X-ray diffraction
2.05Å resolution

Crystal structure of human glutamine synthetase in complex with ADP and phosphate


Function and Biology Details

Reactions catalysed:
Palmitoyl-CoA + [protein]-L-cysteine = [protein]-S-palmitoyl-L-cysteine + CoA
ATP + L-glutamate + NH(3) = ADP + phosphate + L-glutamine
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo decamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Glutamine synthetase Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 384 amino acids
Theoretical weight: 43.36 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P15104 (Residues: 5-365; Coverage: 97%)
Gene names: GLNS, GLUL
Structure domains:

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: C2
Unit cell:
a: 177.6Å b: 122.6Å c: 126.6Å
α: 90° β: 130.6° γ: 90°
R R work R free
0.162 0.159 0.212
Expression system: Escherichia coli BL21(DE3)