2d32

X-ray diffraction
2.4Å resolution

Crystal Structure of Michaelis Complex of gamma-Glutamylcysteine Synthetase

Released:
Source organism: Escherichia coli
Entry authors: Hibi T, Nakayama M, Nii H, Kurokawa Y, Katano H, Oda J

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

Assemblies composition:
homo tetramer (preferred)
homo dodecamer
PDBe Complex ID:
PDB-CPX-141438 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate--cysteine ligase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 518 amino acids
Theoretical weight: 58.27 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6W9 (Residues: 1-518; Coverage: 100%)
Gene names: JW2663, b2688, gsh-I, gshA
Sequence domains: Glutamate-cysteine ligase
Structure domains:

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: R3
Unit cell:
a: 325.53Å b: 325.53Å c: 105.003Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.17 0.168 0.198
Expression system: Escherichia coli