2pth

X-ray diffraction
1.2Å resolution

PEPTIDYL-TRNA HYDROLASE FROM ESCHERICHIA COLI

Released:

Function and Biology Details

Reaction catalysed:
N-substituted aminoacyl-tRNA + H(2)O = N-substituted amino acid + tRNA

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-141581 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-tRNA hydrolase Chain: A
Molecule details ›
Chain: A
Length: 193 amino acids
Theoretical weight: 20.98 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: P0A7D1 (Residues: 2-194; Coverage: 100%)
Gene names: JW1195, b1204, pth
Sequence domains: Peptidyl-tRNA hydrolase
Structure domains: Peptidyl-tRNA hydrolase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LURE BEAMLINE DW32
Spacegroup: P212121
Unit cell:
a: 47.24Å b: 63.59Å c: 62.57Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.196 0.215
Expression system: Escherichia coli K-12