X-ray diffraction
2.19Å resolution

Crystal structure of Peptidyl-tRNA hydrolase from a Gram-positive bacterium, Streptococcus pyogenes at 2.19 Angstrom resolution shows the Closed Structure of the Substrate Binding Cleft


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, B
Molecule details ›
Chains: A, B
Length: 189 amino acids
Theoretical weight: 21.22 KDa
Source organism: Streptococcus pyogenes NZ131
Expression system: Escherichia coli
  • Canonical: B5XIP6 (Residues: 1-189; Coverage: 100%)
Gene names: Spy49_0005, 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: ESRF BEAMLINE BM14
Spacegroup: P1
Unit cell:
a: 36.024Å b: 43.028Å c: 65.1Å
α: 90.33° β: 105.78° γ: 112.51°
R R work R free
0.17 0.168 0.198
Expression system: Escherichia coli