Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit C/D (A7MH24)
Analyse AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit C/D… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A7MH24
- Type
- protein
- Length
- 603 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa130963659F9ADED1C735201Bb05F57675e205B8
- Molecule
- NADH-quinone oxidoreductase subunit C/D
- UniProt
- A7MH24
- Pockets
- 7 · best druggability 0.60
Structure
1 distinct chain · 42% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit C/D | protein | 603 | 42% helix, 16% strand | A7MH24 |
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 357 | 0.60 | 0.77 | 34 | empty |
| 2 | 198 | 0.58 | 0.80 | 28 | empty |
| 3 | 161 | 0.51 | 0.78 | 19 | empty |
| 4 | 147 | 0.49 | 0.78 | 25 | empty |
| 5 | 59 | 0.48 | 0.85 | 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 A7MH24
- Elsewhere: UniProt A7MH24 · AlphaFold DB A7MH24
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