3frc

X-ray diffraction
2Å resolution

Tetramerization and Cooperativity in Plasmodium falciparum glutathione transferase are mediated by the atypic loop 113-118

Released:
Source organism: Plasmodium falciparum
Entry authors: Perbandt M, Liebau E, Ricci G

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-184818 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 211 amino acids
Theoretical weight: 24.82 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8ILQ7 (Residues: 1-211; Coverage: 100%)
Gene names: GST, PF14_0187, PF3D7_1419300
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand 0HG 2 x 0HG
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: P212121
Unit cell:
a: 57.472Å b: 69.407Å c: 123.323Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.22 0.268
Expression system: Escherichia coli