Research workbench
AlphaFold monomer V2.0 prediction for udp-xylose and udp-N- acetylglucosamine transporter (Q969S0)
Analyse AlphaFold monomer V2.0 prediction for udp-xylose and udp-N- acetylglucosamine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q969S0
- Type
- protein
- Length
- 331 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x45fD4D043255F48e1379B3F46b73F7df6F6aac35
- Molecule
- Udp-xylose and udp-N-acetylglucosamine transporter
- UniProt
- Q969S0
- Pockets
- 2 · best druggability 0.77
Structure
1 distinct chain · 76% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-xylose and udp-N-acetylglucosamine transporter | protein | 331 | 76% helix, 2% strand | Q969S0 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1055 | 0.77 | 0.79 | 76 | empty |
| 2 | 75 | 0.31 | 0.72 | 18 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 Q969S0
- Elsewhere: UniProt Q969S0 · AlphaFold DB Q969S0
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