Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit D (A6QCG0)
Analyse AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit D… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A6QCG0
- Type
- protein
- Length
- 409 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x80D2ac0F5e3268bC5C1d28BBAA07E3169BB02b79
- Molecule
- NADH-quinone oxidoreductase subunit D
- UniProt
- A6QCG0
- Pockets
- 3 · best druggability 0.49
Structure
1 distinct chain · 51% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit D | protein | 409 | 51% helix, 12% strand | A6QCG0 |
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 | 185 | 0.49 | 0.76 | 29 | empty |
| 2 | 58 | 0.29 | 0.75 | 15 | empty |
| 3 | 53 | 0.25 | 0.73 | 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 A6QCG0
- Elsewhere: UniProt A6QCG0 · AlphaFold DB A6QCG0
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