› 1onr

X-ray diffraction
1.87Å resolution

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141669 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transaldolase B Chains: A, B
Molecule details ›
Chains: A, B
Length: 316 amino acids
Theoretical weight: 35.13 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A870 (Residues: 2-317; Coverage: 100%)
Gene names: JW0007, b0008, talB, yaaK
Sequence domains: Transaldolase/Fructose-6-phosphate aldolase
Structure domains: Aldolase class I

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 68.9Å b: 91.3Å c: 130.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.201 0.234
Expression system: Escherichia coli

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Citations

11 review citations

One fold with many functions: the evolutionary relationships between TIM barrel families based on their sequences, structures and functions.
Nagano et al. (2002)
10 more

6 mentions without citation

Replacement of a phenylalanine by a tyrosine in the active site confers fructose-6-phosphate aldolase activity to the transaldolase of Escherichia coli and human origin.
Schneider et al. (2008)
5 more