4QT4

Crystal structure of Peptidyl-tRNA hydrolase from a Gram-positive bacterium, Streptococcus pyogenes at 2.19 Angstrom resolution shows the Closed Structure of the Substrate Binding Cleft

Replaces:  4Q55

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

Functional Information from PROSITE/UniProt

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

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. SaggHNGIKSI

Chain	Residue	Details
A	SER109-ILE119

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00083

Chain	Residue	Details
A	HIS20
B	HIS20

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site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00083

Chain	Residue	Details
A	TYR15
A	PHE66
A	ASN68
A	ASN114
B	TYR15
B	PHE66
B	ASN68
B	ASN114

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site_id	SWS_FT_FI3
Number of Residues	2
Details	SITE: Discriminates between blocked and unblocked aminoacyl-tRNA => ECO:0000255|HAMAP-Rule:MF_00083

Chain	Residue	Details
A	ASN10
B	ASN10

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site_id	SWS_FT_FI4
Number of Residues	2
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
B	ASP93

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