Research workbench
AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit H 1 (Q67P15)
Analyse AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit H 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q67P15
- Type
- protein
- Length
- 328 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf4ED13986579E8e227b3ED6c02276c648754EC27
- Molecule
- NADH-quinone oxidoreductase subunit H 1
- UniProt
- Q67P15
- Pockets
- 4 · best druggability 0.74
Structure
1 distinct chain · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit H 1 | protein | 328 | 71% helix, 0% strand | Q67P15 |
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 | 75 | 0.74 | 0.97 | 24 | empty |
| 2 | 307 | 0.63 | 0.79 | 28 | empty |
| 3 | 188 | 0.55 | 0.79 | 32 | empty |
| 4 | 78 | 0.34 | 0.74 | 13 | 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 Q67P15
- Elsewhere: UniProt Q67P15 · AlphaFold DB Q67P15
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