Research workbench
AlphaFold monomer V2.0 prediction for ion-translocating oxidoreductase complex subunit D (A4XS50)
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
- A4XS50
- Type
- protein
- Length
- 343 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0EA189b2343A464f560b44103f6A3396Da1dA8a9
- Molecule
- Ion-translocating oxidoreductase complex subunit D
- UniProt
- A4XS50
- Pockets
- 3 · best druggability 0.82
Structure
1 distinct chain · 61% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ion-translocating oxidoreductase complex subunit D | protein | 343 | 61% helix, 1% strand | A4XS50 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 260 | 0.82 | 0.94 | 44 | empty |
| 2 | 155 | 0.67 | 0.87 | 31 | empty |
| 3 | 78 | 0.42 | 0.79 | 16 | 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 A4XS50
- Elsewhere: UniProt A4XS50 · AlphaFold DB A4XS50
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