5v0i

X-ray diffraction
1.9Å resolution

Crystal Structure of Tryptophanyl-tRNA Synthetase from Escherichia coli Complexed with AMP and Tryptophan

Released:
Entry authors: Maltseva N, Kim Y, Mulligan R, Grimshaw SG, Joachimiak A, Anderson WF, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-159213 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tryptophan--tRNA ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 337 amino acids
Theoretical weight: 37.74 KDa
Source organism: Escherichia coli O157:H7 str. EDL933
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P67589 (Residues: 1-334; Coverage: 100%)
Gene names: ECs4226, Z4737, trpS
Sequence domains: tRNA synthetases class I (W and Y)
Structure domains: HUPs

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 46.745Å b: 110.807Å c: 128.599Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.186 0.217
Expression system: Escherichia coli BL21(DE3)