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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8PU0

Cryo-EM structure of human Elp123 in complex with tRNA, desulpho-CoA, 5'-deoxyadenosine and methionine

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0002098biological_processtRNA wobble uridine modification
A0002926biological_processtRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006417biological_processregulation of translation
A0008033biological_processtRNA processing
A0033588cellular_componentelongator holoenzyme complex
B0000993molecular_functionRNA polymerase II complex binding
B0002098biological_processtRNA wobble uridine modification
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006357biological_processregulation of transcription by RNA polymerase II
B0006368biological_processtranscription elongation by RNA polymerase II
B0006417biological_processregulation of translation
B0008023cellular_componenttranscription elongation factor complex
B0008033biological_processtRNA processing
B0019901molecular_functionprotein kinase binding
B0033588cellular_componentelongator holoenzyme complex
C0000049molecular_functiontRNA binding
C0001764biological_processneuron migration
C0002098biological_processtRNA wobble uridine modification
C0002926biological_processtRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation
C0003723molecular_functionRNA binding
C0003824molecular_functioncatalytic activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005730cellular_componentnucleolus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006357biological_processregulation of transcription by RNA polymerase II
C0006417biological_processregulation of translation
C0007399biological_processnervous system development
C0007417biological_processcentral nervous system development
C0008033biological_processtRNA processing
C0016407molecular_functionacetyltransferase activity
C0016740molecular_functiontransferase activity
C0016746molecular_functionacyltransferase activity
C0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
C0030335biological_processpositive regulation of cell migration
C0033588cellular_componentelongator holoenzyme complex
C0046872molecular_functionmetal ion binding
C0051536molecular_functioniron-sulfur cluster binding
C0051539molecular_function4 iron, 4 sulfur cluster binding
C0106261molecular_functiontRNA uridine(34) acetyltransferase activity
E0000049molecular_functiontRNA binding
E0002098biological_processtRNA wobble uridine modification
E0002926biological_processtRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation
E0005515molecular_functionprotein binding
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0006417biological_processregulation of translation
E0008033biological_processtRNA processing
E0033588cellular_componentelongator holoenzyme complex
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues40
DetailsRepeat: {"description":"WD 1"}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues44
DetailsRepeat: {"description":"WD 2"}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues42
DetailsRepeat: {"description":"WD 4"}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues48
DetailsRepeat: {"description":"WD 6"}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues38
DetailsRepeat: {"description":"WD 9"}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues41
DetailsRepeat: {"description":"WD 13"}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues290
DetailsDomain: {"description":"Radical SAM core","evidences":[{"source":"PROSITE-ProRule","id":"PRU01266","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues151
DetailsDomain: {"description":"N-acetyltransferase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00532","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q02908","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"A0A1C7D1B7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9CZX0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by ALK","evidences":[{"source":"PubMed","id":"31341009","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"31341009","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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PDB entries from 2025-12-24

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