› 1aw9

X-ray diffraction
2.2Å 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 hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195697 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
glutathione transferase Chain: A
Molecule details ›
Chain: A
Length: 216 amino acids
Theoretical weight: 23.46 KDa
Source organism: Zea mays
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9ZP62 (Residues: 2-217; Coverage: 98%)
Gene name: gst3a
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CD 5 x CD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P6322
Unit cell:
a: 97.77Å b: 97.77Å c: 116.45Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.197 0.197 not available
Expression system: Escherichia coli

Quick links

Citations

9 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)
8 more

2 mentions without citation

Functional, Structural and Biochemical Features of Plant Serinyl-Glutathione Transferases.
Sylvestre-Gonon et al. (2019)
1 more