PDBe 1tt4

X-ray diffraction
2.8Å resolution

Structure of NP459575, a predicted glutathione synthase from Salmonella typhimurium

Released:
Entry authors: Miller DJ, Shuvalova L, Anderson WF, Midwest Center for Structural Genomics (MCSG)

Function and Biology Details

Reaction catalysed:
ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative glutamate--cysteine ligase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 396 amino acids
Theoretical weight: 44.39 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8ZR41 (Residues: 1-372; Coverage: 100%)
Gene names: STM0583, ybdK
Sequence domains: Glutamate-cysteine ligase family 2(GCS2)
Structure domains: Creatine Kinase; Chain A, domain 2

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: I23
Unit cell:
a: 188.929Å b: 188.929Å c: 188.929Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.209 0.258
Expression system: Escherichia coli BL21(DE3)