PDBe 2hl2

X-ray diffraction
2.6Å resolution

Crystal structure of the editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi in complex with an analog of seryladenylate

Released:

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 143 amino acids
Theoretical weight: 16.28 KDa
Source organism: Pyrococcus abyssi
Expression system: Escherichia coli BL21
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

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 39.652Å b: 67.363Å c: 98.588Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.213 0.295
Expression system: Escherichia coli BL21