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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1MJ1

FITTING THE TERNARY COMPLEX OF EF-Tu/tRNA/GTP AND RIBOSOMAL PROTEINS INTO A 13 A CRYO-EM MAP OF THE COLI 70S RIBOSOME

Functional Information from GO Data
ChainGOidnamespacecontents
A0003746molecular_functiontranslation elongation factor activity
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
A0006414biological_processtranslational elongation
L0003735molecular_functionstructural constituent of ribosome
L0005840cellular_componentribosome
L0006412biological_processtranslation
L0022625cellular_componentcytosolic large ribosomal subunit
L0070180molecular_functionlarge ribosomal subunit rRNA binding
O0000049molecular_functiontRNA binding
O0003735molecular_functionstructural constituent of ribosome
O0005840cellular_componentribosome
O0006412biological_processtranslation
O0015935cellular_componentsmall ribosomal subunit
O0019843molecular_functionrRNA binding
P0000049molecular_functiontRNA binding
P0003676molecular_functionnucleic acid binding
P0003723molecular_functionRNA binding
P0003735molecular_functionstructural constituent of ribosome
P0005829cellular_componentcytosol
P0005840cellular_componentribosome
P0006412biological_processtranslation
P0015935cellular_componentsmall ribosomal subunit
P0019843molecular_functionrRNA binding
Functional Information from PROSITE/UniProt
site_idPS00055
Number of Residues8
DetailsRIBOSOMAL_S12 Ribosomal protein S12 signature. KkPNSAlR
ChainResidueDetails
OLYS42-ARG49
site_idPS00301
Number of Residues16
DetailsG_TR_1 Translational (tr)-type guanine nucleotide-binding (G) domain signature. DKareERaRGITIntA
ChainResidueDetails
AASP51-ALA66
site_idPS00359
Number of Residues16
DetailsRIBOSOMAL_L11 Ribosomal protein L11 signature. KiIeGTakSMGiEVvD
ChainResidueDetails
LLYS119-ASP134
site_idPS00646
Number of Residues14
DetailsRIBOSOMAL_S13_1 Ribosomal protein S13 signature. RGlRHrrGlpVRGQ
ChainResidueDetails
PARG87-GLN100
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsRegion: {"description":"G1","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues4
DetailsRegion: {"description":"G2","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues3
DetailsRegion: {"description":"G3","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues3
DetailsRegion: {"description":"G4","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsRegion: {"description":"G5","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29546243","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5OPD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
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_FI8
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_FI9
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_FI10
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
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_FI12
Number of Residues1
DetailsModified residue: {"description":"3-methylthioaspartic acid","evidences":[{"source":"PubMed","id":"16287167","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25775268","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues11
DetailsCompositional bias: {"description":"Basic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues31
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
AASP21
site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
AHIS85
site_idMCSA1
Number of Residues4
DetailsM-CSA 535
ChainResidueDetails

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PDB entries from 2026-04-01

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