› 5gk5

X-ray diffraction
1.9Å resolution

Apo structure of fructose 1,6-bisphosphate aldolase from Escherichia coli at 1.9 angstrom resolution

Released:
DOI: 10.2210/pdb5gk5/pdb
PDB entry 5gk5 coloured by chain, front view.
PDB entry 5gk5 coloured by chain, side view.
PDB entry 5gk5 coloured by chain, top view.
Source organism: Escherichia coli K-12
Entry authors: Tran TH, Huynh KH, Ho TH, Kang LW

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 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, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 359 amino acids
Theoretical weight: 39.19 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0AB71 (Residues: 1-359; Coverage: 100%)
Gene names: JW2892, b2925, fba, fbaA, fda
Sequence domains: Fructose-bisphosphate aldolase class-II
Structure domains: Aldolase class I

Ligands and Environments

3 bound ligands:
Ligand GOL 7 x GOL
Ligand ZN 14 x ZN
Ligand PEG 6 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 5C (4A)
Spacegroup: P1
Unit cell:
a: 72.834Å b: 90.535Å c: 113.733Å
α: 90.07° β: 90.01° γ: 90.21°
R-values:
R R work R free
0.174 0.172 0.207
Expression system: Escherichia coli BL21(DE3)

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