Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit B (B5YXS7)
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
- B5YXS7
- Type
- protein
- Length
- 220 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB502bEb1e19F27cA874F3BfeddA8Ba618CC47c31
- Molecule
- NADH-quinone oxidoreductase subunit B
- UniProt
- B5YXS7
- Pockets
- 3 · best druggability 0.57
Structure
1 distinct chain · 38% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit B | protein | 220 | 38% helix, 16% strand | B5YXS7 |
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 296 | 0.57 | 0.77 | 34 | empty |
| 2 | 144 | 0.55 | 0.81 | 23 | empty |
| 3 | 149 | 0.51 | 0.79 | 23 | 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 B5YXS7
- Elsewhere: UniProt B5YXS7 · AlphaFold DB B5YXS7
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