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3EQ3

Model of tRNA(Trp)-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 Residues194
DetailsDomain: {"description":"tr-type G"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues7
DetailsRegion: {"description":"G1","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsRegion: {"description":"G2","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsRegion: {"description":"G3","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsRegion: {"description":"G4","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsRegion: {"description":"G5","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29546243","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5OPD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29546243","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5MI3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5OPD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"6997043","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7021545","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"2022614","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"389663","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6997043","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7021545","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19150849","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24141193","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8416965","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"3-methylthioaspartic acid","evidences":[{"source":"PubMed","id":"8844851","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"N,N,N-trimethylalanine","evidences":[{"source":"PubMed","id":"7004866","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues2
DetailsModified residue: {"description":"N6,N6,N6-trimethyllysine","evidences":[{"source":"PubMed","id":"7004866","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
XASP21

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
XHIS84

240971

PDB entries from 2025-08-27

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