5tev

X-ray diffraction
2.25Å resolution

Crystal structure of a tryptophanyl-tRNA synthetase from Neisseria gonorrhoeae, apo

Released:
Entry authors: Seattle Structural Genomics Center for Infectious Disease, Seattle Structural Genomics Center for Infectious Disease (SSGCID)

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:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-177069 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tryptophan--tRNA ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 344 amino acids
Theoretical weight: 38.66 KDa
Source organism: Neisseria gonorrhoeae FA 1090
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5F7X0 (Residues: 1-336; Coverage: 100%)
Gene names: NGO_1045, trpS
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: APS BEAMLINE 21-ID-F
Spacegroup: P3221
Unit cell:
a: 59.94Å b: 59.94Å c: 355.62Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.178 0.175 0.237
Expression system: Escherichia coli