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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8ASW

Cryo-EM structure of yeast Elp123 in complex with alanine tRNA

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
A0006357biological_processregulation of transcription by RNA polymerase II
A0006417biological_processregulation of translation
A0008033biological_processtRNA processing
A0015031biological_processprotein transport
A0033588cellular_componentelongator holoenzyme complex
A0042802molecular_functionidentical protein binding
B0002098biological_processtRNA wobble uridine modification
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0006357biological_processregulation of transcription by RNA polymerase II
B0006417biological_processregulation of translation
B0008017molecular_functionmicrotubule binding
B0008033biological_processtRNA processing
B0015031biological_processprotein transport
B0032447biological_processprotein urmylation
B0033588cellular_componentelongator holoenzyme complex
B0080090biological_processregulation of primary metabolic process
C0000049molecular_functiontRNA binding
C0002098biological_processtRNA wobble uridine modification
C0002926biological_processtRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation
C0003723molecular_functionRNA binding
C0003824molecular_functioncatalytic activity
C0004402molecular_functionhistone acetyltransferase activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0006417biological_processregulation of translation
C0008033biological_processtRNA processing
C0016740molecular_functiontransferase activity
C0016746molecular_functionacyltransferase activity
C0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
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
D0000049molecular_functiontRNA binding
D0002098biological_processtRNA wobble uridine modification
D0002926biological_processtRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006357biological_processregulation of transcription by RNA polymerase II
D0006417biological_processregulation of translation
D0008033biological_processtRNA processing
D0015031biological_processprotein transport
D0033588cellular_componentelongator holoenzyme complex
D0042802molecular_functionidentical protein binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues62
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues36
DetailsRegion: {"description":"Required for binding to tRNA","evidences":[{"source":"PubMed","id":"24750273","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues28
DetailsCompositional bias: {"description":"Low complexity","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues10
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"25569479","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine; by HRR25","evidences":[{"source":"PubMed","id":"25569479","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues38
DetailsRepeat: {"description":"WD 1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues39
DetailsRepeat: {"description":"WD 2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues37
DetailsRepeat: {"description":"WD 3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues43
DetailsRepeat: {"description":"WD 4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues39
DetailsRepeat: {"description":"WD 5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues41
DetailsRepeat: {"description":"WD 6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues39
DetailsRepeat: {"description":"WD 7","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues38
DetailsRepeat: {"description":"WD 8","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues44
DetailsRepeat: {"description":"WD 9","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues39
DetailsRepeat: {"description":"WD 10","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues41
DetailsRepeat: {"description":"WD 11","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues43
DetailsRepeat: {"description":"WD 12","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues38
DetailsRepeat: {"description":"WD 13","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues290
DetailsDomain: {"description":"Radical SAM core","evidences":[{"source":"PROSITE-ProRule","id":"PRU01266","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16420352","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31309145","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6QK7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"A0A1C7D1B7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"12872131","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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