› 3aex

X-ray diffraction
2.1Å resolution

Catalytic intermediate analogue of threonine synthase from Thermus thermophilus HB8

Released:
DOI: 10.2210/pdb3aex/pdb
PDB entry 3aex coloured by chain, front view.
PDB entry 3aex coloured by chain, side view.
PDB entry 3aex coloured by chain, top view.
Source organism: Thermus thermophilus HB8
Primary publication:
Product-assisted catalysis as the basis of the reaction specificity of threonine synthase.
Murakawa T, Machida Y, Hayashi H
J Biol Chem 286 2774-84 (2011)
PMID: 21084312

Function and Biology Details

Reaction catalysed: 
O-phospho-L-homoserine + H(2)O = L-threonine + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178123 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Threonine synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 351 amino acids
Theoretical weight: 37.05 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5SL02 (Residues: 1-351; Coverage: 100%)
Gene name: TTHA0491
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold

Ligands and Environments

2 bound ligands:
Ligand AN7 2 x AN7
Ligand PO4 2 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P3221
Unit cell:
a: 115.252Å b: 115.252Å c: 99.709Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.216 0.216 0.253
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Controlling reaction specificity in pyridoxal phosphate enzymes.
Toney MD. (2011)
2 other articles

3 mentions without citation

Product-assisted catalysis as the basis of the reaction specificity of threonine synthase.
Murakawa et al. (2011)
2 more