Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit B (A7FGQ6)
Analyse AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit B… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A7FGQ6
- Type
- protein
- Length
- 227 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6F1477A7ba7b4D12E5dE4da4526a61F2AFaa8749
- Molecule
- NADH-quinone oxidoreductase subunit B
- UniProt
- A7FGQ6
- Pockets
- 3 · best druggability 0.60
Structure
1 distinct chain · 40% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit B | protein | 227 | 40% helix, 17% strand | A7FGQ6 |
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 | 277 | 0.60 | 0.79 | 40 | empty |
| 2 | 133 | 0.55 | 0.82 | 21 | empty |
| 3 | 78 | 0.34 | 0.75 | 19 | 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 A7FGQ6
- Elsewhere: UniProt A7FGQ6 · AlphaFold DB A7FGQ6
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