X-ray diffraction
1.5Å resolution

Crystal structure of the editing domain of threonyl-tRNA synthetase complexed with an analog of seryladenylate


Function and Biology Details

Reaction catalysed:
ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Threonine--tRNA ligase Chain: A
Molecule details ›
Chain: A
Length: 224 amino acids
Theoretical weight: 25.47 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21
  • Canonical: P0A8M3 (Residues: 1-224; Coverage: 35%)
Gene names: JW1709, b1719, thrS
Sequence domains: TGS domain
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21
Unit cell:
a: 43.86Å b: 41.22Å c: 68.24Å
α: 90° β: 103.1° γ: 90°
R R work R free
0.202 0.201 0.219
Expression system: Escherichia coli BL21