› 1ucw

X-ray diffraction
2.2Å resolution

COMPLEX OF TRANSALDOLASE WITH THE REDUCED SCHIFF-BASE INTERMEDIATE

Released:
DOI: 10.2210/pdb1ucw/pdb
PDB entry 1ucw coloured by chain, front view.
PDB entry 1ucw coloured by chain, side view.
PDB entry 1ucw coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of the reduced Schiff-base intermediate complex of transaldolase B from Escherichia coli: mechanistic implications for class I aldolases.
Jia J, Schörken U, Lindqvist Y, Sprenger GA, Schneider G
Protein Sci 6 119-24 (1997)
PMID: 9007983

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: 317 amino acids
Theoretical weight: 35.36 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A870 (Residues: 1-317; 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
1 modified residue:
Ligand LLY 2 x LLY

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 69.2Å b: 91.9Å c: 130.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.204 0.244
Expression system: Escherichia coli

Quick links

Citations

9 review citations

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

1 mention without citation

Identifying the subproteome of kinetically stable proteins via diagonal 2D SDS/PAGE.
Xia et al. (2007)