PDBe 3ig8

X-ray diffraction
2.69Å resolution

Saccharomyces cerevisiae glutamate cysteine ligase in complex with Mg2+, L-glutamate and ADP

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate--cysteine ligase Chain: A
Molecule details ›
Chain: A
Length: 692 amino acids
Theoretical weight: 79.93 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P32477 (Residues: 1-678; Coverage: 100%)
Gene names: GSH1, J0832, YJL101C
Sequence domains: Glutamate-cysteine ligase
Structure domains:

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P43212
Unit cell:
a: 117.849Å b: 117.849Å c: 164.444Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.187 0.242
Expression system: Escherichia coli