Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit H (A1SE34)
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
- A1SE34
- Type
- protein
- Length
- 449 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0EA189b2343A464f560b44103f6A3396Da1dA8a9
- Molecule
- NADH-quinone oxidoreductase subunit H
- UniProt
- A1SE34
- Pockets
- 6 · best druggability 0.76
Structure
1 distinct chain · 59% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit H | protein | 449 | 59% helix, 1% strand | A1SE34 |
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 84 | 0.76 | 0.97 | 26 | empty |
| 2 | 188 | 0.63 | 0.83 | 26 | empty |
| 3 | 293 | 0.57 | 0.77 | 36 | empty |
| 4 | 219 | 0.52 | 0.76 | 28 | empty |
| 5 | 88 | 0.42 | 0.79 | 19 | 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 A1SE34
- Elsewhere: UniProt A1SE34 · AlphaFold DB A1SE34
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