› 2aaw

X-ray diffraction
2.4Å resolution

Studies on ligand binding and enzyme inhibition of Plasmodium falciparum glutathione S-transferase

Released:
DOI: 10.2210/pdb2aaw/pdb
PDB entry 2aaw coloured by chain, front view.
PDB entry 2aaw coloured by chain, side view.
PDB entry 2aaw coloured by chain, top view.
Source organism: Plasmodium falciparum
Primary publication:
Plasmodium falciparum glutathione S-transferase--structural and mechanistic studies on ligand binding and enzyme inhibition.
Hiller N, Fritz-Wolf K, Deponte M, Wende W, Zimmermann H, Becker K
Protein Sci 15 281-9 (2006)
PMID: 16385005

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184818 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase Chains: A, C
Molecule details ›
Chains: A, C
Length: 222 amino acids
Theoretical weight: 26.09 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 GTX 2 x GTX
2 bound ligands:
Ligand P33 2 x P33
Ligand DTL 1 x DTL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 61.17Å b: 69.99Å c: 123.69Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.194 0.237
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes.
Deponte M. (2013)
7 more

5 mentions without citation

The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.
Ogungbe et al. (2016)
4 more