› 4uss

X-ray diffraction
2.5Å resolution

Populus trichocarpa glutathione transferase X1-1 (GHR1), complexed with glutathione

Released:
DOI: 10.2210/pdb4uss/pdb
PDB 4uss coloured by chain and viewed from the front.
PDB 4uss coloured by chain and viewed from the side.
PDB 4uss coloured by chain and viewed from the top.
Source organism: Populus trichocarpa
Primary publication:
Glutathionyl-hydroquinone reductases from poplar are plastidial proteins that deglutathionylate both reduced and oxidized quinones.
Lallement PA, Meux E, Gualberto JM, Dumarcay S, Favier F, Didierjean C, Saul F, Haouz A, Morel-Rouhier M, Gelhaye E, Rouhier N, Hecker A
FEBS Lett. (2014)
PMID: 25455804

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GLUTATHIONYL HYDROQUINONE REDUCTASE Chain: A
Molecule details ›
Chain: A
Length: 325 amino acids
Theoretical weight: 37.18 KDa
Source organism: Populus trichocarpa
Expression system: Escherichia coli
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand GSH 1 x GSH
Ligand PO4 2 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P21212
Unit cell:
a: 36.53Å b: 92.409Å c: 86.901Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.183 0.233
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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

2 mentions without citation

Crystal Structure of Saccharomyces cerevisiae ECM4, a Xi-Class Glutathione Transferase that Reacts with Glutathionyl-(hydro)quinones.
Schwartz et al. (2016)
1 more