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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1EFU

ELONGATION FACTOR COMPLEX EF-TU/EF-TS FROM ESCHERICHIA COLI

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0003723molecular_functionRNA binding
A0003746molecular_functiontranslation elongation factor activity
A0003924molecular_functionGTPase activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0006412biological_processtranslation
A0006414biological_processtranslational elongation
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0032045cellular_componentguanyl-nucleotide exchange factor complex
A0046677biological_processresponse to antibiotic
A0046872molecular_functionmetal ion binding
A0097216molecular_functionguanosine tetraphosphate binding
B0003746molecular_functiontranslation elongation factor activity
B0005085molecular_functionguanyl-nucleotide exchange factor activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006412biological_processtranslation
B0006414biological_processtranslational elongation
B0008270molecular_functionzinc ion binding
B0016020cellular_componentmembrane
B0032045cellular_componentguanyl-nucleotide exchange factor complex
C0000166molecular_functionnucleotide binding
C0000287molecular_functionmagnesium ion binding
C0003723molecular_functionRNA binding
C0003746molecular_functiontranslation elongation factor activity
C0003924molecular_functionGTPase activity
C0005515molecular_functionprotein binding
C0005525molecular_functionGTP binding
C0005737cellular_componentcytoplasm
C0005886cellular_componentplasma membrane
C0006412biological_processtranslation
C0006414biological_processtranslational elongation
C0016020cellular_componentmembrane
C0016787molecular_functionhydrolase activity
C0032045cellular_componentguanyl-nucleotide exchange factor complex
C0046677biological_processresponse to antibiotic
C0046872molecular_functionmetal ion binding
C0097216molecular_functionguanosine tetraphosphate binding
D0003746molecular_functiontranslation elongation factor activity
D0005085molecular_functionguanyl-nucleotide exchange factor activity
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006412biological_processtranslation
D0006414biological_processtranslational elongation
D0008270molecular_functionzinc ion binding
D0016020cellular_componentmembrane
D0032045cellular_componentguanyl-nucleotide exchange factor complex
Functional Information from PROSITE/UniProt
site_idPS00301
Number of Residues16
DetailsG_TR_1 Translational (tr)-type guanine nucleotide-binding (G) domain signature. DNapeEKaRGITIntS
ChainResidueDetails
AASP50-SER65
site_idPS01126
Number of Residues16
DetailsEF_TS_1 Elongation factor Ts signature 1. LRerTGaGMmDcKKAL
ChainResidueDetails
BLEU11-LEU26
site_idPS01127
Number of Residues11
DetailsEF_TS_2 Elongation factor Ts signature 2. EVNCQTDFVAK
ChainResidueDetails
BGLU74-LYS84
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsRegion: {"description":"G1","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues6
DetailsRegion: {"description":"G3","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues6
DetailsRegion: {"description":"G4","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues4
DetailsRegion: {"description":"G5","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29546243","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5OPD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00118","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19150849","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"24141193","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"8416965","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues28
DetailsBinding site: {}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues10
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues6
DetailsRegion: {"description":"Involved in Mg(2+) ion dislocation from EF-Tu","evidences":[{"source":"HAMAP-Rule","id":"MF_00050","evidenceCode":"ECO:0000255"}]}
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
CASP21
site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
AHIS84
site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
CHIS84

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PDB entries from 2025-07-16

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