› 3hjm

X-ray diffraction
2.1Å 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, C, D
Molecule details ›
Chains: A, B, C, D
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

5 bound ligands:
Ligand MES 3 x MES
Ligand CA 5 x CA
Ligand CO3 5 x CO3
Ligand CL 3 x CL
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P21
Unit cell:
a: 69.002Å b: 90.393Å c: 75.981Å
α: 90° β: 97.49° γ: 90°
R-values:
R R work R free
0.18 0.18 0.23
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)