3mmt

X-ray diffraction
2.35Å resolution

Crystal structure of fructose bisphosphate aldolase from Bartonella henselae, bound to fructose bisphosphate

Released:
Source organism: Bartonella henselae
Primary publication:
Structure of fructose bisphosphate aldolase from Bartonella henselae bound to fructose 1,6-bisphosphate.
OpenAccess logo Acta Crystallogr Sect F Struct Biol Cryst Commun 67 1051-4 (2011)
PMID: 21904049

Function and Biology Details

Reaction catalysed:
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 tetramer (preferred)
PDBe Complex ID:
PDB-CPX-185242 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-bisphosphate aldolase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 347 amino acids
Theoretical weight: 37.56 KDa
Source organism: Bartonella henselae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8L207 (Residues: 1-343; Coverage: 100%)
Gene name: fbab
Sequence domains: Fructose-bisphosphate aldolase class-I
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P212121
Unit cell:
a: 72.39Å b: 127.71Å c: 157.63Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.177 0.222
Expression system: Escherichia coli BL21(DE3)