› 3upb

X-ray diffraction
1.5Å resolution

1.5 Angstrom Resolution Crystal Structure of Transaldolase from Francisella tularensis in Covalent Complex with Arabinose-5-Phosphate

Released:
DOI: 10.2210/pdb3upb/pdb
PDB entry 3upb coloured by chain, front view.
PDB entry 3upb coloured by chain, side view.
PDB entry 3upb coloured by chain, top view.
Source organism: Francisella tularensis subsp. tularensis
Primary publication:
Arabinose 5-phosphate covalently inhibits transaldolase.
Light SH, Anderson WF
J Struct Funct Genomics 15 41-4 (2014)
PMID: 24510200

Function and Biology Details

Reaction catalysed: 
Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-177676 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transaldolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 345 amino acids
Theoretical weight: 38.48 KDa
Source organism: Francisella tularensis subsp. tularensis
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q5NFX0 (Residues: 1-321; Coverage: 100%)
Gene names: FTT_1093c, talA
Sequence domains: Transaldolase/Fructose-6-phosphate aldolase
Structure domains: Aldolase class I

Ligands and Environments

4 bound ligands:
Ligand P6G 1 x P6G
Ligand A5P 2 x A5P
Ligand PGE 2 x PGE
Ligand PEG 2 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P212121
Unit cell:
a: 55.045Å b: 86.197Å c: 140.547Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.152 0.151 0.175
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

The Pentose Phosphate Pathway Dynamics in Cancer and Its Dependency on Intracellular pH.
Alfarouk et al. (2020)
1 more

1 mention without citation

Recent advances in design of new urease inhibitors: A review.
Kafarski et al. (2018)