› 1axd

X-ray diffraction
2.5Å resolution

STRUCTURE OF GLUTATHIONE S-TRANSFERASE-I BOUND WITH THE LIGAND LACTOYLGLUTATHIONE

Released:
DOI: 10.2210/pdb1axd/pdb
PDB entry 1axd coloured by chain, front view.
PDB entry 1axd coloured by chain, side view.
PDB entry 1axd coloured by chain, top view.
Source organism: Zea mays
Primary publication:
Crystal structure of herbicide-detoxifying maize glutathione S-transferase-I in complex with lactoylglutathione: evidence for an induced-fit mechanism.
Neuefeind T, Huber R, Dasenbrock H, Prade L, Bieseler B
J Mol Biol 274 446-53 (1997)
PMID: 9417926

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:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146292 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Glutathione S-transferase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 209 amino acids
Theoretical weight: 23.33 KDa
Source organism: Zea mays
Expression system: Escherichia coli
UniProt:
  • Canonical: P12653 (Residues: 2-210; Coverage: 98%)
Gene name: GST1
Sequence domains:
Structure domains:
LACTOYLGLUTATHIONE Chains: C, D
Molecule details ›
Chains: C, D
Length: 3 amino acids
Theoretical weight: 379 Da
Source organism: Zea mays

Ligands and Environments

No bound ligands
2 modified residues:
Ligand GGL 2 x GGL
Ligand CYW 2 x CYW

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P21
Unit cell:
a: 54.54Å b: 78.91Å c: 55.61Å
α: 90° β: 107.24° γ: 90°
R-values:
R R work R free
0.174 0.174 not available
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

10 mentions without citation

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