2e1d

X-ray diffraction
2Å resolution

Crystal structure of mouse transaldolase

Released:
Source organism: Mus musculus
Entry authors: Kishishita S, Murayama K, Chen L, Liu ZJ, Wang BC, 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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187983 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transaldolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 331 amino acids
Theoretical weight: 36.45 KDa
Source organism: Mus musculus
Expression system: Not provided
UniProt:
  • Canonical: Q93092 (Residues: 11-334; Coverage: 96%)
Gene names: Tal, Taldo, Taldo1
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: APS BEAMLINE 22-ID
Spacegroup: P21
Unit cell:
a: 51.984Å b: 107.488Å c: 60.877Å
α: 90° β: 96.91° γ: 90°
R-values:
R R work R free
0.169 0.169 0.211
Expression system: Not provided