PDBe 1v4g

X-ray diffraction
2.5Å resolution

Crystal Structure of gamma-Glutamylcysteine Synthetase from Escherichia coli B


Function and Biology Details

Reaction catalysed:
ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Glutamate--cysteine ligase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 518 amino acids
Theoretical weight: 58.3 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
  • Canonical: P0A6W9 (Residues: 1-518; Coverage: 100%)
Gene names: JW2663, b2688, gsh-I, gshA
Sequence domains: Glutamate-cysteine ligase
Structure domains: Creatine Kinase; Chain A, domain 2

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: R3
Unit cell:
a: 326.818Å b: 326.818Å c: 104.726Å
α: 90° β: 90° γ: 120°
R R work R free
0.207 0.206 0.236
Expression system: Escherichia coli