› 2uu7

X-ray diffraction
3Å resolution

Crystal structure of apo glutamine synthetase from dog (Canis familiaris)

Released:
DOI: 10.2210/pdb2uu7/pdb
PDB entry 2uu7 coloured by chain, front view.
PDB entry 2uu7 coloured by chain, side view.
PDB entry 2uu7 coloured by chain, top view.
Source organism: Canis lupus familiaris
Primary publication:
Crystal structures of mammalian glutamine synthetases illustrate substrate-induced conformational changes and provide opportunities for drug and herbicide design.
Krajewski WW, Collins R, Holmberg-Schiavone L, Jones TA, Karlberg T, Mowbray SL
J Mol Biol 375 217-28 (2008)
PMID: 18005987

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:
Sequence domains:

Structure analysis Details

Assembly composition:
homo decamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184619 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamine synthetase Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O
Length: 381 amino acids
Theoretical weight: 43.15 KDa
Source organism: Canis lupus familiaris
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8HZM5 (Residues: 1-373; Coverage: 100%)
Gene name: GLUL
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MG 15 x MG
Ligand CL 15 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: C2221
Unit cell:
a: 183.59Å b: 485.602Å c: 192.156Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.213 0.23
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

12 review citations

The Pleiotropic Effects of Glutamine Metabolism in Cancer.
Bott et al. (2019)
11 more

7 mentions without citation

Molecular Mechanisms of Glutamine Synthetase Mutations that Lead to Clinically Relevant Pathologies.
Frieg et al. (2016)
6 more