› 2qdg

X-ray diffraction
2.2Å resolution

Fructose-1,6-bisphosphate Schiff base intermediate in FBP aldolase from Leishmania mexicana

Released:
DOI: 10.2210/pdb2qdg/pdb
PDB entry 2qdg coloured by chain, front view.
PDB entry 2qdg coloured by chain, side view.
PDB entry 2qdg coloured by chain, top view.
Source organism: Leishmania mexicana
Primary publication:
Carboxy-terminus recruitment induced by substrate binding in eukaryotic fructose bis-phosphate aldolases.
Lafrance-Vanasse J, Sygusch J
Biochemistry 46 9533-40 (2007)
PMID: 17661446

Function and Biology Details

Reaction catalysed: 
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193610 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-bisphosphate aldolase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 391 amino acids
Theoretical weight: 43.06 KDa
Source organism: Leishmania mexicana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9U5N6 (Residues: 1-371; Coverage: 100%)
Gene name: ald
Sequence domains: Fructose-bisphosphate aldolase class-I
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
Ligand PO4 8 x PO4
Ligand 2FP 4 x 2FP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P212121
Unit cell:
a: 85.109Å b: 117.09Å c: 161.798Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.185 0.238
Expression system: Escherichia coli

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Citations

3 mentions without citation

The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.
Ogungbe et al. (2016)
2 more