› 10gs

X-ray diffraction
2.2Å resolution

HUMAN GLUTATHIONE S-TRANSFERASE P1-1, COMPLEX WITH TER117

Released:
DOI: 10.2210/pdb10gs/pdb
PDB entry 10gs coloured by chain, front view.
PDB entry 10gs coloured by chain, side view.
PDB entry 10gs 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
Molecule details ›
Chains: A, B
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 VWW 2 x VWW
1 bound ligand:
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: 79.723Å b: 90.46Å c: 69.404Å
α: 90° β: 98.19° γ: 90°
R-values:
R R work R free
0.176 0.176 0.214
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

17 mentions without citation

Molecular regulations and therapeutic targets of Gaucher disease.
Chen et al. (2018)
16 more