› 1lkc

X-ray diffraction
1.8Å resolution

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

Released:
DOI: 10.2210/pdb1lkc/pdb
PDB 1lkc coloured by chain and viewed from the front.
PDB 1lkc coloured by chain and viewed from the side.
PDB 1lkc coloured by chain and viewed from the top.
Source organism: Salmonella enterica
Primary publication:
Three-dimensional structure of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica.
Cheong CG, Bauer CB, Brushaber KR, Escalante-Semerena JC, Rayment I
Biochemistry 41 4798-808 (2002)
PMID: 11939774

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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
UniProt:
  • 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:
Ligand PO4 1 x PO4
Ligand EDO 2 x EDO
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-values:
R R work R free
0.203 0.203 0.236
Expression system: Escherichia coli

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Citations

1 review citation

Biosynthesis of the modified tetrapyrroles-the pigments of life.
Bryant et al. (2020)
6 other articles

1 mention without citation

Bioinformatic analysis of the fold type I PLP-dependent enzymes reveals determinants of reaction specificity in l-threonine aldolase from Aeromonas jandaei.
Fesko et al. (2018)