4rz5

X-ray diffraction
1.8Å resolution

Transaldolase B E96Q from E.coli

Released:
Source organism: Escherichia coli K-12
Entry authors: Stellmacher L, Sandalova T, Leptihn S, Schneider G, Sprenger GA, Samland AK

Function and Biology Details

Reaction catalysed:
Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transaldolase B Chains: A, B
Molecule details ›
Chains: A, B
Length: 337 amino acids
Theoretical weight: 37.46 KDa
Source organism: Escherichia coli K-12
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

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 66.76Å b: 90.24Å c: 131.89Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.208 0.262
Expression system: Escherichia coli