3r8r

X-ray diffraction
1.9Å resolution

Transaldolase from Bacillus subtilis

Released:
Model geometry
Fit model/data

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:

Structure analysis Details

Assembly composition:
homo decamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148687 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transaldolase Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, P, R, T, U, V, W
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, P, R, T, U, V, W
Length: 212 amino acids
Theoretical weight: 23 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P19669 (Residues: 1-212; Coverage: 100%)
Gene names: BSU37110, orfU, tal, ywjH
Sequence domains: Transaldolase/Fructose-6-phosphate aldolase
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P21
Unit cell:
a: 143.299Å b: 127.28Å c: 158.448Å
α: 90° β: 98.1° γ: 90°
R-values:
R R work R free
0.202 0.2 0.229
Expression system: Escherichia coli