Research workbench
AlphaFold monomer V2.0 prediction for na(+)-translocating NADH- quinone reductase subunit B (Q9JVP9)
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
- Q9JVP9
- Type
- protein
- Length
- 410 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf4ED13986579E8e227b3ED6c02276c648754EC27
- Molecule
- Na(+)-translocating NADH-quinone reductase subunit B
- UniProt
- Q9JVP9
- Pockets
- 6 · best druggability 0.74
Structure
1 distinct chain · 67% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Na(+)-translocating NADH-quinone reductase subunit B | protein | 410 | 67% helix, 0% strand | Q9JVP9 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 90 | 0.74 | 0.96 | 23 | empty |
| 2 | 86 | 0.65 | 0.91 | 32 | empty |
| 3 | 179 | 0.51 | 0.77 | 29 | empty |
| 4 | 108 | 0.43 | 0.77 | 15 | empty |
| 5 | 57 | 0.30 | 0.76 | 18 | 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 Q9JVP9
- Elsewhere: UniProt Q9JVP9 · AlphaFold DB Q9JVP9
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