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4P7B

Crystal structure of S. typhimurium peptidyl-tRNA hydrolase

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
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 PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue TRS A 201
ChainResidue
AASP30
ATYR49
AHOH513

site_idAC2
Number of Residues5
Detailsbinding site for residue TRS C 201
ChainResidue
CASP30
CHOH304
CHOH325
CHOH438
CHOH559

Functional Information from PROSITE/UniProt
site_idPS01195
Number of Residues14
DetailsPEPT_TRNA_HYDROL_1 Peptidyl-tRNA hydrolase signature 1. YaaTRHNaGawYVD
ChainResidueDetails
ATYR17-ASP30

site_idPS01196
Number of Residues11
DetailsPEPT_TRNA_HYDROL_2 Peptidyl-tRNA hydrolase signature 2. GhggHNGLKDI
ChainResidueDetails
AGLY111-ILE121

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00083","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00083","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
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 Residues2
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

247536

PDB entries from 2026-01-14

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