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8X5T

Crystal structure of Thermus thermophilus peptidyl-tRNA hydrolase in complex with adenosine 5'-monophosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0003723molecular_functionRNA binding
A0004045molecular_functionpeptidyl-tRNA hydrolase activity
A0005737cellular_componentcytoplasm
A0006515biological_processprotein quality control for misfolded or incompletely synthesized proteins
A0016787molecular_functionhydrolase activity
A0072344biological_processrescue of stalled ribosome
B0000049molecular_functiontRNA binding
B0003723molecular_functionRNA binding
B0004045molecular_functionpeptidyl-tRNA hydrolase activity
B0005737cellular_componentcytoplasm
B0006515biological_processprotein quality control for misfolded or incompletely synthesized proteins
B0016787molecular_functionhydrolase activity
B0072344biological_processrescue of stalled ribosome
C0000049molecular_functiontRNA binding
C0003723molecular_functionRNA binding
C0004045molecular_functionpeptidyl-tRNA hydrolase activity
C0005737cellular_componentcytoplasm
C0006515biological_processprotein quality control for misfolded or incompletely synthesized proteins
C0016787molecular_functionhydrolase activity
C0072344biological_processrescue of stalled ribosome
Functional Information from PROSITE/UniProt
site_idPS01195
Number of Residues14
DetailsPEPT_TRNA_HYDROL_1 Peptidyl-tRNA hydrolase signature 1. YarTRHNlGfmVLD
ChainResidueDetails
ATYR14-ASP27

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00083
ChainResidueDetails
AHIS19
BHIS19
CHIS19

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00083
ChainResidueDetails
ATYR14
ATYR55
AASN57
BTYR14
BTYR55
BASN57
CTYR14
CTYR55
CASN57

site_idSWS_FT_FI3
Number of Residues3
DetailsSITE: Discriminates between blocked and unblocked aminoacyl-tRNA => ECO:0000255|HAMAP-Rule:MF_00083
ChainResidueDetails
AASN9
BASN9
CASN9

site_idSWS_FT_FI4
Number of Residues3
DetailsSITE: Stabilizes the basic form of H active site to accept a proton => ECO:0000255|HAMAP-Rule:MF_00083
ChainResidueDetails
AASP82
BASP82
CASP82

236620

PDB entries from 2025-05-28

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