Research workbench
AlphaFold monomer V2.0 prediction for NADPH-dependent oxidoreductase (Q6GC90)
Analyse AlphaFold monomer V2.0 prediction for NADPH-dependent oxidoreductase (Q6GC90) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q6GC90
- Type
- protein
- Length
- 251 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xE98bd0722a8eEb0377b675F85e9ceBC2DbC988D6
- Molecule
- NADPH-dependent oxidoreductase
- UniProt
- Q6GC90
- Pockets
- 1 · best druggability 0.33
Structure
1 distinct chain · 50% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADPH-dependent oxidoreductase | protein | 251 | 50% helix, 12% strand | Q6GC90 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 77 | 0.33 | 0.74 | 15 | 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 Q6GC90
- Elsewhere: UniProt Q6GC90 · AlphaFold DB Q6GC90
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