Research workbench
AlphaFold monomer V2.0 prediction for peroxiredoxin TSA2 (Q04120)
Analyse AlphaFold monomer V2.0 prediction for peroxiredoxin TSA2 (Q04120) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q04120
- Type
- protein
- Length
- 196 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x35612D34a32C306CA4fc1edA9360D1F717e25950
- Molecule
- Peroxiredoxin TSA2
- UniProt
- Q04120
Structure
1 distinct chain · 32% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peroxiredoxin TSA2 | protein | 196 | 32% helix, 25% strand | Q04120 |
Compared structures
- 5EPT · Crystal structure of S. cerevisiae TSA2 in the disulfide state · an experimental structure of the same protein · chain A against H, TM-score 0.85
- 5EPT · Crystal Structure of S. cerevisiae TSA2 in the disulfide state · an experimental structure of the same protein · chain A against H, TM-score 0.85
- 6UTL · Yeast Thiol Specific antoxidant 2 with C171S mutation and catalytic cysteine alkylated… · an experimental structure of the same protein · chain A against H, TM-score 0.83
- 6UTL · Yeast thiol specific antoxidant 2 with C171S mutation and catalytic cysteine alkylated… · an experimental structure of the same protein · chain A against A, TM-score 0.83
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 Q04120
- Elsewhere: UniProt Q04120 · AlphaFold DB Q04120
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