› 1m0t

X-ray diffraction
2.3Å resolution

Yeast Glutathione Synthase

Released:
DOI: 10.2210/pdb1m0t/pdb
PDB entry 1m0t coloured by chain, front view.
PDB entry 1m0t coloured by chain, side view.
PDB entry 1m0t coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Large conformational changes in the catalytic cycle of glutathione synthase.
Gogos A, Shapiro L
Structure 10 1669-76 (2002)
PMID: 12467574

Function and Biology Details

Reaction catalysed: 
ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-170614 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione synthetase GSH2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 491 amino acids
Theoretical weight: 55.88 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q08220 (Residues: 1-491; Coverage: 100%)
Gene names: GSH2, YOL049W
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 6 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 32-ID
Spacegroup: C2221
Unit cell:
a: 69.869Å b: 155.069Å c: 190.582Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.216 0.237
Expression system: Escherichia coli BL21

Quick links

Citations

3 review citations

Emerging regulatory paradigms in glutathione metabolism.
Liu et al. (2014)
2 more

2 mentions without citation

High-throughput computational and experimental techniques in structural genomics.
Chance et al. (2004)
1 more