Research workbench
AlphaFold monomer V2.0 prediction for hydroxyacylglutathione hydrolase (Q12BV7)
Analyse AlphaFold monomer V2.0 prediction for hydroxyacylglutathione hydrolase (Q12BV7) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q12BV7
- Type
- protein
- Length
- 263 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6Ed09D80e98fE15DE51C9E7a8896AbF1f2365C3e
- Molecule
- Hydroxyacylglutathione hydrolase
- UniProt
- Q12BV7
- Pockets
- 1 · best druggability 0.35
Structure
1 distinct chain · 36% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hydroxyacylglutathione hydrolase | protein | 263 | 36% helix, 24% strand | Q12BV7 |
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 | 86 | 0.35 | 0.75 | 21 | 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 Q12BV7
- Elsewhere: UniProt Q12BV7 · AlphaFold DB Q12BV7
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