Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

8ASV

Cryo-EM structure of yeast Elongator complex

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
E0000049molecular_functiontRNA binding
E0002098biological_processtRNA wobble uridine modification
E0005515molecular_functionprotein binding
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005737cellular_componentcytoplasm
E0005777cellular_componentperoxisome
E0005829cellular_componentcytosol
E0006400biological_processtRNA modification
E0006417biological_processregulation of translation
E0008033biological_processtRNA processing
E0016887molecular_functionATP hydrolysis activity
E0033588cellular_componentelongator holoenzyme complex
E0042802molecular_functionidentical protein binding
F0000049molecular_functiontRNA binding
F0002098biological_processtRNA wobble uridine modification
F0005515molecular_functionprotein binding
F0005634cellular_componentnucleus
F0005654cellular_componentnucleoplasm
F0005737cellular_componentcytoplasm
F0006357biological_processregulation of transcription by RNA polymerase II
F0006417biological_processregulation of translation
F0008033biological_processtRNA processing
F0016887molecular_functionATP hydrolysis activity
F0032447biological_processprotein urmylation
F0033588cellular_componentelongator holoenzyme complex
F0042802molecular_functionidentical protein binding
G0000049molecular_functiontRNA binding
G0002098biological_processtRNA wobble uridine modification
G0005515molecular_functionprotein binding
G0005634cellular_componentnucleus
G0005654cellular_componentnucleoplasm
G0005737cellular_componentcytoplasm
G0006357biological_processregulation of transcription by RNA polymerase II
G0006417biological_processregulation of translation
G0008033biological_processtRNA processing
G0016887molecular_functionATP hydrolysis activity
G0033588cellular_componentelongator holoenzyme complex
G0042802molecular_functionidentical protein binding
H0000049molecular_functiontRNA binding
H0002098biological_processtRNA wobble uridine modification
H0005515molecular_functionprotein binding
H0005634cellular_componentnucleus
H0005654cellular_componentnucleoplasm
H0005737cellular_componentcytoplasm
H0005777cellular_componentperoxisome
H0005829cellular_componentcytosol
H0006400biological_processtRNA modification
H0006417biological_processregulation of translation
H0008033biological_processtRNA processing
H0016887molecular_functionATP hydrolysis activity
H0033588cellular_componentelongator holoenzyme complex
H0042802molecular_functionidentical protein binding
I0000049molecular_functiontRNA binding
I0002098biological_processtRNA wobble uridine modification
I0005515molecular_functionprotein binding
I0005634cellular_componentnucleus
I0005654cellular_componentnucleoplasm
I0005737cellular_componentcytoplasm
I0006357biological_processregulation of transcription by RNA polymerase II
I0006417biological_processregulation of translation
I0008033biological_processtRNA processing
I0016887molecular_functionATP hydrolysis activity
I0032447biological_processprotein urmylation
I0033588cellular_componentelongator holoenzyme complex
I0042802molecular_functionidentical protein binding
J0000049molecular_functiontRNA binding
J0002098biological_processtRNA wobble uridine modification
J0005515molecular_functionprotein binding
J0005634cellular_componentnucleus
J0005654cellular_componentnucleoplasm
J0005737cellular_componentcytoplasm
J0006357biological_processregulation of transcription by RNA polymerase II
J0006417biological_processregulation of translation
J0008033biological_processtRNA processing
J0016887molecular_functionATP hydrolysis activity
J0033588cellular_componentelongator holoenzyme complex
J0042802molecular_functionidentical protein binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"25569479","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues71
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues18
DetailsRegion: {"description":"Required for binding to tRNA","evidences":[{"source":"PubMed","id":"24750273","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues40
DetailsCompositional bias: {"description":"Low complexity","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
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 Residues10
DetailsCompositional bias: {"description":"Acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues152
DetailsDomain: {"description":"N-acetyltransferase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00532","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI21
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_FI22
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"A0A1C7D1B7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI23
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

site_idSWS_FT_FI24
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"25569479","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17330950","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

PDB statisticsPDBj update infoContact PDBjnumon