Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit N (B0TH87)
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
- B0TH87
- Type
- protein
- Length
- 472 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x362a6d063b1B7E1B6EfD3A9A7CA3612e3FE037AA
- Molecule
- NADH-quinone oxidoreductase subunit N
- UniProt
- B0TH87
- Pockets
- 3 · best druggability 0.40
Structure
1 distinct chain · 76% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit N | protein | 472 | 76% helix, 2% strand | B0TH87 |
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 | 103 | 0.40 | 0.75 | 15 | empty |
| 2 | 102 | 0.38 | 0.75 | 21 | empty |
| 3 | 62 | 0.30 | 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 B0TH87
- Elsewhere: UniProt B0TH87 · AlphaFold DB B0TH87
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