2pth Summary



The structure was published by Schmitt, E., Mechulam, Y., Fromant, M., Plateau, P., and Blanquet, S., in 1997 in a paper entitled "Crystal structure at 1.2 A resolution and active site mapping of Escherichia coli peptidyl-tRNA hydrolase." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.2 Å and deposited in 1997.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of PEPTIDYL-TRNA HYDROLASE. This molecule has the UniProt identifier P0A7D1 (PTH_ECOLI)search. The sample contained 193 residues which is 99% of the natural sequence. Out of 193 residues 193 were observed and are deposited in the PDB.

The molecule is most likely monomeric.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A PEPTIDYL-TRNA HYDROLASE P0A7D1 (2-194) (PTH_ECOLI)search Escherichia coli K-12search 99% 193 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P0A7D1 (2 - 194) PEPTIDYL-TRNA HYDROLASE Escherichia coli K-12

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P0A7D1) Peptidyl-tRNA hydrolase-likesearch Rossmann foldsearch PF01195: Peptidyl-tRNA hydrolasesearch

Chain ID Biological process (GO) Cellular component (GO) Molecular function (GO)
A (P0A7D1) misfolded or incompletely synthesized protein catabolic processsearch cytoplasmsearch aminoacyl-tRNA hydrolase activitysearch hydrolase activitysearch

Chain InterPro annotation
A Peptidyl-tRNA hydrolasesearch Peptidyl-tRNA hydrolase, conserved sitesearch