Research workbench
AlphaFold monomer V2.0 prediction for na(+)-translocating NADH- quinone reductase subunit B (B5Y1F0)
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
- B5Y1F0
- Type
- protein
- Length
- 412 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xE83892548e88C098Ea0eB1D6dAb6CCCF839Ad27B
- Molecule
- Na(+)-translocating NADH-quinone reductase subunit B
- UniProt
- B5Y1F0
- 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 | 412 | 67% helix, 0% strand | B5Y1F0 |
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 94 | 0.74 | 0.96 | 25 | empty |
| 2 | 106 | 0.64 | 0.89 | 33 | empty |
| 3 | 225 | 0.53 | 0.77 | 27 | empty |
| 4 | 107 | 0.50 | 0.81 | 19 | empty |
| 5 | 96 | 0.39 | 0.76 | 21 | 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 B5Y1F0
- Elsewhere: UniProt B5Y1F0 · AlphaFold DB B5Y1F0
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