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9R85

Cryo-EM structure of the E3 ligase HECTD3 conjugated to ubiquitin

Functional Information from GO Data
ChainGOidnamespacecontents
A0004842molecular_functionubiquitin-protein transferase activity
A0005515molecular_functionprotein binding
A0016567biological_processprotein ubiquitination
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0048471cellular_componentperinuclear region of cytoplasm
A0061630molecular_functionubiquitin protein ligase activity
Functional Information from PROSITE/UniProt
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
CLYS27-ASP52

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues178
DetailsDomain: {"description":"DOC","evidences":[{"source":"PROSITE-ProRule","id":"PRU00614","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues345
DetailsDomain: {"description":"HECT","evidences":[{"source":"PROSITE-ProRule","id":"PRU00104","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Glycyl thioester intermediate"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

251174

PDB entries from 2026-03-25

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