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3J0D

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

Functional Information from GO Data
ChainGOidnamespacecontents
G0000027biological_processribosomal large subunit assembly
G0002181biological_processcytoplasmic translation
G0003735molecular_functionstructural constituent of ribosome
G0005515molecular_functionprotein binding
G0005737cellular_componentcytoplasm
G0005829cellular_componentcytosol
G0005840cellular_componentribosome
G0006412biological_processtranslation
G0006415biological_processtranslational termination
G0015968biological_processstringent response
G0019843molecular_functionrRNA binding
G0022625cellular_componentcytosolic large ribosomal subunit
G0070180molecular_functionlarge ribosomal subunit rRNA binding
G1990904cellular_componentribonucleoprotein complex
I0000049molecular_functiontRNA binding
I0000372biological_processGroup I intron splicing
I0002181biological_processcytoplasmic translation
I0003735molecular_functionstructural constituent of ribosome
I0005515molecular_functionprotein binding
I0005737cellular_componentcytoplasm
I0005829cellular_componentcytosol
I0005840cellular_componentribosome
I0006412biological_processtranslation
I0015935cellular_componentsmall ribosomal subunit
I0019843molecular_functionrRNA binding
I0022627cellular_componentcytosolic small ribosomal subunit
I0033120biological_processpositive regulation of RNA splicing
I0034336molecular_functionmisfolded RNA binding
I0034337biological_processRNA folding
I0046677biological_processresponse to antibiotic
I1990145biological_processmaintenance of translational fidelity
I1990904cellular_componentribonucleoprotein complex
J0005737cellular_componentcytoplasm
J0006412biological_processtranslation
J0006415biological_processtranslational termination
Functional Information from PROSITE/UniProt
site_idPS00055
Number of Residues8
DetailsRIBOSOMAL_S12 Ribosomal protein S12 signature. KkPNSAlR
ChainResidueDetails
ILYS42-ARG49

site_idPS00359
Number of Residues16
DetailsRIBOSOMAL_L11 Ribosomal protein L11 signature. RsIeGTarSMGlVVeD
ChainResidueDetails
GARG126-ASP141

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: 3-methylthioaspartic acid => ECO:0000269|PubMed:8844851
ChainResidueDetails
IASP88

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ILYS107
GLYS39

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122
ChainResidueDetails
GLYS71
GLYS80

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PDB entries from 2024-07-24

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