3r1m

X-ray diffraction
1.5Å resolution

Structure of bifunctional fructose 1,6-bisphosphate aldolase/phosphatase (aldolase form)

Released:

Function and Biology Details

Reactions catalysed:
D-fructose 1,6-bisphosphate + H(2)O = D-fructose 6-phosphate + phosphate
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo octamer (preferred)
PDBe Complex ID:
PDB-CPX-123809 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-1,6-bisphosphate aldolase/phosphatase Chain: A
Molecule details ›
Chain: A
Length: 385 amino acids
Theoretical weight: 42.76 KDa
Source organism: Sulfurisphaera tokodaii str. 7
Expression system: Escherichia coli
UniProt:
  • Canonical: F9VMT6 (Residues: 1-384; Coverage: 100%)
Gene names: STK_03180, fbp
Sequence domains: Fructose-1,6-bisphosphatase

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: I422
Unit cell:
a: 112.543Å b: 112.543Å c: 153.608Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.196 0.215
Expression system: Escherichia coli