Research workbench
AlphaFold monomer V2.0 prediction for glucan 1,3-beta-glucosidase (Q12626)
Analyse AlphaFold monomer V2.0 prediction for glucan 1,3-beta-glucosidase (Q12626) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q12626
- Type
- protein
- Length
- 435 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb3c0C983Fc44934AC589D7131C08a72544EBB92E
- Molecule
- Glucan 1,3-beta-glucosidase
- UniProt
- Q12626
- Pockets
- 3 · best druggability 0.60
Structure
1 distinct chain · 32% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucan 1,3-beta-glucosidase | protein | 435 | 32% helix, 11% strand | Q12626 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 258 | 0.60 | 0.80 | 36 | empty |
| 2 | 138 | 0.46 | 0.77 | 21 | empty |
| 3 | 58 | 0.34 | 0.77 | 14 | 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 Q12626
- Elsewhere: UniProt Q12626 · AlphaFold DB Q12626
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