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AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit N 1 (A9B6Y0)
Analyse AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit N 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A9B6Y0
- Type
- protein
- Length
- 491 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x11a6d1FddF7C73C4eE19B953B3c6ab9325775E17
- Molecule
- NADH-quinone oxidoreductase subunit N 1
- UniProt
- A9B6Y0
- Pockets
- 3 · best druggability 0.44
Structure
1 distinct chain · 75% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit N 1 | protein | 491 | 75% helix, 3% strand | A9B6Y0 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 120 | 0.44 | 0.76 | 18 | empty |
| 2 | 95 | 0.36 | 0.75 | 21 | empty |
| 3 | 51 | 0.30 | 0.75 | 12 | 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 A9B6Y0
- Elsewhere: UniProt A9B6Y0 · AlphaFold DB A9B6Y0
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