2isw

X-ray diffraction
1.75Å resolution

Structure of Giardia fructose-1,6-biphosphate aldolase in complex with phosphoglycolohydroxamate

Released:

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 dimer (preferred)
PDBe Complex ID:
PDB-CPX-108573 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-bisphosphate aldolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 323 amino acids
Theoretical weight: 35.29 KDa
Source organism: Giardia intestinalis
Expression system: Escherichia coli
UniProt:
  • Canonical: A8B2U2 (Residues: 1-323; Coverage: 100%)
Gene names: FBPA, GL50803_0011043, fba
Sequence domains: Fructose-bisphosphate aldolase class-II
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-BM
Spacegroup: C2221
Unit cell:
a: 90.02Å b: 90.05Å c: 166.09Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.186 0.225
Expression system: Escherichia coli