Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4ERX

Crystal structure of the complex of peptidyl-tRNA hydrolase from Pseudomonas aeruginosa with diethylene glycol at 2.5 Angstrom resolution

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
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PEG A 201
ChainResidue
AHIS22
AASP95
ALEU97
AHIS115
AASN116
AGLU161
AHOH366

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PEG B 201
ChainResidue
BGLY114
BHIS115
BASN116
BVAL151
BHOH383
BHIS22
BASP95

Functional Information from PROSITE/UniProt
site_idPS01195
Number of Residues14
DetailsPEPT_TRNA_HYDROL_1 Peptidyl-tRNA hydrolase signature 1. YdqTRHNaGalFVE
ChainResidueDetails
ATYR17-GLU30

site_idPS01196
Number of Residues11
DetailsPEPT_TRNA_HYDROL_2 Peptidyl-tRNA hydrolase signature 2. GhggHNGLRDI
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"},{"source":"PubMed","id":"25101795","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00083","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"25101795","evidenceCode":"ECO:0000305"}]}
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"},{"source":"PubMed","id":"25101795","evidenceCode":"ECO:0000305"}]}
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

239149

PDB entries from 2025-07-23

PDB statisticsPDBj update infoContact PDBjnumon