6e0g

Electron Microscopy
2.9Å resolution

Mitochondrial peroxiredoxin from Leishmania infantum after heat stress without unfolding client protein

Released:

Function and Biology Details

Reaction catalysed:
Thioredoxin + ROOH = thioredoxin disulfide + H(2)O + ROH
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo decamer (preferred)
PDBe Complex ID:
PDB-CPX-105664 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
thioredoxin-dependent peroxiredoxin Chains: A, B, C, D, E, F, G, H, I, J
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J
Length: 226 amino acids
Theoretical weight: 25.4 KDa
Source organism: Leishmania infantum
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A6L0XFC6 (Residues: 1-226; Coverage: 100%)
Gene names: LINJ_23_0050, mTXNPx, tryparedoxin peroxidase
Sequence domains:
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.9Å
Relevant EMDB volumes: EMD-8947
Expression system: Escherichia coli