Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit H 2 (Q9EV66)
Analyse AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit H 2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9EV66
- Type
- protein
- Length
- 328 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xC3Bd79E88714EbaDaCeF9C2A7Aa4f6E58AFE8289
- Molecule
- NADH-quinone oxidoreductase subunit H 2
- UniProt
- Q9EV66
- Pockets
- 3 · best druggability 0.56
Structure
1 distinct chain · 68% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit H 2 | protein | 328 | 68% helix, 2% strand | Q9EV66 |
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 | 270 | 0.56 | 0.76 | 28 | empty |
| 2 | 248 | 0.54 | 0.77 | 26 | empty |
| 3 | 70 | 0.34 | 0.74 | 14 | 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 Q9EV66
- Elsewhere: UniProt Q9EV66 · AlphaFold DB Q9EV66
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