X-ray diffraction
2.5Å resolution

Crystal structure of the aminoacylation catalytic fragment of human tryptophanyl-tRNA synthetase


Function and Biology Details

Reaction catalysed:
ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp)
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
T2-TrpRS Chain: A
Molecule details ›
Chain: A
Length: 378 amino acids
Theoretical weight: 43.39 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P23381 (Residues: 94-471; Coverage: 80%)
Gene names: IFI53, WARS, WARS1, WRS
Sequence domains: tRNA synthetases class I (W and Y)
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P6522
Unit cell:
a: 82.24Å b: 82.24Å c: 263.56Å
α: 90° β: 90° γ: 120°
R R work R free
0.245 0.245 0.296
Expression system: Escherichia coli