› 1i2q

X-ray diffraction
2.05Å resolution

CRYSTAL STRUCTURE OF ESCHERICHIA COLI TRANSALDOLASE B MUTANT T156A

Released:
DOI: 10.2210/pdb1i2q/pdb
PDB entry 1i2q coloured by chain, front view.
PDB entry 1i2q coloured by chain, side view.
PDB entry 1i2q coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Identification of catalytically important residues in the active site of Escherichia coli transaldolase.
Schörken U, Thorell S, Schürmann M, Jia J, Sprenger GA, Schneider G
Eur J Biochem 268 2408-15 (2001)
PMID: 11298760

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141670 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transaldolase B Chains: A, B
Molecule details ›
Chains: A, B
Length: 316 amino acids
Theoretical weight: 35.1 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
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 69.143Å b: 91.76Å c: 131.031Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.186 0.207
Expression system: Escherichia coli

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Citations

2 review citations

Transaldolase: from biochemistry to human disease.
Samland et al. (2009)
1 more