› 5dal

X-ray diffraction
1.5Å resolution

Crystal Structure of human Glutathione Transferase Pi complexed with a metalloid in the presence of Glutathione

Released:
DOI: 10.2210/pdb5dal/pdb
PDB entry 5dal coloured by chain, front view.
PDB entry 5dal coloured by chain, side view.
PDB entry 5dal coloured by chain, top view.
Source organism: Homo sapiens
Entry authors: Parker LJ, Parker MW, Morton CJ

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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140592 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Glutathione S-transferase P Chain: A
Molecule details ›
Chain: A
Length: 210 amino acids
Theoretical weight: 23.39 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:
Glutathione S-transferase P Chain: B
Molecule details ›
Chain: B
Length: 210 amino acids
Theoretical weight: 23.38 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 5AU 2 x 5AU

Cofactor: Ligand GSH 2 x GSH
3 bound ligands:
Ligand MES 2 x MES
Ligand PA0 2 x PA0
Ligand SO4 1 x SO4
1 modified residue:
Ligand CSO 1 x CSO

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: C2
Unit cell:
a: 77.55Å b: 90.22Å c: 68.67Å
α: 90° β: 98.01° γ: 90°
R-values:
R R work R free
0.181 0.18 0.212
Expression system: Escherichia coli

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