3VJR

Crystal structure of Peptidyl-tRNA hydrolase from Escherichia coli in complex with the CCA-acceptor-T[PSI]C domain of tRNA

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	0071236	biological_process	cellular response to antibiotic
A	0072344	biological_process	rescue of stalled ribosome
C	0000049	molecular_function	tRNA binding
C	0003723	molecular_function	RNA binding
C	0004045	molecular_function	peptidyl-tRNA hydrolase activity
C	0005737	cellular_component	cytoplasm
C	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
C	0016787	molecular_function	hydrolase activity
C	0071236	biological_process	cellular response to antibiotic
C	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. YaaTRHNaGawFVD

Chain	Residue	Details
A	TYR19-ASP32

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

Chain	Residue	Details
A	GLY113-ILE123

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00083","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22923517","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9303320","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00083","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21718701","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00083","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22923517","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21718701","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	2
Details	Site: {"description":"Discriminates between blocked and unblocked aminoacyl-tRNA","evidences":[{"source":"HAMAP-Rule","id":"MF_00083","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21718701","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	2
Details	Site: {"description":"Stabilizes the basic form of H active site to accept a proton","evidences":[{"source":"HAMAP-Rule","id":"MF_00083","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21718701","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"22923517","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9303320","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 931

Chain	Residue	Details
A	HIS24	proton shuttle (general acid/base)
A	ASN72	electrostatic stabiliser
A	ASP97	electrostatic stabiliser, modifies pKa
A	ASN118	electrostatic stabiliser

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site_id	MCSA2
Number of Residues	4
Details	M-CSA 931

Chain	Residue	Details
C	HIS24	proton shuttle (general acid/base)
C	ASN72	electrostatic stabiliser
C	ASP97	electrostatic stabiliser, modifies pKa
C	ASN118	electrostatic stabiliser

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