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Structural basis of the thiol resolving mechanism in yeast mitochondrial 1-cys peroxiredoxin via GLUTATHIONE/THIOREDOXIN systems
Analyse Structural basis of the thiol resolving mechanism in yeast mitochondrial 1-cys… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5YKJ
- Type
- protein
- Length
- 213 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peroxiredoxin PRX1, mitochondrial
- EC
- 1.11.1.15
- UniProt
- P34227
- Ligands
- NA
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peroxiredoxin PRX1, mitochondrial (EC 1.11.1.15) | protein | 213 | 31% helix, 22% strand | P34227 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 modified (oxidation).
Compared structures
- 5YKJ · Structural basis of the thiol resolving mechanism in yeast mitochondrial 1-Cys… · the same entry in another collection · chain A against A, TM-score 1.00
- P34227 · AlphaFold monomer V2.0 prediction for peroxiredoxin PRX1, mitochondrial (P34227) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 P34227
- Elsewhere: RCSB PDB 5YKJ · PDBe 5YKJ · UniProt P34227
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