Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit B (A9MJ98)
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
- A9MJ98
- Type
- protein
- Length
- 220 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc4D46881AFD81F838F24Bb4F822bcC9938d48395
- Molecule
- NADH-quinone oxidoreductase subunit B
- UniProt
- A9MJ98
- Pockets
- 3 · best druggability 0.56
Structure
1 distinct chain · 38% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit B | protein | 220 | 38% helix, 18% strand | A9MJ98 |
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 | 305 | 0.56 | 0.76 | 35 | empty |
| 2 | 212 | 0.54 | 0.78 | 31 | empty |
| 3 | 107 | 0.46 | 0.79 | 26 | 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 A9MJ98
- Elsewhere: UniProt A9MJ98 · AlphaFold DB A9MJ98
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