X-ray diffraction
1.65Å resolution

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 Chain: A
Molecule details ›
Chain: A
Length: 222 amino acids
Theoretical weight: 24.42 KDa
Source organism: Burkholderia thailandensis E264
Expression system: Escherichia coli
  • Canonical: Q2T1B9 (Residues: 1-201; Coverage: 100%)
Gene names: BTH_I0472, pth
Sequence domains: Peptidyl-tRNA hydrolase
Structure domains: Peptidyl-tRNA hydrolase

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: I222
Unit cell:
a: 53.34Å b: 93.58Å c: 106.76Å
α: 90° β: 90° γ: 90°
R R work R free
0.177 0.175 0.206
Expression system: Escherichia coli