Research workbench
AlphaFold monomer V2.0 prediction for ATP synthase subunit beta (Q87E90)
Analyse AlphaFold monomer V2.0 prediction for ATP synthase subunit beta (Q87E90) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q87E90
- Type
- protein
- Length
- 466 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5dFaD101aDf247804E2d52a7c5a93527E0cEe735
- Molecule
- ATP synthase subunit beta
- UniProt
- Q87E90
- Pockets
- 8 · best druggability 0.54
Structure
1 distinct chain · 39% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP synthase subunit beta | protein | 466 | 39% helix, 21% strand | Q87E90 |
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 103 | 0.54 | 0.83 | 17 | empty |
| 2 | 172 | 0.51 | 0.78 | 28 | empty |
| 3 | 89 | 0.48 | 0.82 | 22 | empty |
| 4 | 58 | 0.40 | 0.80 | 15 | empty |
| 5 | 111 | 0.39 | 0.76 | 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 Q87E90
- Elsewhere: UniProt Q87E90 · AlphaFold DB Q87E90
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