6kl8

X-ray diffraction
1.94Å resolution

Crystal structure of Piptidyl t-RNA hydrolase from Acinetobacter baumannii with bound NaCl at the substrate binding site

Released:
Model geometry
Fit model/data
Entry authors: Viswanathan V, Sharma P, Singh PK, Sharma S, Singh TP

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)
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: 21.25 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

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RRCAT INDUS-2 BEAMLINE PX-BL21
Spacegroup: P212121
Unit cell:
a: 33.961Å b: 66.099Å c: 75.825Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.131 0.127 0.164
Expression system: Escherichia coli