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AlphaFold monomer V2.0 prediction for na(+)-translocating NADH- quinone reductase subunit a (A5UAX1)
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
- A5UAX1
- Type
- protein
- Length
- 447 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x434b0DC4af054BE165a98eb346BDbBb0889A5EB3
- Molecule
- Na(+)-translocating NADH-quinone reductase subunit a
- UniProt
- A5UAX1
- Pockets
- 4 · best druggability 0.81
Structure
1 distinct chain · 25% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Na(+)-translocating NADH-quinone reductase subunit a | protein | 447 | 25% helix, 25% strand | A5UAX1 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1118 | 0.81 | 0.82 | 97 | empty |
| 2 | 112 | 0.41 | 0.76 | 28 | empty |
| 3 | 127 | 0.40 | 0.75 | 24 | empty |
| 4 | 57 | 0.29 | 0.75 | 14 | 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 A5UAX1
- Elsewhere: UniProt A5UAX1 · AlphaFold DB A5UAX1
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