PDBe 1y2q

X-ray diffraction
1.95Å resolution

Crystal structure of the editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi

Released:
Source organism: Pyrococcus abyssi
Primary publication:
A D-amino acid editing module coupled to the translational apparatus in archaea.
Nat. Struct. Mol. Biol. 12 556-7 (2005)
PMID: 15908961

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
Macromolecule:
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(DE3)
UniProt:
  • 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

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P3221
Unit cell:
a: 61.752Å b: 61.752Å c: 64.894Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.209 0.205 0.272
Expression system: Escherichia coli BL21(DE3)