4rrm

X-ray diffraction
1.55Å resolution

E129A mutant of N-terminal editing domain of threonyl-tRNA synthetase from Aeropyrum pernix with L-Thr3AA

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)
PDBe Complex ID:
PDB-CPX-195497 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Threonine--tRNA ligase editing subunit Chain: A
Molecule details ›
Chain: A
Length: 136 amino acids
Theoretical weight: 15.08 KDa
Source organism: Aeropyrum pernix K1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9YFY3 (Residues: 1-136; Coverage: 32%)
Gene names: APE_0117.1, thrS2
Sequence domains: Archaea-specific editing domain of threonyl-tRNA synthetase
Structure domains: D-tyrosyl-tRNA(Tyr) deacylase

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: P41212
Unit cell:
a: 47.091Å b: 47.091Å c: 112.729Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.188 0.259
Expression system: Escherichia coli