Research workbench
AlphaFold monomer V2.0 prediction for ATP synthase subunit beta (Q7NHG7)
Analyse AlphaFold monomer V2.0 prediction for ATP synthase subunit beta (Q7NHG7) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q7NHG7
- Type
- protein
- Length
- 478 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7a1388B6Aad67B04634A32f63b8A6D6005eab86c
- Molecule
- ATP synthase subunit beta
- UniProt
- Q7NHG7
- Pockets
- 6 · best druggability 0.56
Structure
1 distinct chain · 40% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP synthase subunit beta | protein | 478 | 40% helix, 23% strand | Q7NHG7 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 266 | 0.56 | 0.77 | 39 | empty |
| 2 | 96 | 0.52 | 0.83 | 21 | empty |
| 3 | 100 | 0.46 | 0.79 | 12 | empty |
| 4 | 56 | 0.38 | 0.80 | 18 | empty |
| 5 | 93 | 0.38 | 0.75 | 20 | 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 Q7NHG7
- Elsewhere: UniProt Q7NHG7 · AlphaFold DB Q7NHG7
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