Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit H (B9JVF3)
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
- B9JVF3
- Type
- protein
- Length
- 347 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xEa58c7534E5701aA8370E0fAEb19b7e14653e69c
- Molecule
- NADH-quinone oxidoreductase subunit H
- UniProt
- B9JVF3
- Pockets
- 4 · best druggability 0.75
Structure
1 distinct chain · 72% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit H | protein | 347 | 72% helix, 1% strand | B9JVF3 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 81 | 0.75 | 0.98 | 22 | empty |
| 2 | 290 | 0.58 | 0.77 | 31 | empty |
| 3 | 147 | 0.56 | 0.81 | 19 | empty |
| 4 | 99 | 0.42 | 0.77 | 18 | 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 B9JVF3
- Elsewhere: UniProt B9JVF3 · AlphaFold DB B9JVF3
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