Research workbench
AlphaFold monomer V2.0 prediction for glutathione-dependent formaldehyde-activating enzyme (A1AXY8)
Analyse AlphaFold monomer V2.0 prediction for glutathione-dependent… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A1AXY8
- Type
- protein
- Length
- 194 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x35612D34a32C306CA4fc1edA9360D1F717e25950
- Molecule
- Glutathione-dependent formaldehyde-activating enzyme
- UniProt
- A1AXY8
- Pockets
- 2 · best druggability 0.57
Structure
1 distinct chain · 23% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione-dependent formaldehyde-activating enzyme | protein | 194 | 23% helix, 25% strand | A1AXY8 |
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 | 144 | 0.57 | 0.81 | 30 | empty |
| 2 | 99 | 0.52 | 0.83 | 18 | 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 A1AXY8
- Elsewhere: UniProt A1AXY8 · AlphaFold DB A1AXY8
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