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7csn

X-ray diffraction
1Å resolution

Crystal structure of peptidyl-tRNA hydrolase from Acinetobacter baumannii at 1.00 A resolution

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

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

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P212121
Unit cell:
a: 34Å b: 66.25Å c: 76.23Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.145 0.145 0.157
Expression system: Escherichia coli