› 3ln7

X-ray diffraction
3.2Å resolution

Crystal structure of a bifunctional glutathione synthetase from Pasteurella multocida

Released:
DOI: 10.2210/pdb3ln7/pdb
Model geometry
Fit model/data
PDB entry 3ln7 coloured by chain, front view.
PDB entry 3ln7 coloured by chain, side view.
PDB entry 3ln7 coloured by chain, top view.
Source organism: Pasteurella multocida
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:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189983 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione biosynthesis bifunctional protein GshAB Chains: A, B
Molecule details ›
Chains: A, B
Length: 757 amino acids
Theoretical weight: 86.89 KDa
Source organism: Pasteurella multocida
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9CM00 (Residues: 1-757; Coverage: 100%)
Gene names: PM1048, gshAB, gshF
Sequence domains:
Structure domains: Creatine Kinase; Chain A, domain 2

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 40 x MSE

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: C2
Unit cell:
a: 205.24Å b: 87.07Å c: 145.98Å
α: 90° β: 126.53° γ: 90°
R-values:
R R work R free
0.275 0.275 0.314
Expression system: Escherichia coli

Quick links