› 5tle

X-ray diffraction
1.58Å resolution

Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with the inhibitor 2-phosphate-naphthalene 6-bisphosphonate

Released:
DOI: 10.2210/pdb5tle/pdb
PDB entry 5tle coloured by chain, front view.
PDB entry 5tle coloured by chain, side view.
PDB entry 5tle coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
Bisphosphonate Inhibitors of Mammalian Glycolytic Aldolase.
Heron PW, Abellán-Flos M, Salmon L, Sygusch J
J Med Chem 61 10558-10572 (2018)
PMID: 30418024

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 analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133666 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-bisphosphate aldolase A Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 363 amino acids
Theoretical weight: 39.26 KDa
Source organism: Oryctolagus cuniculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00883 (Residues: 2-364; Coverage: 100%)
Gene name: ALDOA
Sequence domains: Fructose-bisphosphate aldolase class-I
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
Ligand RD1 4 x RD1
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08B1-1
Spacegroup: P21
Unit cell:
a: 83.742Å b: 103.717Å c: 84.524Å
α: 90° β: 98.81° γ: 90°
R-values:
R R work R free
0.131 0.131 0.158
Expression system: Escherichia coli

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Citations

2 review citations

Multifunctional Fructose 1,6-Bisphosphate Aldolase as a Therapeutic Target.
Pirovich et al. (2021)
1 more