2iqt

X-ray diffraction
2.46Å resolution

Crystal Structure of Fructose-Bisphosphate Aldolase, Class I from Porphyromonas gingivalis

Released:
Source organism: Porphyromonas gingivalis W83
Entry authors: Kim Y, Zhou M, Moy S, Joachimiak A, Midwest Center for Structural Genomics (MCSG)

Function and Biology Details

Reaction catalysed:
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-bisphosphate aldolase class 1 Chain: A
Molecule details ›
Chain: A
Length: 296 amino acids
Theoretical weight: 33.96 KDa
Source organism: Porphyromonas gingivalis W83
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P60053 (Residues: 1-293; Coverage: 100%)
Gene names: PG_1755, fbaB, fda
Sequence domains: Fructose-bisphosphate aldolase class-I
Structure domains: Aldolase class I

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P3121
Unit cell:
a: 68.737Å b: 68.737Å c: 154.113Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.187 0.182 0.232
Expression system: Escherichia coli BL21(DE3)