› 3v2i

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:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174001 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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
UniProt:
  • 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:
Ligand CIT 1 x CIT
Ligand UNL 1 x UNL
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-values:
R R work R free
0.177 0.175 0.206
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product.
Dailey et al. (2017)
10 more

3 mentions without citation

Combining functional and structural genomics to sample the essential Burkholderia structome.
Baugh et al. (2013)
2 more