› 1gsa

X-ray diffraction
2Å resolution

STRUCTURE OF GLUTATHIONE SYNTHETASE COMPLEXED WITH ADP AND GLUTATHIONE

Released:
DOI: 10.2210/pdb1gsa/pdb
PDB entry 1gsa coloured by chain, front view.
PDB entry 1gsa coloured by chain, side view.
PDB entry 1gsa coloured by chain, top view.
Source organism: Escherichia coli B
Primary publication:
A pseudo-michaelis quaternary complex in the reverse reaction of a ligase: structure of Escherichia coli B glutathione synthetase complexed with ADP, glutathione, and sulfate at 2.0 A resolution.
Hara T, Kato H, Katsube Y, Oda J
Biochemistry 35 11967-74 (1996)
PMID: 8810901

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 tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137639 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione synthetase Chain: A
Molecule details ›
Chain: A
Length: 316 amino acids
Theoretical weight: 35.6 KDa
Source organism: Escherichia coli B
Expression system: Escherichia coli
UniProt:
  • Canonical: P04425 (Residues: 1-316; Coverage: 100%)
Gene names: JW2914, b2947, gsh-II, gshB
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GSH 1 x GSH
3 bound ligands:
Ligand MG 2 x MG
Ligand SO4 1 x SO4
Ligand ADP 1 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P6222
Unit cell:
a: 87.25Å b: 87.25Å c: 169.58Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.188 0.188 not available
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Phosphatidylinositol phosphate kinase: a link between protein kinase and glutathione synthase folds.
Grishin NV. (1999)
1 more

11 mentions without citation

A normalized root-mean-square distance for comparing protein three-dimensional structures.
Carugo et al. (2001)
10 more