Research workbench
AlphaFold monomer V2.0 prediction for beta-scruin (Q25386)
Analyse AlphaFold monomer V2.0 prediction for beta-scruin (Q25386) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q25386
- Type
- protein
- Length
- 916 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa130963659F9ADED1C735201Bb05F57675e205B8
- Molecule
- Beta-scruin
- UniProt
- Q25386
- Pockets
- 11 · best druggability 0.78
Structure
1 distinct chain · 11% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-scruin | protein | 916 | 11% helix, 35% strand | Q25386 |
Pockets
11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 432 | 0.78 | 0.86 | 40 | empty |
| 2 | 515 | 0.77 | 0.85 | 40 | empty |
| 3 | 1192 | 0.75 | 0.77 | 114 | empty |
| 4 | 185 | 0.56 | 0.80 | 30 | empty |
| 5 | 98 | 0.42 | 0.77 | 18 | 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 Q25386
- Elsewhere: UniProt Q25386 · AlphaFold DB Q25386
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