› 5kej

X-ray diffraction
2.35Å resolution

Crystallographic structure of the Tau class glutathione S-transferase MiGSTU in complex with S-hexyl-glutathione

Released:
DOI: 10.2210/pdb5kej/pdb
PDB entry 5kej coloured by chain, front view.
PDB entry 5kej coloured by chain, side view.
PDB entry 5kej coloured by chain, top view.
Source organism: Mangifera indica
Primary publication:
Insights into ligand binding to a glutathione S-transferase from mango: Structure, thermodynamics and kinetics.
Valenzuela-Chavira I, Contreras-Vergara CA, Arvizu-Flores AA, Serrano-Posada H, Lopez-Zavala AA, García-Orozco KD, Hernandez-Paredes J, Rudiño-Piñera E, Stojanoff V, Sotelo-Mundo RR, Islas-Osuna MA
Biochimie 135 35-45 (2017)
PMID: 28104507

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-495932 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
glutathione transferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 229 amino acids
Theoretical weight: 25.55 KDa
Source organism: Mangifera indica
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A1P8NWC2 (Residues: 1-229; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GTX 2 x GTX
1 bound ligand:
Ligand PEG 6 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL14-1
Spacegroup: P212121
Unit cell:
a: 64.319Å b: 88.805Å c: 96.583Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.188 0.226
Expression system: Escherichia coli BL21(DE3)

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Citations

10 citation in other articles

Is there a role for tau glutathione transferases in tetrapyrrole metabolism and retrograde signalling in plants?
Sylvestre-Gonon et al. (2020)
9 more

2 mentions without citation

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