› 6ep6

X-ray diffraction
1.59Å resolution

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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase U23 Chains: A, B
Molecule details ›
Chains: A, B
Length: 220 amino acids
Theoretical weight: 25.71 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9M9F1 (Residues: 1-220; Coverage: 100%)
Gene names: At1g78320, F3F9.14, GSTU23
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MG 2 x MG
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: C2
Unit cell:
a: 88.597Å b: 50.449Å c: 113.702Å
α: 90° β: 108.66° γ: 90°
R-values:
R R work R free
0.19 0.189 0.22
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Reactive oxygen species signalling in plant stress responses.
Mittler et al. (2022)
1 more

1 mention without citation

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