Function and Biology Details
Reactions catalysed:
Catalyzes the rearrangement of -S-S- bonds in proteins
Thioredoxin + ROOH = thioredoxin disulfide + H(2)O + ROH
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126678 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protein disulfide-isomerase A6
Molecule details ›
Chains: A, B
Length: 142 amino acids
Theoretical weight: 15.64 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Thioredoxin
Structure domains: Glutaredoxin
Length: 142 amino acids
Theoretical weight: 15.64 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
Q15084 (Residues: 20-140; Coverage: 29%)
Sequence domains: Thioredoxin
Structure domains: Glutaredoxin
Peroxiredoxin-4
Molecule details ›
Chains: C, D
Length: 20 amino acids
Theoretical weight: 2.09 KDa
Source organism: Mus musculus
Expression system: Not provided
UniProt:
Sequence domains: C-terminal domain of 1-Cys peroxiredoxin
Length: 20 amino acids
Theoretical weight: 2.09 KDa
Source organism: Mus musculus
Expression system: Not provided
UniProt:
- Canonical: O08807 (Residues: 244-263; Coverage: 9%)
Sequence domains: C-terminal domain of 1-Cys peroxiredoxin
