2cwn

X-ray diffraction
2.1Å resolution

Crystal structure of mouse transaldolase

Released:
Source organism: Mus musculus
Entry authors: Handa N, Arai R, Nishino A, Uchikubo T, Takemoto C, Morita S, Kinoshita Y, Nagano Y, Uda H, Terada T, Shirouzu M, Yokoyama S, 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:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187982 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transaldolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 332 amino acids
Theoretical weight: 36.49 KDa
Source organism: Mus musculus
Expression system: Not provided
UniProt:
  • Canonical: Q93092 (Residues: 13-337; Coverage: 96%)
Gene names: Tal, Taldo, Taldo1
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: P21212
Unit cell:
a: 79.05Å b: 108.009Å c: 75.608Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.196 0.239
Expression system: Not provided