Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit H (Q8EI35)
Analyse AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit H… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q8EI35
- Type
- protein
- Length
- 322 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc65cB70a906CEEA439D51B5d816F369AA26D074F
- Molecule
- NADH-quinone oxidoreductase subunit H
- UniProt
- Q8EI35
- Pockets
- 3 · best druggability 0.51
Structure
1 distinct chain · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit H | protein | 322 | 72% helix, 0% strand | Q8EI35 |
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 | 145 | 0.51 | 0.79 | 19 | empty |
| 2 | 139 | 0.50 | 0.78 | 27 | empty |
| 3 | 148 | 0.48 | 0.78 | 23 | 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 Q8EI35
- Elsewhere: UniProt Q8EI35 · AlphaFold DB Q8EI35
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