2fjk

X-ray diffraction
2.2Å resolution

Crystal structure of Fructose-1,6-Bisphosphate Aldolase in Thermus caldophilus

Released:
Source organism: Thermus caldophilus
Primary publication:
Stereoselectivity of fructose-1,6-bisphosphate aldolase in Thermus caldophilus.
Biochem Biophys Res Commun 347 616-25 (2006)
PMID: 16843441

Function and Biology Details

Reaction catalysed:
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-180632 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-bisphosphate aldolase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 305 amino acids
Theoretical weight: 33.41 KDa
Source organism: Thermus caldophilus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q703I2 (Residues: 1-305; Coverage: 100%)
Gene name: fba
Sequence domains: Fructose-bisphosphate aldolase class-II
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-18B
Spacegroup: P212121
Unit cell:
a: 98.9Å b: 113.1Å c: 115.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.248 0.237 0.286
Expression system: Escherichia coli BL21(DE3)