Research workbench
AlphaFold monomer V2.0 prediction for na(+)-translocating NADH- quinone reductase subunit D (Q9X4Q6)
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
- Q9X4Q6
- Type
- protein
- Length
- 210 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x117E5163DF1bD8F3b06437B966A7eb1f790855eb
- Molecule
- Na(+)-translocating NADH-quinone reductase subunit D
- UniProt
- Q9X4Q6
Structure
1 distinct chain · 76% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Na(+)-translocating NADH-quinone reductase subunit D | protein | 210 | 76% helix, 3% strand | Q9X4Q6 |
Compared structures
- 8EVU · Cryo EM structure of Vibrio cholerae NQR · an experimental structure of the same protein · chain A against D, TM-score 0.92
- 8A1U · Sodium pumping NADH-qui oxidoreductase with substrates NADH and Q2 · an experimental structure of the same protein · chain A against D, TM-score 0.91
- 4P6V · Crystal structure of the na+-translocating NADH: ubiquinone oxidoreductase from vibrio… · an experimental structure of the same protein · chain A against D, TM-score 0.80
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 Q9X4Q6
- Elsewhere: UniProt Q9X4Q6 · AlphaFold DB Q9X4Q6
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