› 1wn2

X-ray diffraction
1.2Å resolution

Crystal structure of project ID PH1539 from Pyrococcus horikoshii OT3

Released:
DOI: 10.2210/pdb1wn2/pdb
PDB entry 1wn2 coloured by chain, front view.
PDB entry 1wn2 coloured by chain, side view.
PDB entry 1wn2 coloured by chain, top view.
Source organism: Pyrococcus horikoshii OT3
Primary publication:
Structure of peptidyl-tRNA hydrolase 2 from Pyrococcus horikoshii OT3: insight into the functional role of its dimeric state.
Shimizu K, Kuroishi C, Sugahara M, Kunishima N
Acta Crystallogr D Biol Crystallogr 64 444-53 (2008)
PMID: 18391411

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130749 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-tRNA hydrolase Chain: A
Molecule details ›
Chain: A
Length: 121 amino acids
Theoretical weight: 13.4 KDa
Source organism: Pyrococcus horikoshii OT3
Expression system: Escherichia coli
UniProt:
  • Canonical: O74017 (Residues: 1-121; Coverage: 100%)
Gene names: PH1539, pth
Sequence domains: Peptidyl-tRNA hydrolase PTH2
Structure domains: Bit1

Ligands and Environments

1 bound ligand:
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: P41212
Unit cell:
a: 49.67Å b: 49.67Å c: 85.791Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.193 0.215
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Structural and functional insights into peptidyl-tRNA hydrolase.
Sharma et al. (2014)
4 other articles

1 mention without citation

Analysis of the impact of solvent on contacts prediction in proteins.
Samsonov et al. (2009)