› 3km6

X-ray diffraction
2.1Å resolution

Crystal Structure of the Human GST Pi C47S/Y108V Double Mutant in Complex with the Ethacrynic Acid-Glutathione Conjugate

Released:
DOI: 10.2210/pdb3km6/pdb
PDB entry 3km6 coloured by chain, front view.
PDB entry 3km6 coloured by chain, side view.
PDB entry 3km6 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Diuretic drug binding to human glutathione transferase P1-1: potential role of Cys-101 revealed in the double mutant C47S/Y108V.
Quesada-Soriano I, Parker LJ, Primavera A, Wielens J, Holien JK, Casas-Solvas JM, Vargas-Berenguel A, Aguilera AM, Nuccetelli M, Mazzetti AP, Lo Bello M, Parker MW, García-Fuentes L
J Mol Recognit 24 220-34
PMID: 20540076

Function and Biology Details

Reaction catalysed: 
RX + glutathione = HX + R-S-glutathione
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140593 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase P Chains: A, B
Molecule details ›
Chains: A, B
Length: 209 amino acids
Theoretical weight: 23.17 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09211 (Residues: 2-210; Coverage: 100%)
Gene names: FAEES3, GST3, GSTP1
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GSH 2 x GSH
2 bound ligands:
Ligand EAA 2 x EAA
Ligand CA 6 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: C2
Unit cell:
a: 75.876Å b: 89.242Å c: 69.206Å
α: 90° β: 89.89° γ: 90°
R-values:
R R work R free
0.155 0.153 0.206
Expression system: Escherichia coli

Quick links

Citations

8 citation in other articles

FDA-approved drugs and other compounds tested as inhibitors of human glutathione transferase P1-1.
Musdal et al. (2013)
7 more

1 mention without citation

The metabolic bioactivation of caffeic acid phenethyl ester (CAPE) mediated by tyrosinase selectively inhibits glutathione S-transferase.
Kudugunti et al. (2011)