X-ray diffraction
1.6Å resolution

Crystal structure of S. typhimurium peptidyl-tRNA hydrolase


Function and Biology Details

Reaction catalysed:
N-substituted aminoacyl-tRNA + H(2)O = N-substituted amino acid + tRNA
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Peptidyl-tRNA hydrolase Chains: A, C
Molecule details ›
Chains: A, C
Length: 200 amino acids
Theoretical weight: 22.04 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Expression system: Escherichia coli
  • Canonical: A0A0F6B281 (Residues: 2-194; Coverage: 100%)
Gene names: STM14_2156, pth
Sequence domains: Peptidyl-tRNA hydrolase
Structure domains: Peptidyl-tRNA hydrolase

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 62.097Å b: 64.925Å c: 110.489Å
α: 90° β: 90° γ: 90°
R R work R free
0.175 0.174 0.198
Expression system: Escherichia coli