› 4png

X-ray diffraction
1.53Å resolution

Glutathione S-transferase from Drosophila melanogaster - isozyme E7

Released:
DOI: 10.2210/pdb4png/pdb
PDB entry 4png coloured by chain, front view.
PDB entry 4png coloured by chain, side view.
PDB entry 4png coloured by chain, top view.
Source organism: Drosophila melanogaster
Primary publication:
Comparison of epsilon- and delta-class glutathione S-transferases: the crystal structures of the glutathione S-transferases DmGSTE6 and DmGSTE7 from Drosophila melanogaster.
Scian M, Le Trong I, Mazari AM, Mannervik B, Atkins WM, Stenkamp RE
Acta Crystallogr D Biol Crystallogr 71 2089-98 (2015)
PMID: 26457432

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-106798 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S transferase E7 Chains: A, B
Molecule details ›
Chains: A, B
Length: 229 amino acids
Theoretical weight: 26.37 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli
UniProt:
  • Canonical: A1ZB72 (Residues: 1-223; Coverage: 100%)
Gene names: CG17531, DmGSTE7, Dmel\CG17531, Dmel_CG17531, E7, GST-E7, GSTE7, GstE7, gstE7, gste7
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GSF 2 x GSF
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P212121
Unit cell:
a: 56.731Å b: 87.09Å c: 87.226Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.158 0.191
Expression system: Escherichia coli

Quick links

Citations

1 review citation

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

4 mentions without citation

An integrated approach to unravel a crucial structural property required for the function of the insect steroidogenic Halloween protein Noppera-bo.
Koiwai et al. (2020)
3 more