› 1pgt

X-ray diffraction
1.8Å resolution

CRYSTAL STRUCTURE OF HUMAN GLUTATHIONE S-TRANSFERASE P1-1[V104] COMPLEXED WITH S-HEXYLGLUTATHIONE

Released:
DOI: 10.2210/pdb1pgt/pdb
PDB entry 1pgt coloured by chain, front view.
PDB entry 1pgt coloured by chain, side view.
PDB entry 1pgt coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure and function of the xenobiotic substrate-binding site and location of a potential non-substrate-binding site in a class pi glutathione S-transferase.
Ji X, Tordova M, O'Donnell R, Parsons JF, Hayden JB, Gilliland GL, Zimniak P
Biochemistry 36 9690-702 (1997)
PMID: 9245401

Function and Biology Details

Reaction catalysed: 
RX + glutathione = HX + R-S-glutathione
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure 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: 210 amino acids
Theoretical weight: 23.36 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09211 (Residues: 1-210; Coverage: 100%)
Gene names: FAEES3, GST3, GSTP1
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GTX 2 x GTX
1 bound ligand:
Ligand EPE 2 x EPE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: C2
Unit cell:
a: 79.39Å b: 90.8Å c: 69.15Å
α: 90° β: 98.08° γ: 90°
R-values:
R R work R free
0.182 0.182 not available
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Glutathione transferases: a structural perspective.
Oakley A. (2011)
5 more

2 mentions without citation

Glutathione transferases are structural and functional outliers in the thioredoxin fold.
Atkinson et al. (2009)
1 more