Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit M (Q1RKE5)
Analyse AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit M… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q1RKE5
- Type
- protein
- Length
- 494 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0D671490EE06E75975e90D7F99F73B20BE618744
- Molecule
- NADH-quinone oxidoreductase subunit M
- UniProt
- Q1RKE5
- Pockets
- 3 · best druggability 0.63
Structure
1 distinct chain · 79% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit M | protein | 494 | 79% helix, 4% strand | Q1RKE5 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 209 | 0.63 | 0.83 | 35 | empty |
| 2 | 99 | 0.52 | 0.83 | 17 | empty |
| 3 | 103 | 0.48 | 0.80 | 16 | 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 Q1RKE5
- Elsewhere: UniProt Q1RKE5 · AlphaFold DB Q1RKE5
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