2vl2

X-ray diffraction
1.92Å resolution

Oxidized and reduced forms of human peroxiredoxin 5

Released:

Function and Biology Details

Reaction catalysed:
2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo dimer
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peroxiredoxin-5, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 172 amino acids
Theoretical weight: 18.21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli M15
UniProt:
  • Canonical: P30044 (Residues: 54-214; Coverage: 75%)
Gene names: ACR1, PRDX5, SBBI10
Sequence domains: Redoxin
Structure domains: Glutaredoxin
Peroxiredoxin-5, mitochondrial Chain: C
Molecule details ›
Chain: C
Length: 172 amino acids
Theoretical weight: 18.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli M15
UniProt:
  • Canonical: P30044 (Residues: 54-214; Coverage: 75%)
Gene names: ACR1, PRDX5, SBBI10
Sequence domains: Redoxin
Structure domains: Glutaredoxin

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: C2221
Unit cell:
a: 79.067Å b: 102.016Å c: 146.643Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.205 0.255
Expression system: Escherichia coli M15