Function and Biology Details
Reactions catalysed:
Thioredoxin + ROOH = thioredoxin disulfide + H(2)O + ROH
Peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH = peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
Sulfiredoxin-1 and Peroxiredoxin-1 (preferred)
PDBe Complex ID:
PDB-CPX-170402 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peroxiredoxin-1
Molecule details ›
Chains: A, B
Length: 206 amino acids
Theoretical weight: 23.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains: Glutaredoxin
Length: 206 amino acids
Theoretical weight: 23.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
Q06830 (Residues: 1-199; Coverage: 100%)
Sequence domains:
Structure domains: Glutaredoxin
Sulfiredoxin-1
Molecule details ›
Chains: X, Y
Length: 110 amino acids
Theoretical weight: 11.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Structure domains: Conserved hypothetical protein from pyrococcus furiosus pfu- 392566-001, ParB domain
Length: 110 amino acids
Theoretical weight: 11.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: Q9BYN0 (Residues: 32-137; Coverage: 77%)
Structure domains: Conserved hypothetical protein from pyrococcus furiosus pfu- 392566-001, ParB domain
