Research workbench
AlphaFold monomer V2.0 prediction for na(+)-translocating NADH- quinone reductase subunit F (A6T526)
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
- A6T526
- Type
- protein
- Length
- 407 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9B130d619fCFc21d0D08E5Ce38Cf42A5fbe230CB
- Molecule
- Na(+)-translocating NADH-quinone reductase subunit F
- UniProt
- A6T526
- Pockets
- 3 · best druggability 0.73
Structure
1 distinct chain · 33% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Na(+)-translocating NADH-quinone reductase subunit F | protein | 407 | 33% helix, 29% strand | A6T526 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 769 | 0.73 | 0.78 | 70 | empty |
| 2 | 161 | 0.47 | 0.76 | 22 | empty |
| 3 | 63 | 0.44 | 0.83 | 15 | empty |
Compared structures
- 7QTY · X-ray structure of FAD domain of nqrf of klebsiella pneumoniae · an experimental structure of the same protein · chain A against A, TM-score 0.68
- 7QTY · X-ray structure of FAD domain of NqrF of Klebsiella pneumoniae · an experimental structure of the same protein · chain A against A, TM-score 0.68
- 7QU0 · X-ray structure of FAD domain of nqrf of klebsiella pneumoniae · an experimental structure of the same protein · chain A against A, TM-score 0.68
- 7QU0 · X-ray structure of FAD domain of NqrF of Klebsiella pneumoniae · an experimental structure of the same protein · chain A against A, TM-score 0.68
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 A6T526
- Elsewhere: UniProt A6T526 · AlphaFold DB A6T526
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