Research workbench
AlphaFold monomer V2.0 prediction for FAD-linked oxidoreductase OXR1 (G4N285)
Analyse AlphaFold monomer V2.0 prediction for FAD-linked oxidoreductase OXR1 (G4N285) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- G4N285
- Type
- protein
- Length
- 507 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x822BfDB52f100Af7414C872a89eE1bfF1069766B
- Molecule
- FAD-linked oxidoreductase OXR1
- UniProt
- G4N285
- Pockets
- 2 · best druggability 0.85
Structure
1 distinct chain · 35% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | FAD-linked oxidoreductase OXR1 | protein | 507 | 35% helix, 22% strand | G4N285 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 622 | 0.85 | 0.90 | 74 | empty |
| 2 | 296 | 0.55 | 0.76 | 40 | 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 G4N285
- Elsewhere: UniProt G4N285 · AlphaFold DB G4N285
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