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AlphaFold monomer V2.0 prediction for na(+)-translocating NADH- quinone reductase subunit F (Q9LCJ4)
Analyse AlphaFold monomer V2.0 prediction for na(+)-translocating NADH- quinone… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9LCJ4
- Type
- protein
- Length
- 303 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa5bBccF395a3ABe9B629B9f9f8fBd173cC6F75b8
- Molecule
- Na(+)-translocating NADH-quinone reductase subunit F
- UniProt
- Q9LCJ4
- Pockets
- 2 · best druggability 0.42
Structure
1 distinct chain · 29% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Na(+)-translocating NADH-quinone reductase subunit F | protein | 303 | 29% helix, 30% strand | Q9LCJ4 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 143 | 0.42 | 0.75 | 24 | empty |
| 2 | 57 | 0.34 | 0.78 | 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 Q9LCJ4
- Elsewhere: UniProt Q9LCJ4 · AlphaFold DB Q9LCJ4
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