Annotations: 2PTH

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d2ptha_	Alpha and beta proteins (a/b)	Phosphorylase/hydrolase-like	Peptidyl-tRNA hydrolase-like	Peptidyl-tRNA hydrolase-like	Peptidyl-tRNA hydrolase	(Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Peptidyl-tRNA hydrolase-like	8032190	4000577	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Peptidyl-tRNA hydrolase-like	8044568	3000647	SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF01195	e2pthA1	A: a/b three-layered sandwiches	X: Phosphorylase/hydrolase-like	H: Peptidyl-tRNA hydrolase-like (From Topology)	T: Peptidyl-tRNA hydrolase-like	F: PF01195	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.1470	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Peptidyl-tRNA hydrolase	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF01195	Peptidyl-tRNA hydrolase (Pept_tRNA_hydro)	Peptidyl-tRNA hydrolase	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	PEPTIDYL-TRNA HYDROLASE	aminoacyl-tRNA hydrolase activity hydrolase activity, acting on ester bonds catalytic activity, acting on RNA catalytic activity, acting on a nucleic acid carboxylic ester hydrolase activity hydrolase activity catalytic activity, acting on a tRNA catalytic activity	organonitrogen compound catabolic process organonitrogen compound metabolic process catabolic process proteolysis involved in protein catabolic process primary metabolic process protein catabolic process macromolecule catabolic process organic substance metabolic process proteolysis metabolic process protein metabolic process macromolecule metabolic process protein quality control for misfolded or incompletely synthesized proteins organic substance catabolic process organonitrogen compound catabolic process organonitrogen compound metabolic process catabolic process proteolysis involved in protein catabolic process primary metabolic process protein catabolic process macromolecule catabolic process organic substance metabolic process proteolysis metabolic process protein metabolic process macromolecule metabolic process protein quality control for misfolded or incompletely synthesized proteins organic substance catabolic process cellular biosynthetic process cellular metabolic process organonitrogen compound biosynthetic process translation gene expression macromolecule biosynthetic process biosynthetic process organic substance biosynthetic process cellular process	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR018171	Peptidyl-tRNA hydrolase, conserved site	Conserved Site
A	IPR036416	Peptidyl-tRNA hydrolase superfamily	Homologous Superfamily
A	IPR001328	Peptidyl-tRNA hydrolase	Family

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	aminoacyl-tRNA hydrolase M-CSA #931	Peptidyl-tRNA hydrolase (PTH) is a bacterial enzyme that cleaves peptidyl-tRNA or N-acyl-aminoacyl-tRNA to yield free peptides or N-acyl-amino acids and tRNA. The natural substrate for this enzyme may be peptidyl-tRNA which drop off the ribosome during protein synthesis [PMID:1833189, PMID:8635758]. Bacterial PTH has been found to be evolutionary related to a yeast protein [PMID:8563640].	Defined by 4 residues: HIS:A-20ASN:A-68ASP:A-93ASN:A-114 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 3.1.1.29 (PDB Primary Data) Search M-CSA Motif + EC 3.1.1.29

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.