Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit H (Q1LPV6)
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
- Q1LPV6
- Type
- protein
- Length
- 354 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xC17d31fe90ba2F028F3A7B668B9af47b13aB2683
- Molecule
- NADH-quinone oxidoreductase subunit H
- UniProt
- Q1LPV6
- Pockets
- 3 · best druggability 0.76
Structure
1 distinct chain · 71% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit H | protein | 354 | 71% helix, 1% strand | Q1LPV6 |
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 100 | 0.76 | 0.97 | 30 | empty |
| 2 | 296 | 0.60 | 0.78 | 28 | empty |
| 3 | 295 | 0.55 | 0.76 | 28 | 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 Q1LPV6
- Elsewhere: UniProt Q1LPV6 · AlphaFold DB Q1LPV6
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