X-ray diffraction
1.8Å resolution

Crystal Structure of L-Threonine-O-3-Phosphate Decarboxylase from Salmonella enterica


Function and Biology Details

Reaction catalysed:
L-threonine O-3-phosphate = (R)-1-aminopropan-2-yl phosphate + CO(2)
Biochemical function:
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
Structure domains:

Ligands and Environments

Cofactor: Ligand PLP 1 x PLP
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: I222
Unit cell:
a: 67.96Å b: 101.55Å c: 117.23Å
α: 90° β: 90° γ: 90°
R R work R free
0.203 0.203 0.236
Expression system: Escherichia coli