Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit D (Q5HSL5)
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
- Q5HSL5
- Type
- protein
- Length
- 408 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa035E6D3B1efC66Af27788374F32B4851461992f
- Molecule
- NADH-quinone oxidoreductase subunit D
- UniProt
- Q5HSL5
- Pockets
- 3 · best druggability 0.55
Structure
1 distinct chain · 50% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit D | protein | 408 | 50% helix, 12% strand | Q5HSL5 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 55 | 0.55 | 0.89 | 16 | empty |
| 2 | 126 | 0.45 | 0.78 | 18 | empty |
| 3 | 85 | 0.34 | 0.74 | 20 | 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 Q5HSL5
- Elsewhere: UniProt Q5HSL5 · AlphaFold DB Q5HSL5
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