Research workbench
AlphaFold monomer V2.0 prediction for ATP synthase subunit beta, chloroplastic (Q09FV4)
Analyse AlphaFold monomer V2.0 prediction for ATP synthase subunit beta, chloroplastic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q09FV4
- Type
- protein
- Length
- 498 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBeB220F0B5b0C48F46B5DDd3E3b071BC0827f8D6
- Molecule
- ATP synthase subunit beta, chloroplastic
- UniProt
- Q09FV4
- Pockets
- 8 · best druggability 0.55
Structure
1 distinct chain · 38% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP synthase subunit beta, chloroplastic | protein | 498 | 38% helix, 22% strand | Q09FV4 |
Pockets
8 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 211 | 0.55 | 0.78 | 31 | empty |
| 2 | 100 | 0.48 | 0.81 | 18 | empty |
| 3 | 97 | 0.44 | 0.79 | 20 | empty |
| 4 | 50 | 0.40 | 0.81 | 15 | empty |
| 5 | 64 | 0.34 | 0.76 | 14 | 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 Q09FV4
- Elsewhere: UniProt Q09FV4 · AlphaFold DB Q09FV4
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