |
| 2 | 98 | 0.45 | 0.79 | 19 | empty |
| 3 | 138 | 0.39 | 0.74 | 25 | empty |
| 4 | 92 | 0.36 | 0.75 | 21 | empty |
| 5 | 56 | 0.32 | 0.77 | 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 Q5KYS1
- Elsewhere: UniProt Q5KYS1 · AlphaFold DB Q5KYS1
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