› 3hkr

X-ray diffraction
1.8Å resolution

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:
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: 23.18 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 CA 5 x CA
Ligand MES 2 x MES
Ligand CO3 3 x CO3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Spacegroup: C2
Unit cell:
a: 77.1Å b: 90.3Å c: 68.9Å
α: 90° β: 98.2° γ: 90°
R-values:
R R work R free
0.17 0.17 0.21
Expression system: Escherichia coli

Quick links

Citations

10 citation in other articles

Chemical proteomics with sulfonyl fluoride probes reveals selective labeling of functional tyrosines in glutathione transferases.
Gu et al. (2013)
9 more

1 mention without citation

Influence of the H-site residue 108 on human glutathione transferase P1-1 ligand binding: structure-thermodynamic relationships and thermal stability.
Quesada-Soriano et al. (2009)