Research workbench
AlphaFold monomer V2.0 prediction for alpha-xylosidase a (A2QTU5)
Analyse AlphaFold monomer V2.0 prediction for alpha-xylosidase a (A2QTU5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A2QTU5
- Type
- protein
- Length
- 736 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x46EfCa788d03A3e879DAcDb96552AB8Bbc7e20b3
- Molecule
- Alpha-xylosidase a
- UniProt
- A2QTU5
- Pockets
- 7 · best druggability 0.51
Structure
1 distinct chain · 24% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-xylosidase a | protein | 736 | 24% helix, 26% strand | A2QTU5 |
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 84 | 0.51 | 0.84 | 20 | empty |
| 2 | 189 | 0.50 | 0.77 | 27 | empty |
| 3 | 165 | 0.45 | 0.75 | 28 | empty |
| 4 | 63 | 0.35 | 0.77 | 11 | empty |
| 5 | 62 | 0.31 | 0.75 | 13 | empty |
Modifications
Observed in the structure: 2 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 A2QTU5
- Elsewhere: UniProt A2QTU5 · AlphaFold DB A2QTU5
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