3fr3

X-ray diffraction
1.9Å 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

Reaction catalysed:
RX + glutathione = HX + R-S-glutathione
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-184819 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 208 amino acids
Theoretical weight: 24.33 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8ILQ7 (Residues: 1-113, 119-211; Coverage: 98%)
Gene names: GST, PF14_0187, PF3D7_1419300
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GDS 2 x GDS
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: P21212
Unit cell:
a: 60.89Å b: 87.062Å c: 74.823Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.211 0.252
Expression system: Escherichia coli