Research workbench
AlphaFold monomer V2.0 prediction for beta-1-syntrophin (Q99L88)
Analyse AlphaFold monomer V2.0 prediction for beta-1-syntrophin (Q99L88) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q99L88
- Type
- protein
- Length
- 537 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xDE2799055eD4c588222eDb2258e35ff086b5A24d
- Molecule
- Beta-1-syntrophin
- UniProt
- Q99L88
- Pockets
- 7 · best druggability 0.57
Structure
1 distinct chain · 22% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-1-syntrophin | protein | 537 | 22% helix, 34% strand | Q99L88 |
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 245 | 0.57 | 0.78 | 30 | empty |
| 2 | 149 | 0.56 | 0.82 | 26 | empty |
| 3 | 245 | 0.50 | 0.75 | 29 | empty |
| 4 | 225 | 0.49 | 0.75 | 30 | empty |
| 5 | 159 | 0.44 | 0.75 | 24 | 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 Q99L88
- Elsewhere: UniProt Q99L88 · AlphaFold DB Q99L88
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