› 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 entry 1lkc coloured by chain, front view.
PDB entry 1lkc coloured by chain, side view.
PDB entry 1lkc coloured by chain, top view.
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)
Assembly name:
PDBe Complex ID:
PDB-CPX-161271 (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
Sequence domains: Aminotransferase class I and II
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

2 review citations

Biosynthesis of the modified tetrapyrroles-the pigments of life.
Bryant et al. (2020)
1 more

2 mentions without citation

Automatic multiple-zone rigid-body refinement with a large convergence radius.
Afonine et al. (2009)
1 more