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AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit C/D (A5FXJ8)
Analyse AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit C/D… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5FXJ8
- Type
- protein
- Length
- 592 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x92f96107f8fA08E20b96ef0480Fa095378eF082F
- Molecule
- NADH-quinone oxidoreductase subunit C/D
- UniProt
- A5FXJ8
- Pockets
- 6 · best druggability 0.64
Structure
1 distinct chain · 41% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH-quinone oxidoreductase subunit C/D | protein | 592 | 41% helix, 16% strand | A5FXJ8 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 394 | 0.64 | 0.78 | 50 | empty |
| 2 | 359 | 0.62 | 0.78 | 35 | empty |
| 3 | 134 | 0.46 | 0.77 | 18 | empty |
| 4 | 56 | 0.43 | 0.83 | 14 | empty |
| 5 | 50 | 0.27 | 0.75 | 14 | 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 A5FXJ8
- Elsewhere: UniProt A5FXJ8 · AlphaFold DB A5FXJ8
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