3a04

X-ray diffraction
1.97Å resolution

Crystal structure of tryptophanyl-tRNA synthetase from hyperthermophilic archaeon, Aeropyrum pernix K1

Released:

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
Macromolecule:
Tryptophan--tRNA ligase Chain: A
Molecule details ›
Chain: A
Length: 372 amino acids
Theoretical weight: 42.22 KDa
Source organism: Aeropyrum pernix
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y924 (Residues: 1-372; Coverage: 100%)
Gene names: APE_2461.1, trpS
Sequence domains: tRNA synthetases class I (W and Y)
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: C2221
Unit cell:
a: 98.709Å b: 103.194Å c: 97.806Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.178 0.235
Expression system: Escherichia coli