Research workbench
AlphaFold monomer V2.0 prediction for hydroxyacylglutathione hydrolase, mitochondrial (Q16775)
Analyse AlphaFold monomer V2.0 prediction for hydroxyacylglutathione hydrolase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q16775
- Type
- protein
- Length
- 308 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4Ef77Afb5a3D9F41c95Be3227D1CC986CCb61835
- UniProt
- Q16775
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 308 | — | Q16775 |
Compared structures
- 1QH5 · Human glyoxalase II with S-(N-hydroxy-N-bromophenylcarbamoyl) glutathione · an experimental structure of the same protein · chain A against B, TM-score 0.84
- 1QH5 · Human glyoxalase II with S-(N-hydroxy-N-BROMOPHENYLCARBAMOYL)GLUTATHIONE · an experimental structure of the same protein · chain A against B, TM-score 0.84
- 1QH3 · Human glyoxalase II with cacodylate and acetate ions present in the active site · an experimental structure of the same protein · chain A against A, TM-score 0.84
- 1QH3 · Human glyoxalase II with cacodylate and acetate ions present in the active site · an experimental structure of the same protein · chain A against A, TM-score 0.84
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 Q16775
- Elsewhere: UniProt Q16775 · AlphaFold DB Q16775
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