› 3tb2

X-ray diffraction
2.3Å resolution

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183147 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thioredoxin domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 220 amino acids
Theoretical weight: 25.36 KDa
Source organism: Plasmodium yoelii
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q86SB3 (Residues: 1-220; Coverage: 100%)
Gene names: PY17X_1231500, PYYM_1230700
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand SO4 5 x SO4
Ligand GOL 4 x GOL
Ligand EDO 21 x EDO
1 modified residue:
Ligand CSD 4 x CSD

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: C2221
Unit cell:
a: 90.39Å b: 156.842Å c: 178.075Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.166 0.203
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

34 review citations

Structure-based insights into the catalytic power and conformational dexterity of peroxiredoxins.
Hall et al. (2011)
33 more

3 mentions without citation

Observed octameric assembly of a Plasmodium yoelii peroxiredoxin can be explained by the replacement of native "ball-and-socket" interacting residues by an affinity tag.
Gretes et al. (2013)
2 more