› 1lw5

X-ray diffraction
2.05Å resolution

X-ray structure of L-Threonine Aldolase (low-specificity) in complex with glycine

Released:
DOI: 10.2210/pdb1lw5/pdb
PDB entry 1lw5 coloured by chain, front view.
PDB entry 1lw5 coloured by chain, side view.
PDB entry 1lw5 coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
X-ray structures of threonine aldolase complexes: structural basis of substrate recognition.
Kielkopf CL, Burley SK
Biochemistry 41 11711-20 (2002)
PMID: 12269813

Function and Biology Details

Reaction catalysed: 
L-threonine = glycine + acetaldehyde
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194873 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aromatic amino acid beta-eliminating lyase/threonine aldolase domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 347 amino acids
Theoretical weight: 38.94 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9X266 (Residues: 1-343; Coverage: 100%)
Gene name: TM_1744
Sequence domains: Beta-eliminating lyase
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 1 x PLP
3 bound ligands:
Ligand CA 6 x CA
Ligand CL 6 x CL
Ligand PLG 3 x PLG
2 modified residues:
Ligand MSE 56 x MSE
Ligand LLP 4 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9A
Spacegroup: P212121
Unit cell:
a: 96.02Å b: 100.71Å c: 150.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.207 0.237
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Threonine aldolases-screening, properties and applications in the synthesis of non-proteinogenic beta-hydroxy-alpha-amino acids.
Dückers et al. (2010)
4 more

3 mentions without citation

Threonine aldolases: perspectives in engineering and screening the enzymes with enhanced substrate and stereo specificities.
Fesko K. (2016)
2 more