Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit N (B9LGS9)
Analyse AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit N… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B9LGS9
- Type
- protein
- Length
- 528 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf87a97E0A4bB354D834857B14296240B167cbe70
- Molecule
- NADH-quinone oxidoreductase subunit N
- UniProt
- B9LGS9
- Pockets
- 4 · best druggability 0.64
Structure
1 distinct chain · 75% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit N | protein | 528 | 75% helix, 2% strand | B9LGS9 |
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 | 361 | 0.64 | 0.78 | 26 | empty |
| 2 | 194 | 0.49 | 0.76 | 24 | empty |
| 3 | 84 | 0.33 | 0.74 | 22 | empty |
| 4 | 52 | 0.28 | 0.74 | 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 B9LGS9
- Elsewhere: UniProt B9LGS9 · AlphaFold DB B9LGS9
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