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AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit H (Q9I0J5)
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
- Q9I0J5
- Type
- protein
- Length
- 331 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3132e98DE724412A5569A3600695F9Abcc9c375D
- Molecule
- NADH-quinone oxidoreductase subunit H
- UniProt
- Q9I0J5
- Pockets
- 4 · best druggability 0.53
Structure
1 distinct chain · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit H | protein | 331 | 72% helix, 0% strand | Q9I0J5 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 145 | 0.53 | 0.80 | 20 | empty |
| 2 | 168 | 0.51 | 0.77 | 22 | empty |
| 3 | 81 | 0.36 | 0.76 | 22 | empty |
| 4 | 51 | 0.29 | 0.74 | 11 | 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 Q9I0J5
- Elsewhere: UniProt Q9I0J5 · AlphaFold DB Q9I0J5
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