Research workbench
AlphaFold monomer V2.0 prediction for ion-translocating oxidoreductase complex subunit E (Q9EVN2)
Analyse AlphaFold monomer V2.0 prediction for ion-translocating oxidoreductase complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9EVN2
- Type
- protein
- Length
- 241 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3298b100681D3A2372Bba3b2f282750dD71629B9
- Molecule
- Ion-translocating oxidoreductase complex subunit E
- UniProt
- Q9EVN2
- Pockets
- 4 · best druggability 0.59
Structure
1 distinct chain · 75% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ion-translocating oxidoreductase complex subunit E | protein | 241 | 75% helix, 0% strand | Q9EVN2 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 328 | 0.59 | 0.77 | 45 | empty |
| 2 | 95 | 0.46 | 0.80 | 22 | empty |
| 3 | 170 | 0.44 | 0.74 | 24 | empty |
| 4 | 69 | 0.35 | 0.77 | 13 | 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 Q9EVN2
- Elsewhere: UniProt Q9EVN2 · AlphaFold DB Q9EVN2
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