PDBe 1va6

X-ray diffraction
2.1Å resolution

Crystal structure of Gamma-glutamylcysteine synthetase from Escherichia Coli B complexed with Transition-state analogue


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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Glutamate--cysteine ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 518 amino acids
Theoretical weight: 58.27 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 modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P21
Unit cell:
a: 70.468Å b: 97.36Å c: 102.185Å
α: 90° β: 109.63° γ: 90°
R R work R free
0.2 0.2 0.225
Expression system: Escherichia coli