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5ZX8

Crystal structure of peptidyl-tRNA hydrolase from Thermus thermophilus

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
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue FLC A 201
ChainResidue
AGLY11
AHOH353
AGLU12
AARG13
AARG68
ALYS157
AARG165
AMPD204
AHOH324
AHOH330

site_idAC2
Number of Residues12
Detailsbinding site for residue FLC A 202
ChainResidue
ASER-2
AARG18
APRO127
APRO128
AARG132
AGLU135
ATYR136
ASER139
AARG142
AHOH310
AHOH346
AHOH352

site_idAC3
Number of Residues8
Detailsbinding site for residue MPD A 203
ChainResidue
AGLY30
ASER32
AALA67
AILE72
APRO73
APRO74
ATHR114
AHOH363

site_idAC4
Number of Residues5
Detailsbinding site for residue MPD A 204
ChainResidue
APRO10
ATYR14
ATYR55
APHE69
AFLC201

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 Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00083","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00083","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsSite: {"description":"Discriminates between blocked and unblocked aminoacyl-tRNA","evidences":[{"source":"HAMAP-Rule","id":"MF_00083","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Stabilizes the basic form of H active site to accept a proton","evidences":[{"source":"HAMAP-Rule","id":"MF_00083","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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