PDBe 2hl0

X-ray diffraction
1.86Å resolution

Crystal structure of the editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi in complex with seryl-3'-aminoadenosine


Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Threonine--tRNA ligase Chain: A
Molecule details ›
Chain: A
Length: 143 amino acids
Theoretical weight: 16.28 KDa
Source organism: Pyrococcus abyssi
Expression system: Escherichia coli BL21
  • Canonical: Q9UZ14 (Residues: 1-143; Coverage: 23%)
Gene names: PAB1490, PYRAB13430, thrS
Sequence domains: Archaea-specific editing domain of threonyl-tRNA synthetase

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: I222
Unit cell:
a: 53.022Å b: 77.223Å c: 90.952Å
α: 90° β: 90° γ: 90°
R R work R free
0.193 0.193 0.22
Expression system: Escherichia coli BL21