Function and Biology Details
Reaction catalysed:
ATP + L-glutamate + NH(3) = ADP + phosphate + L-glutamine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Glutamine synthetase, catalytic domain
- Glutamine synthetase, N-terminal domain
- Glutamine synthetase, N-terminal domain superfamily
- Glutamine synthetase, glycine-rich site
- Glutamine synthetase/guanido kinase, catalytic domain
- Glutamine synthetase, N-terminal conserved site
- Rossmann-like alpha/beta/alpha sandwich fold
Structure analysis Details
Assembly composition:
homo decamer (preferred)
Assembly name:
Glutamine synthetase (preferred)
PDBe Complex ID:
PDB-CPX-517475 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamine synthetase
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J
Length: 378 amino acids
Theoretical weight: 41.55 KDa
Source organism: Medicago truncatula
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 378 amino acids
Theoretical weight: 41.55 KDa
Source organism: Medicago truncatula
Expression system: Escherichia coli
UniProt:
- Canonical:
O04998 (Residues: 1-356; Coverage: 100%)
Sequence domains:
Structure domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
ESRF BEAMLINE ID14-2
Spacegroup:
P21
Expression system: Escherichia coli
