› 3kaj

X-ray diffraction
2Å resolution

Apoenzyme structure of homoglutathione synthetase from Glycine max in open conformation

Released:
DOI: 10.2210/pdb3kaj/pdb
PDB entry 3kaj coloured by chain, front view.
PDB entry 3kaj coloured by chain, side view.
PDB entry 3kaj coloured by chain, top view.
Source organism: Glycine max
Primary publication:
Structural basis for evolution of product diversity in soybean glutathione biosynthesis.
Galant A, Arkus KA, Zubieta C, Cahoon RE, Jez JM
Plant Cell 21 3450-8 (2009)
PMID: 19948790

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192365 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione synthetase Chains: A, B
Molecule details ›
Chains: A, B
Length: 499 amino acids
Theoretical weight: 55.73 KDa
Source organism: Glycine max
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9M426 (Residues: 1-499; Coverage: 100%)
Gene name: hGS
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P21
Unit cell:
a: 64.957Å b: 80.549Å c: 89.995Å
α: 90° β: 96.94° γ: 90°
R-values:
R R work R free
0.202 0.198 0.269
Expression system: Escherichia coli

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Citations

6 review citations

Sensing sulfur conditions: simple to complex protein regulatory mechanisms in plant thiol metabolism.
Yi et al. (2010)
5 more