Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit N 2 (B5YL23)
Analyse AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit N 2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B5YL23
- Type
- protein
- Length
- 452 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x74a75d409518fd03AC5d8A8296be5D6D37473B19
- Molecule
- NADH-quinone oxidoreductase subunit N 2
- UniProt
- B5YL23
- Pockets
- 3 · best druggability 0.56
Structure
1 distinct chain · 79% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit N 2 | protein | 452 | 79% helix, 3% strand | B5YL23 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 175 | 0.56 | 0.80 | 26 | empty |
| 2 | 93 | 0.35 | 0.73 | 13 | empty |
| 3 | 62 | 0.35 | 0.77 | 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 B5YL23
- Elsewhere: UniProt B5YL23 · AlphaFold DB B5YL23
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