Research workbench
AlphaFold monomer V2.0 prediction for V-type ATP synthase subunit E (A1RSF2)
Analyse AlphaFold monomer V2.0 prediction for V-type ATP synthase subunit E (A1RSF2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A1RSF2
- Type
- protein
- Length
- 190 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4a9eD2eAf8d72EFA9810BAb10Ec13711141c1541
- Molecule
- V-type ATP synthase subunit E
- UniProt
- A1RSF2
- Pockets
- 1 · best druggability 0.41
Structure
1 distinct chain · 75% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | V-type ATP synthase subunit E | protein | 190 | 75% helix, 10% strand | A1RSF2 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 87 | 0.41 | 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 A1RSF2
- Elsewhere: UniProt A1RSF2 · AlphaFold DB A1RSF2
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