› 2fno

X-ray diffraction
2Å resolution

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181466 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GST N-terminal domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 248 amino acids
Theoretical weight: 27.9 KDa
Source organism: Agrobacterium fabrum str. C58
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7D2W7 (Residues: 1-232; Coverage: 100%)
Gene names: Atu5508, gst
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SCN 4 x SCN
1 modified residue:
Ligand MSE 16 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: C2
Unit cell:
a: 110.204Å b: 50.261Å c: 117.66Å
α: 90° β: 115.72° γ: 90°
R-values:
R R work R free
0.183 0.181 0.219
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Glutathione transferases in bacteria.
Allocati et al. (2009)
1 more

1 mention without citation

Comparison of epsilon- and delta-class glutathione S-transferases: the crystal structures of the glutathione S-transferases DmGSTE6 and DmGSTE7 from Drosophila melanogaster.
Scian et al. (2015)