Research workbench
AlphaFold monomer V2.0 prediction for ATP synthase subunit beta, chloroplastic (O03075)
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
- O03075
- Type
- protein
- Length
- 473 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5Be6db7bf0250FDCB4deFDb7f993cB6C300c26C2
- Molecule
- ATP synthase subunit beta, chloroplastic
- UniProt
- O03075
- Pockets
- 5 · best druggability 0.59
Structure
1 distinct chain · 36% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP synthase subunit beta, chloroplastic | protein | 473 | 36% helix, 23% strand | O03075 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 213 | 0.59 | 0.81 | 38 | empty |
| 2 | 340 | 0.55 | 0.74 | 31 | empty |
| 3 | 97 | 0.54 | 0.83 | 23 | empty |
| 4 | 89 | 0.49 | 0.82 | 16 | empty |
| 5 | 59 | 0.33 | 0.77 | 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 O03075
- Elsewhere: UniProt O03075 · AlphaFold DB O03075
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