Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit N (A0RME1)
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
- A0RME1
- Type
- protein
- Length
- 469 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x40B9C9d5F084D34d026E9d5Dd10501AcdF6d6152
- Molecule
- NADH-quinone oxidoreductase subunit N
- UniProt
- A0RME1
- Pockets
- 3 · best druggability 0.54
Structure
1 distinct chain · 76% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit N | protein | 469 | 76% helix, 1% strand | A0RME1 |
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 | 219 | 0.54 | 0.77 | 35 | empty |
| 2 | 120 | 0.41 | 0.75 | 20 | empty |
| 3 | 65 | 0.37 | 0.77 | 13 | 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 A0RME1
- Elsewhere: UniProt A0RME1 · AlphaFold DB A0RME1
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