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X-ray diffraction
1.49Å resolution

Crystal structure of Arg119Gln mutant of Peptidyl-tRNA Hydrolase from Acinetobacter Baumannii at 1.49 A resolution

Released:
DOI: 10.2210/pdb4olj/pdb
Model geometry
Fit model/data
PDB entry 4olj coloured by chain, front view.
PDB entry 4olj coloured by chain, side view.
PDB entry 4olj coloured by chain, top view.
Source organism: Acinetobacter baumannii ATCC 19606 = CIP 70.34 = JCM 6841
Entry authors: Sikarwar J, Dube D, Kaushik S, Sinha M, Kaur P, Sharma S, Singh TP

Function and Biology Details

Reaction catalysed: 
an N-acyl-L-alpha-aminoacyl-tRNA + H2O = an N-acyl-L-amino acid + a tRNA+ H(+).
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: 196 amino acids
Theoretical weight: 21.22 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

2 bound ligands:
Ligand GOL 1 x GOL
Ligand TLA 1 x TLA
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P212121
Unit cell:
a: 34.088Å b: 65.834Å c: 76.121Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.158 0.192
Expression system: Escherichia coli

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