X-ray diffraction
2Å resolution

Crystal structure of an active fragment of human tryptophanyl-tRNA synthetase with cytokine activity


Function and Biology Details

Reaction catalysed:
ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp)
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Tryptophan--tRNA ligase, cytoplasmic Chains: A, B
Molecule details ›
Chains: A, B
Length: 437 amino acids
Theoretical weight: 50.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P23381 (Residues: 48-471; Coverage: 90%)
Gene names: IFI53, WARS, WARS1, WRS
Sequence domains: tRNA synthetases class I (W and Y)
Structure domains:

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: C2
Unit cell:
a: 134.658Å b: 96.46Å c: 97.132Å
α: 90° β: 129.9° γ: 90°
R R work R free
0.255 0.254 0.298
Expression system: Escherichia coli