Research workbench
AlphaFold monomer V2.0 prediction for glucosidase 2 subunit beta (Q9FM96)
Analyse AlphaFold monomer V2.0 prediction for glucosidase 2 subunit beta (Q9FM96) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9FM96
- Type
- protein
- Length
- 647 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x42fB943ABB54FcE752274CE38bcF736f69B067D1
- Molecule
- Glucosidase 2 subunit beta
- UniProt
- Q9FM96
- Pockets
- 3 · best druggability 0.63
Structure
1 distinct chain · 32% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucosidase 2 subunit beta | protein | 647 | 32% helix, 12% strand | Q9FM96 |
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 | 428 | 0.63 | 0.77 | 39 | empty |
| 2 | 141 | 0.40 | 0.73 | 25 | empty |
| 3 | 69 | 0.37 | 0.77 | 17 | empty |
Modifications
Observed in the structure: 8 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 Q9FM96
- Elsewhere: UniProt Q9FM96 · AlphaFold DB Q9FM96
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