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AlphaFold monomer V2.0 prediction for na(+)-translocating NADH- quinone reductase subunit B (A5UAX2)
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
- A5UAX2
- Type
- protein
- Length
- 411 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB44F19a0cb161828322eEEd13F55d4C3C34938d2
- Molecule
- Na(+)-translocating NADH-quinone reductase subunit B
- UniProt
- A5UAX2
- Pockets
- 5 · best druggability 0.66
Structure
1 distinct chain · 66% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Na(+)-translocating NADH-quinone reductase subunit B | protein | 411 | 66% helix, 0% strand | A5UAX2 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 185 | 0.66 | 0.86 | 34 | empty |
| 2 | 96 | 0.49 | 0.81 | 18 | empty |
| 3 | 69 | 0.45 | 0.82 | 15 | empty |
| 4 | 92 | 0.37 | 0.76 | 23 | empty |
| 5 | 66 | 0.33 | 0.76 | 17 | 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 A5UAX2
- Elsewhere: UniProt A5UAX2 · AlphaFold DB A5UAX2
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