› 4jx9

X-ray diffraction
1.4Å resolution

Crystal structure of the complex of peptidyl t-RNA hydrolase from Acinetobacter baumannii with uridine at 1.4A resolution

Released:
DOI: 10.2210/pdb4jx9/pdb
PDB entry 4jx9 coloured by chain, front view.
PDB entry 4jx9 coloured by chain, side view.
PDB entry 4jx9 coloured by chain, top view.
Source organism: Acinetobacter baumannii ATCC 19606 = CIP 70.34 = JCM 6841
Primary publication:
The mode of inhibitor binding to peptidyl-tRNA hydrolase: binding studies and structure determination of unbound and bound peptidyl-tRNA hydrolase from Acinetobacter baumannii.
Kaushik S, Singh N, Yamini S, Singh A, Sinha M, Arora A, Kaur P, Sharma S, Singh TP
OpenAccess logo PLoS One 8 e67547 (2013)
PMID: 23844024

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-111925 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-tRNA hydrolase Chain: A
Molecule details ›
Chain: A
Length: 193 amino acids
Theoretical weight: 20.97 KDa
Source organism: Acinetobacter baumannii ATCC 19606 = CIP 70.34 = JCM 6841
Expression system: Escherichia coli
UniProt:
  • Canonical: D0C9L6 (Residues: 1-193; Coverage: 100%)
Gene names: HMPREF0010_01329, pth
Sequence domains: Peptidyl-tRNA hydrolase
Structure domains: Peptidyl-tRNA hydrolase

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P212121
Unit cell:
a: 33.945Å b: 65.783Å c: 75.752Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.193 0.209
Expression system: Escherichia coli

Quick links

Citations

1 review citation

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

2 mentions without citation

The mode of inhibitor binding to peptidyl-tRNA hydrolase: binding studies and structure determination of unbound and bound peptidyl-tRNA hydrolase from Acinetobacter baumannii.
Kaushik et al. (2013)
1 more