Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit D (A5IHW0)
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
- A5IHW0
- Type
- protein
- Length
- 417 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0EA189b2343A464f560b44103f6A3396Da1dA8a9
- Molecule
- NADH-quinone oxidoreductase subunit D
- UniProt
- A5IHW0
- Pockets
- 4 · best druggability 0.50
Structure
1 distinct chain · 52% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit D | protein | 417 | 52% helix, 12% strand | A5IHW0 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 72 | 0.50 | 0.84 | 20 | empty |
| 2 | 80 | 0.43 | 0.80 | 20 | empty |
| 3 | 80 | 0.38 | 0.77 | 18 | empty |
| 4 | 93 | 0.35 | 0.74 | 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 A5IHW0
- Elsewhere: UniProt A5IHW0 · AlphaFold DB A5IHW0
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