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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
ChainGOidnamespacecontents
A0004045molecular_functionaminoacyl-tRNA hydrolase activity
A0005737cellular_componentcytoplasm
A0006412biological_processtranslation
A0006515biological_processprotein quality control for misfolded or incompletely synthesized proteins
A0016787molecular_functionhydrolase activity
C0004045molecular_functionaminoacyl-tRNA hydrolase activity
C0005737cellular_componentcytoplasm
C0006412biological_processtranslation
C0006515biological_processprotein quality control for misfolded or incompletely synthesized proteins
C0016787molecular_functionhydrolase activity
Functional Information from PROSITE/UniProt
site_idPS01195
Number of Residues14
DetailsPEPT_TRNA_HYDROL_1 Peptidyl-tRNA hydrolase signature 1. YaaTRHNaGawFVD
ChainResidueDetails
ATYR19-ASP32

site_idPS01196
Number of Residues11
DetailsPEPT_TRNA_HYDROL_2 Peptidyl-tRNA hydrolase signature 2. GhggHNGLKDI
ChainResidueDetails
AGLY113-ILE123

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 931
ChainResidueDetails
AHIS24proton shuttle (general acid/base)
AASN72electrostatic stabiliser
AASP97electrostatic stabiliser, modifies pKa
AASN118electrostatic stabiliser

site_idMCSA2
Number of Residues4
DetailsM-CSA 931
ChainResidueDetails
CHIS24proton shuttle (general acid/base)
CASN72electrostatic stabiliser
CASP97electrostatic stabiliser, modifies pKa
CASN118electrostatic stabiliser

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PDB entries from 2024-04-24

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