› 3ohi

X-ray diffraction
2.3Å resolution

Structure of Giardia fructose-1,6-biphosphate aldolase in complex with 3-hydroxy-2-pyridone

Released:
DOI: 10.2210/pdb3ohi/pdb
PDB entry 3ohi coloured by chain, front view.
PDB entry 3ohi coloured by chain, side view.
PDB entry 3ohi coloured by chain, top view.
Source organism: Giardia intestinalis
Primary publication:
Rational design, synthesis and evaluation of first generation inhibitors of the Giardia lamblia fructose-1,6-biphosphate aldolase.
Li Z, Liu Z, Cho DW, Zou J, Gong M, Breece RM, Galkin A, Li L, Zhao H, Maestas GD, Tierney DL, Herzberg O, Dunaway-Mariano D, Mariano PS
J Inorg Biochem 105 509-17 (2011)
PMID: 21333622

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
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
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:
Ligand ZN 2 x ZN
Ligand HDX 2 x HDX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P212121
Unit cell:
a: 53.58Å b: 64.95Å c: 171.45Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.199 0.274
Expression system: Escherichia coli

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Citations

2 review citations

Drug Development Against the Major Diarrhea-Causing Parasites of the Small Intestine, Cryptosporidium and Giardia.
Miyamoto et al. (2015)
1 more