Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit D (Q2RJU4)
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
- Q2RJU4
- Type
- protein
- Length
- 371 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xA09372C68486A4D623540780401ED026eEcdc381
- Molecule
- NADH-quinone oxidoreductase subunit D
- UniProt
- Q2RJU4
- Pockets
- 2 · best druggability 0.46
Structure
1 distinct chain · 51% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit D | protein | 371 | 51% helix, 13% strand | Q2RJU4 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 63 | 0.46 | 0.83 | 17 | empty |
| 2 | 75 | 0.31 | 0.74 | 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 Q2RJU4
- Elsewhere: UniProt Q2RJU4 · AlphaFold DB Q2RJU4
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