1wx0

X-ray diffraction
2.27Å resolution

Crystal structure of transaldolase from Thermus thermophilus HB8

Released:
Source organism: Thermus thermophilus HB8
Entry authors: Asada Y, Kunishima N, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

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-178015 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable transaldolase Chains: A, B, C, D, E, F, G, H, I, J
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J
Length: 223 amino acids
Theoretical weight: 24.05 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5SJE8 (Residues: 1-223; Coverage: 100%)
Gene names: TTHA1066, tal
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: SPRING-8 BEAMLINE BL26B1
Spacegroup: P21
Unit cell:
a: 93.693Å b: 142.702Å c: 96.595Å
α: 90° β: 114.458° γ: 90°
R-values:
R R work R free
0.198 0.196 0.239
Expression system: Escherichia coli BL21(DE3)