› 1gnw

X-ray diffraction
2.2Å resolution

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155467 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase F2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 211 amino acids
Theoretical weight: 24.03 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: P46422 (Residues: 2-212; Coverage: 100%)
Gene names: At4g02520, GSTF2, PM24.1, T10P11.18
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GTX 4 x GTX
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P63
Unit cell:
a: 113.3Å b: 113.3Å c: 69.96Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.175 0.175 not available
Expression system: Escherichia coli

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Citations

16 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)
15 more

9 mentions without citation

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