Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit H 1 (Q13BG9)
Analyse AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit H 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q13BG9
- Type
- protein
- Length
- 319 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB7950E95eAd230FCC2CE18A361294b6999077050
- Molecule
- NADH-quinone oxidoreductase subunit H 1
- UniProt
- Q13BG9
- Pockets
- 2 · best druggability 0.60
Structure
1 distinct chain · 73% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit H 1 | protein | 319 | 73% helix, 0% strand | Q13BG9 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 251 | 0.60 | 0.79 | 28 | empty |
| 2 | 168 | 0.48 | 0.76 | 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 Q13BG9
- Elsewhere: UniProt Q13BG9 · AlphaFold DB Q13BG9
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