› 8gss

X-ray diffraction
1.9Å resolution

Human glutathione S-transferase P1-1, complex with glutathione

Released:
DOI: 10.2210/pdb8gss/pdb
PDB entry 8gss coloured by chain, front view.
PDB entry 8gss coloured by chain, side view.
PDB entry 8gss coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The structures of human glutathione transferase P1-1 in complex with glutathione and various inhibitors at high resolution.
Oakley AJ, Lo Bello M, Battistoni A, Ricci G, Rossjohn J, Villar HO, Parker MW
J Mol Biol 274 84-100 (1997)
PMID: 9398518

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, C
Molecule details ›
Chains: A, B, C
Length: 209 amino acids
Theoretical weight: 23.25 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 3 x GSH
2 bound ligands:
Ligand SO4 2 x SO4
Ligand MES 2 x MES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: C2
Unit cell:
a: 121.891Å b: 85.716Å c: 81.733Å
α: 90° β: 110.63° γ: 90°
R-values:
R R work R free
0.193 0.193 0.229
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily.
Sheehan et al. (2001)
10 more

2 mentions without citation

A functionally conserved basic residue in glutathione transferases interacts with the glycine moiety of glutathione and is pivotal for enzyme catalysis.
Vararattanavech et al. (2007)
1 more