› 5dak

X-ray diffraction
2.11Å resolution

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

Released:
DOI: 10.2210/pdb5dak/pdb
PDB entry 5dak coloured by chain, front view.
PDB entry 5dak coloured by chain, side view.
PDB entry 5dak 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: 23.38 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:
Glutathione S-transferase P Chain: B
Molecule details ›
Chain: B
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:

Ligands and Environments

2 bound ligands:
Ligand MES 2 x MES
Ligand ARS 2 x ARS
1 modified residue:
Ligand CSO 1 x CSO

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Spacegroup: C2
Unit cell:
a: 74.629Å b: 95.509Å c: 68.247Å
α: 90° β: 98.26° γ: 90°
R-values:
R R work R free
0.159 0.157 0.204
Expression system: Escherichia coli

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