X-ray diffraction
2.6Å resolution

Crystal structure of human glutamine synthetase in complex with ADP and methionine sulfoximine 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, F, G, H, I, J
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J
Length: 384 amino acids
Theoretical weight: 43.36 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P15104 (Residues: 5-365; Coverage: 97%)
Gene names: GLNS, GLUL
Sequence domains:
Structure domains:

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: C2
Unit cell:
a: 181.21Å b: 126.08Å c: 188.17Å
α: 90° β: 92.14° γ: 90°
R R work R free
0.168 0.166 0.217
Expression system: Escherichia coli