3V2I

Structure of a Peptidyl-tRNA hydrolase (PTH) from Burkholderia thailandensis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000049	molecular_function	tRNA binding
A	0003723	molecular_function	RNA binding
A	0004045	molecular_function	peptidyl-tRNA hydrolase activity
A	0005737	cellular_component	cytoplasm
A	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
A	0016787	molecular_function	hydrolase activity
A	0072344	biological_process	rescue of stalled ribosome

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CIT A 202

Chain	Residue
A	ARG19
A	ARG19
A	PHE157
A	LYS160
A	LYS160
A	ARG163
A	ARG163
A	HOH338

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Functional Information from PROSITE/UniProt

site_id	PS01195
Number of Residues	14
Details	PEPT_TRNA_HYDROL_1 Peptidyl-tRNA hydrolase signature 1. YtaTRHNaGfwLVD

Chain	Residue	Details
A	TYR15-ASP28

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site_id	PS01196
Number of Residues	11
Details	PEPT_TRNA_HYDROL_2 Peptidyl-tRNA hydrolase signature 2. GsggHNGLKDI

Chain	Residue	Details
A	GLY109-ILE119

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00083

Chain	Residue	Details
A	HIS20

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site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00083

Chain	Residue	Details
A	TYR15
A	TYR66
A	ASN68
A	ASN114

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site_id	SWS_FT_FI3
Number of Residues	1
Details	SITE: Discriminates between blocked and unblocked aminoacyl-tRNA => ECO:0000255|HAMAP-Rule:MF_00083

Chain	Residue	Details
A	ASN10

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site_id	SWS_FT_FI4
Number of Residues	1
Details	SITE: Stabilizes the basic form of H active site to accept a proton => ECO:0000255|HAMAP-Rule:MF_00083

Chain	Residue	Details
A	ASP93

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