Research workbench
AlphaFold monomer V2.0 prediction for xylose import ATP-binding protein xylg (Q663Y5)
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
- Q663Y5
- Type
- protein
- Length
- 510 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7a1388B6Aad67B04634A32f63b8A6D6005eab86c
- Molecule
- Xylose import ATP-binding protein xylg
- UniProt
- Q663Y5
- Pockets
- 7 · best druggability 0.53
Structure
1 distinct chain · 37% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Xylose import ATP-binding protein xylg | protein | 510 | 37% helix, 26% strand | Q663Y5 |
Pockets
7 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 | 0.53 | 0.75 | 33 | empty |
| 2 | 130 | 0.48 | 0.78 | 22 | empty |
| 3 | 114 | 0.40 | 0.76 | 21 | empty |
| 4 | 69 | 0.39 | 0.79 | 13 | empty |
| 5 | 75 | 0.30 | 0.74 | 15 | 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 Q663Y5
- Elsewhere: UniProt Q663Y5 · AlphaFold DB Q663Y5
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