Research workbench
AlphaFold monomer V2.0 prediction for FAD-linked oxidoreductase virf (G9N4A7)
Analyse AlphaFold monomer V2.0 prediction for FAD-linked oxidoreductase virf (G9N4A7) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- G9N4A7
- Type
- protein
- Length
- 451 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb4D2d9c96b0D792d0b77e7147D724cc1F801ae58
- Molecule
- FAD-linked oxidoreductase virf
- UniProt
- G9N4A7
- Pockets
- 2 · best druggability 0.87
Structure
1 distinct chain · 37% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | FAD-linked oxidoreductase virf | protein | 451 | 37% helix, 26% strand | G9N4A7 |
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 | 785 | 0.87 | 0.91 | 102 | empty |
| 2 | 65 | 0.34 | 0.77 | 18 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 G9N4A7
- Elsewhere: UniProt G9N4A7 · AlphaFold DB G9N4A7
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