PDBe 3ln6

X-ray diffraction
2.95Å resolution

Crystal structure of a bifunctional glutathione synthetase from Streptococcus agalactiae

Released:
Entry authors: Stout J, Vergauwen B, Savvides SN

Function and Biology Details

Reactions catalysed:
ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione biosynthesis bifunctional protein GshAB Chain: A
Molecule details ›
Chain: A
Length: 750 amino acids
Theoretical weight: 85.69 KDa
Source organism: Streptococcus agalactiae serogroup V
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8DXM9 (Residues: 1-750; Coverage: 100%)
Gene names: SAG1821, gshAB, gshF
Sequence domains:
Structure domains: Creatine Kinase; Chain A, domain 2

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A, ESRF BEAMLINE ID14-2
Spacegroup: I4122
Unit cell:
a: 143.02Å b: 143.02Å c: 211.23Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.253 0.253 0.286
Expression system: Escherichia coli