› 3mak

X-ray diffraction
1.8Å resolution

Crystal structure of Glutathione transferase dmGSTD1 from Drosophila melanogaster, in complex with glutathione

Released:
DOI: 10.2210/pdb3mak/pdb
PDB entry 3mak coloured by chain, front view.
PDB entry 3mak coloured by chain, side view.
PDB entry 3mak coloured by chain, top view.
Source organism: Drosophila melanogaster
Primary publication:
Structural evidence for conformational changes of Delta class glutathione transferases after ligand binding.
Wongsantichon J, Robinson RC, Ketterman AJ
Arch Biochem Biophys 521 77-83 (2012)
PMID: 22475449

Function and Biology Details

Reactions catalysed: 
RX + glutathione = HX + R-S-glutathione
1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane = 1,1-dichloro-2,2-bis(4-chlorophenyl)ethylene + chloride
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148971 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase D1 Chain: A
Molecule details ›
Chain: A
Length: 209 amino acids
Theoretical weight: 23.89 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P20432 (Residues: 1-209; Coverage: 100%)
Gene names: CG10045, GST, GSTD1-1, Gst1, GstD1
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GSH 1 x GSH
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: C2
Unit cell:
a: 71.352Å b: 63.137Å c: 54.24Å
α: 90° β: 129.55° γ: 90°
R-values:
R R work R free
0.162 0.16 0.2
Expression system: Escherichia coli BL21(DE3)

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Citations

6 citation in other articles

Mechanistic studies of FosB: a divalent-metal-dependent bacillithiol-S-transferase that mediates fosfomycin resistance in Staphylococcus aureus.
Roberts et al. (2013)
5 more

4 mentions without citation

Functional and Structural Diversity of Insect Glutathione S-transferases in Xenobiotic Adaptation.
Koirala B K et al. (2022)
3 more