3tbf

X-ray diffraction
2.28Å resolution

C-terminal domain of glucosamine-fructose-6-phosphate aminotransferase from Francisella tularensis.

Released:
Entry authors: Osipiuk J, Zhou M, Maltseva N, Kim Y, Papazisi L, Anderson WF, Joachimiak A, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-177707 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamine--fructose-6-phosphate aminotransferase [isomerizing] Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 372 amino acids
Theoretical weight: 41.3 KDa
Source organism: Francisella tularensis subsp. tularensis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5NHQ9 (Residues: 241-612; Coverage: 61%)
Gene names: FTT_0388, glmS
Sequence domains: SIS domain
Structure domains: Glucose-6-phosphate isomerase like protein; domain 1

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 71.37Å b: 262.911Å c: 83.797Å
α: 90° β: 91.32° γ: 90°
R-values:
R R work R free
0.175 0.172 0.232
Expression system: Escherichia coli BL21(DE3)