Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit H (C3JY87)
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
- C3JY87
- Type
- protein
- Length
- 335 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x769063e6fD12eaBbc955d6025BD35BF88Ab86D4D
- Molecule
- NADH-quinone oxidoreductase subunit H
- UniProt
- C3JY87
- Pockets
- 4 · best druggability 0.71
Structure
1 distinct chain · 73% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit H | protein | 335 | 73% helix, 1% strand | C3JY87 |
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 | 60 | 0.71 | 0.97 | 21 | empty |
| 2 | 266 | 0.59 | 0.78 | 40 | empty |
| 3 | 243 | 0.58 | 0.78 | 24 | empty |
| 4 | 55 | 0.29 | 0.74 | 12 | 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 C3JY87
- Elsewhere: UniProt C3JY87 · AlphaFold DB C3JY87
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