Research workbench
AlphaFold monomer V2.0 prediction for NADH dehydrogenase (ubiquinone) complex I, assembly factor 6 (A7YVD7)
Analyse AlphaFold monomer V2.0 prediction for NADH dehydrogenase (ubiquinone) complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A7YVD7
- Type
- protein
- Length
- 333 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x18b6aa73f166Dd46ca6E15d135DF8033C4C01318
- Molecule
- NADH dehydrogenase (ubiquinone) complex I, assembly factor 6
- UniProt
- A7YVD7
- Pockets
- 2 · best druggability 0.76
Structure
1 distinct chain · 63% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH dehydrogenase (ubiquinone) complex I, assembly factor 6 | protein | 333 | 63% helix, 0% strand | A7YVD7 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 648 | 0.76 | 0.82 | 54 | empty |
| 2 | 60 | 0.30 | 0.75 | 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 A7YVD7
- Elsewhere: UniProt A7YVD7 · AlphaFold DB A7YVD7
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