1xff

X-ray diffraction
1.8Å resolution

Function and Biology Details

Reaction catalysed:
L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-147884 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamine--fructose-6-phosphate aminotransferase [isomerizing] Chains: A, B
Molecule details ›
Chains: A, B
Length: 240 amino acids
Theoretical weight: 26.51 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P17169 (Residues: 2-241; Coverage: 39%)
Gene names: JW3707, b3729, glmS
Sequence domains: Glutamine amidotransferase domain
Structure domains: Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P212121
Unit cell:
a: 70.38Å b: 82.52Å c: 86.05Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.161 0.161 not available
Expression system: Escherichia coli