Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit D (A5VAM0)
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
- A5VAM0
- Type
- protein
- Length
- 406 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4Ef77Afb5a3D9F41c95Be3227D1CC986CCb61835
- Molecule
- NADH-quinone oxidoreductase subunit D
- UniProt
- A5VAM0
- Pockets
- 3 · best druggability 0.53
Structure
1 distinct chain · 50% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit D | protein | 406 | 50% helix, 12% strand | A5VAM0 |
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 | 129 | 0.53 | 0.81 | 26 | empty |
| 2 | 58 | 0.52 | 0.87 | 18 | empty |
| 3 | 78 | 0.30 | 0.73 | 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 A5VAM0
- Elsewhere: UniProt A5VAM0 · AlphaFold DB A5VAM0
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