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AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit H (A6V4E2)
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
- A6V4E2
- Type
- protein
- Length
- 331 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x93bc14F5480294582746A78146D4954f61e03248
- Molecule
- NADH-quinone oxidoreductase subunit H
- UniProt
- A6V4E2
- Pockets
- 4 · best druggability 0.71
Structure
1 distinct chain · 73% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit H | protein | 331 | 73% helix, 0% strand | A6V4E2 |
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 | 20 | empty |
| 2 | 144 | 0.51 | 0.79 | 27 | empty |
| 3 | 163 | 0.50 | 0.77 | 24 | empty |
| 4 | 134 | 0.46 | 0.77 | 20 | 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 A6V4E2
- Elsewhere: UniProt A6V4E2 · AlphaFold DB A6V4E2
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