› 1o5t

X-ray diffraction
2.5Å resolution

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

Released:
DOI: 10.2210/pdb1o5t/pdb
PDB entry 1o5t coloured by chain, front view.
PDB entry 1o5t coloured by chain, side view.
PDB entry 1o5t coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of human tryptophanyl-tRNA synthetase catalytic fragment: insights into substrate recognition, tRNA binding, and angiogenesis activity.
Yu Y, Liu Y, Shen N, Xu X, Xu F, Jia J, Jin Y, Arnold E, Ding J
J Biol Chem 279 8378-88 (2004)
PMID: 14660560

Function and Biology Details

Reaction catalysed: 
ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149944 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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
UniProt:
  • 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-values:
R R work R free
0.245 0.245 0.296
Expression system: Escherichia coli

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Citations

2 review citations

Designing novel spectral classes of proteins with a tryptophan-expanded genetic code.
Budisa et al. (2004)
1 more

8 mentions without citation

Unique roles of tryptophanyl-tRNA synthetase in immune control and its therapeutic implications.
Jin M. (2019)
7 more