PDBe 2d33

X-ray diffraction
2.6Å resolution

Crystal Structure of gamma-Glutamylcysteine Synthetase Complexed with Aluminum Fluoride

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

Assembly composition:
homo tetramer (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: 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: R3
Unit cell:
a: 325.226Å b: 325.226Å c: 105.181Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.164 0.162 0.191
Expression system: Escherichia coli