X-ray diffraction
1.8Å resolution

Crystal Structure of L-Threonine-O-3-phosphate Decarboxylase from S. enterica complexed with its reaction intermediate


Function and Biology Details

Reaction catalysed:
L-threonine O-3-phosphate = (R)-1-aminopropan-2-yl phosphate + CO(2)
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Threonine-phosphate decarboxylase Chain: A
Molecule details ›
Chain: A
Length: 364 amino acids
Theoretical weight: 40.85 KDa
Source organism: Salmonella enterica
Expression system: Escherichia coli
  • Canonical: P97084 (Residues: 1-364; Coverage: 100%)
Gene names: STM0644, cobD
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: I222
Unit cell:
a: 66.646Å b: 103.293Å c: 117.117Å
α: 90° β: 90° γ: 90°
R R work R free
0.196 0.196 0.229
Expression system: Escherichia coli