› 3csj

X-ray diffraction
1.9Å resolution

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

3 bound ligands:
Ligand CL 1 x CL
Ligand MES 2 x MES
Ligand CBL 1 x CBL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: C2
Unit cell:
a: 77.84Å b: 89.93Å c: 69.07Å
α: 90° β: 97.7° γ: 90°
R-values:
R R work R free
0.179 0.176 0.233
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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

1 mention without citation

Supporting precision medicine by data mining across multi-disciplines: an integrative approach for generating comprehensive linkages between single nucleotide variants (SNVs) and drug-binding sites.
Roy Choudhury et al. (2017)