› 1dos

X-ray diffraction
1.67Å resolution

STRUCTURE OF FRUCTOSE-BISPHOSPHATE ALDOLASE

Released:
DOI: 10.2210/pdb1dos/pdb
PDB entry 1dos coloured by chain, front view.
PDB entry 1dos coloured by chain, side view.
PDB entry 1dos coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Novel active site in Escherichia coli fructose 1,6-bisphosphate aldolase.
Blom NS, Tétreault S, Coulombe R, Sygusch J
Nat Struct Biol 3 856-62 (1996)
PMID: 8836102

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 dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142018 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-bisphosphate aldolase class 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 358 amino acids
Theoretical weight: 39.03 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AB71 (Residues: 2-359; Coverage: 100%)
Gene names: JW2892, b2925, fba, fbaA, fda
Sequence domains: Fructose-bisphosphate aldolase class-II
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
Ligand ZN 2 x ZN
Ligand NH4 2 x NH4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 90.53Å b: 73.38Å c: 57.8Å
α: 90° β: 106.6° γ: 90°
R-values:
R R work R free
0.171 0.171 0.204
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Zinc enzymes.
Coleman JE. (1998)
6 more

11 mentions without citation

Peptide-plane flipping in proteins.
Hayward S. (2001)
10 more