› 1r8g

X-ray diffraction
2.15Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160133 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative glutamate--cysteine ligase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 372 amino acids
Theoretical weight: 42.25 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P77213 (Residues: 1-372; Coverage: 100%)
Gene names: JW0570, b0581, ybdK
Sequence domains: Glutamate-cysteine ligase family 2(GCS2)
Structure domains: Creatine Kinase; Chain A, domain 2

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 22 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P21
Unit cell:
a: 49.47Å b: 100.32Å c: 71.37Å
α: 90° β: 99.94° γ: 90°
R-values:
R R work R free
0.189 0.189 0.252
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Structure, function, and post-translational regulation of the catalytic and modifier subunits of glutamate cysteine ligase.
Franklin et al. (2009)
2 more

4 mentions without citation

Molecular analysis of the prokaryotic ubiquitin-like protein (Pup) conjugation pathway in Mycobacterium tuberculosis.
Cerda-Maira et al. (2010)
3 more