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8J1P

Cryo-EM structure of Ufd4 in complex with K29/48 triUb

Functional Information from GO Data
ChainGOidnamespacecontents
A0000209biological_processprotein polyubiquitination
A0004842molecular_functionubiquitin-protein transferase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0006511biological_processubiquitin-dependent protein catabolic process
A0010994biological_processfree ubiquitin chain polymerization
A0016607cellular_componentnuclear speck
A0016740molecular_functiontransferase activity
A0035519biological_processprotein K29-linked ubiquitination
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0061630molecular_functionubiquitin protein ligase activity
A1904855molecular_functionproteasome regulatory particle binding
Functional Information from PROSITE/UniProt
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KacIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
DLYS27-ASP52
CLYS27-ASP52

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00104","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues75
DetailsDomain: {"description":"Ubiquitin-like 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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