Research workbench
AlphaFold monomer V2.0 prediction for ion-translocating oxidoreductase complex subunit E (Q9CNP5)
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
- Q9CNP5
- Type
- protein
- Length
- 224 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5789C821eF3e8D61750de197f4929F6643abaaFe
- Molecule
- Ion-translocating oxidoreductase complex subunit E
- UniProt
- Q9CNP5
- Pockets
- 3 · best druggability 0.47
Structure
1 distinct chain · 76% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ion-translocating oxidoreductase complex subunit E | protein | 224 | 76% helix, 2% strand | Q9CNP5 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 172 | 0.47 | 0.76 | 27 | empty |
| 2 | 93 | 0.37 | 0.75 | 15 | empty |
| 3 | 65 | 0.32 | 0.74 | 12 | 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 Q9CNP5
- Elsewhere: UniProt Q9CNP5 · AlphaFold DB Q9CNP5
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