Research workbench
AlphaFold monomer V2.0 prediction for glutathione-dependent formaldehyde-activating enzyme (Q51669)
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
- Q51669
- Type
- protein
- Length
- 194 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7a1388B6Aad67B04634A32f63b8A6D6005eab86c
- Molecule
- Glutathione-dependent formaldehyde-activating enzyme
- UniProt
- Q51669
- Pockets
- 2 · best druggability 0.52
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 | Q51669 |
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 | 142 | 0.52 | 0.79 | 24 | empty |
| 2 | 102 | 0.50 | 0.82 | 19 | empty |
Compared structures
- 1X6M · Crystal structure of the glutathione-dependent formaldehyde-activating enzyme (gfa) · an experimental structure of the same protein · chain A against C, TM-score 0.99
- 1X6M · Crystal structure of the glutathione-dependent formaldehyde-activating enzyme (Gfa) · an experimental structure of the same protein · chain A against C, TM-score 0.99
- 1XA8 · Crystal Structure Analysis of Glutathione-dependent formaldehyde-activating enzyme (Gfa) · an experimental structure of the same protein · chain A against D, TM-score 0.99
- 1XA8 · Crystal structure analysis of glutathione-dependent formaldehyde- activating enzyme (gfa) · an experimental structure of the same protein · chain A against D, TM-score 0.99
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 Q51669
- Elsewhere: UniProt Q51669 · AlphaFold DB Q51669
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