4s1w

X-ray diffraction
1.65Å resolution

Structure of a putative Glutamine--Fructose-6-Phosphate Aminotransferase from Staphylococcus aureus subsp. aureus Mu50

Released:
Model geometry
Fit model/data
Source organism: Staphylococcus aureus
Entry authors: Filippova EV, Shuvalova L, Kiryukhina O, Jedrzejczak R, Babnigg G, Rubin E, Sacchettini J, Joachimiak A, Anderson WF, Midwest Center for Structural Genomics (MCSG), Structures of Mtb Proteins Conferring Susceptibility to Known Mtb Inhibitors (MTBI)

Function and Biology Details

Reaction catalysed:
L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-102252 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamine--fructose-6-phosphate aminotransferase [isomerizing] Chains: A, B
Molecule details ›
Chains: A, B
Length: 358 amino acids
Theoretical weight: 39.43 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0J9X200 (Residues: 1-358; Coverage: 100%)
Sequence domains: SIS domain
Structure domains: Glucose-6-phosphate isomerase like protein; domain 1

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: C2
Unit cell:
a: 115.245Å b: 61.617Å c: 104.69Å
α: 90° β: 112.79° γ: 90°
R-values:
R R work R free
0.161 0.16 0.192
Expression system: Escherichia coli BL21(DE3)