› 1lc5

X-ray diffraction
1.46Å resolution

Crystal Structure of L-Threonine-O-3-phosphate Decarboxylase from S. enterica in its apo state

Released:
DOI: 10.2210/pdb1lc5/pdb
PDB entry 1lc5 coloured by chain, front view.
PDB entry 1lc5 coloured by chain, side view.
PDB entry 1lc5 coloured by chain, top view.
Source organism: Salmonella enterica
Primary publication:
Structural studies of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica: the apo, substrate, and product-aldimine complexes.
Cheong CG, Escalante-Semerena JC, Rayment I
Biochemistry 41 9079-89 (2002)
PMID: 12119022

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

1 bound ligand:
Ligand PO4 2 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: I222
Unit cell:
a: 75.99Å b: 103.34Å c: 109.25Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.19 0.214
Expression system: Escherichia coli

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Citations

8 citation in other articles

Biosynthesis of Histidine.
Winkler et al. (2009)
7 more

2 mentions without citation

Using neural networks and evolutionary information in decoy discrimination for protein tertiary structure prediction.
Tan et al. (2008)
1 more