Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit B (B5FPG8)
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
- B5FPG8
- Type
- protein
- Length
- 220 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x12036AF92D04543C69d73C1E0B95D813ddc5bfa1
- Molecule
- NADH-quinone oxidoreductase subunit B
- UniProt
- B5FPG8
- Pockets
- 3 · best druggability 0.60
Structure
1 distinct chain · 37% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit B | protein | 220 | 37% helix, 16% strand | B5FPG8 |
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 | 121 | 0.60 | 0.85 | 17 | empty |
| 2 | 287 | 0.56 | 0.76 | 38 | empty |
| 3 | 193 | 0.55 | 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 B5FPG8
- Elsewhere: UniProt B5FPG8 · AlphaFold DB B5FPG8
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