Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3J0E

Models for the T. thermophilus ribosome recycling factor and the E. coli elongation factor G bound to the E. coli post-termination complex

Functional Information from GO Data
ChainGOidnamespacecontents
F0000049molecular_functiontRNA binding
F0000372biological_processGroup I intron splicing
F0002181biological_processcytoplasmic translation
F0003735molecular_functionstructural constituent of ribosome
F0005515molecular_functionprotein binding
F0005737cellular_componentcytoplasm
F0005829cellular_componentcytosol
F0005840cellular_componentribosome
F0006412biological_processtranslation
F0015935cellular_componentsmall ribosomal subunit
F0019843molecular_functionrRNA binding
F0022627cellular_componentcytosolic small ribosomal subunit
F0033120biological_processpositive regulation of RNA splicing
F0034336molecular_functionmisfolded RNA binding
F0034337biological_processRNA folding
F0046677biological_processresponse to antibiotic
F1990145biological_processmaintenance of translational fidelity
F1990904cellular_componentribonucleoprotein complex
G0005737cellular_componentcytoplasm
G0006412biological_processtranslation
G0006415biological_processtranslational termination
G0043023molecular_functionribosomal large subunit binding
H0003746molecular_functiontranslation elongation factor activity
H0003924molecular_functionGTPase activity
H0005525molecular_functionGTP binding
H0005737cellular_componentcytoplasm
H0005829cellular_componentcytosol
H0006412biological_processtranslation
H0006414biological_processtranslational elongation
H0016787molecular_functionhydrolase activity
H0032790biological_processribosome disassembly
H0097216molecular_functionguanosine tetraphosphate binding
Functional Information from PROSITE/UniProt
site_idPS00055
Number of Residues8
DetailsRIBOSOMAL_S12 Ribosomal protein S12 signature. KkPNSAlR
ChainResidueDetails
FLYS42-ARG49

site_idPS00301
Number of Residues16
DetailsG_TR_1 Translational (tr)-type guanine nucleotide-binding (G) domain signature. DWmeqEQeRGITItsA
ChainResidueDetails
HASP51-ALA66

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
HALA17
HASP88
HASN142

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
HLYS504
HLYS643

224572

PDB entries from 2024-09-04

PDB statisticsPDBj update infoContact PDBjnumon