Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit H (B9JD51)
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
- B9JD51
- Type
- protein
- Length
- 347 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xcb1EC5B5B6ffa5F727AeFD9fa20a78E85ca3141c
- Molecule
- NADH-quinone oxidoreductase subunit H
- UniProt
- B9JD51
- Pockets
- 4 · best druggability 0.77
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 | B9JD51 |
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 | 99 | 0.77 | 0.97 | 32 | empty |
| 2 | 266 | 0.60 | 0.79 | 27 | empty |
| 3 | 159 | 0.57 | 0.80 | 17 | empty |
| 4 | 148 | 0.49 | 0.78 | 24 | 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 B9JD51
- Elsewhere: UniProt B9JD51 · AlphaFold DB B9JD51
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