PDBe 4rrr

X-ray diffraction
1.86Å resolution

K121M mutant of N-terminal editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi 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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Threonine--tRNA ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 147 amino acids
Theoretical weight: 16.74 KDa
Source organism: Pyrococcus abyssi GE5
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UZ14 (Residues: 1-147; Coverage: 24%)
Gene names: PAB1490, PYRAB13430, thrS
Sequence domains: Archaea-specific editing domain of threonyl-tRNA synthetase
Structure domains: D-tyrosyl-trna(Tyr) Deacylase; Chain: A;

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P212121
Unit cell:
a: 38.586Å b: 66.312Å c: 93.688Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.2 0.23
Expression system: Escherichia coli