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3EQ4

Model of tRNA(Leu)-EF-Tu in the ribosomal pre-accommodated state revealed by cryo-EM

Functional Information from GO Data
ChainGOidnamespacecontents
I0000027biological_processribosomal large subunit assembly
I0002181biological_processcytoplasmic translation
I0003723molecular_functionRNA binding
I0003735molecular_functionstructural constituent of ribosome
I0005515molecular_functionprotein binding
I0005737cellular_componentcytoplasm
I0005829cellular_componentcytosol
I0005840cellular_componentribosome
I0006412biological_processtranslation
I0006415biological_processtranslational termination
I0015968biological_processstringent response
I0019843molecular_functionrRNA binding
I0022625cellular_componentcytosolic large ribosomal subunit
I0070180molecular_functionlarge ribosomal subunit rRNA binding
I1990904cellular_componentribonucleoprotein complex
L0000049molecular_functiontRNA binding
L0000372biological_processGroup I intron splicing
L0002181biological_processcytoplasmic translation
L0003723molecular_functionRNA binding
L0003735molecular_functionstructural constituent of ribosome
L0005515molecular_functionprotein binding
L0005737cellular_componentcytoplasm
L0005829cellular_componentcytosol
L0005840cellular_componentribosome
L0006412biological_processtranslation
L0015935cellular_componentsmall ribosomal subunit
L0019843molecular_functionrRNA binding
L0022627cellular_componentcytosolic small ribosomal subunit
L0033120biological_processpositive regulation of RNA splicing
L0034336molecular_functionmisfolded RNA binding
L0034337biological_processRNA folding
L0046677biological_processresponse to antibiotic
L1990145biological_processmaintenance of translational fidelity
L1990904cellular_componentribonucleoprotein complex
X0003746molecular_functiontranslation elongation factor activity
X0003924molecular_functionGTPase activity
X0005525molecular_functionGTP binding
X0006414biological_processtranslational elongation
Functional Information from PROSITE/UniProt
site_idPS00055
Number of Residues8
DetailsRIBOSOMAL_S12 Ribosomal protein S12 signature. KkPNSAlR
ChainResidueDetails
LLYS42-ARG49

site_idPS00301
Number of Residues16
DetailsG_TR_1 Translational (tr)-type guanine nucleotide-binding (G) domain signature. DNapeEKaRGITIntS
ChainResidueDetails
XASP50-SER65

site_idPS00359
Number of Residues16
DetailsRIBOSOMAL_L11 Ribosomal protein L11 signature. RsIeGTarSMGlVVeD
ChainResidueDetails
IARG126-ASP141

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N,N,N-trimethylalanine => ECO:0000269|PubMed:7004866
ChainResidueDetails
IALA1
XASP80
XASN135

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6,N6,N6-trimethyllysine => ECO:0000269|PubMed:7004866
ChainResidueDetails
ILYS3
ILYS39

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122
ChainResidueDetails
ILYS71
ILYS80
XLYS248
XLYS252
XLYS294

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:2022614, ECO:0000269|PubMed:389663, ECO:0000269|PubMed:6997043, ECO:0000269|PubMed:7021545
ChainResidueDetails
XLYS56

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122
ChainResidueDetails
XLYS313

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000305|PubMed:19150849, ECO:0000305|PubMed:24141193, ECO:0000305|PubMed:8416965
ChainResidueDetails
XTHR382

218853

PDB entries from 2024-04-24

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