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7MEX

Structure of yeast Ubr1 in complex with Ubc2 and N-degron

Functional Information from GO Data
ChainGOidnamespacecontents
A0000151cellular_componentubiquitin ligase complex
A0000209biological_processprotein polyubiquitination
A0004842molecular_functionubiquitin-protein transferase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0006513biological_processprotein monoubiquitination
A0008270molecular_functionzinc ion binding
A0008540cellular_componentproteasome regulatory particle, base subcomplex
A0016567biological_processprotein ubiquitination
A0016740molecular_functiontransferase activity
A0034620biological_processcellular response to unfolded protein
A0036503biological_processERAD pathway
A0046872molecular_functionmetal ion binding
A0061630molecular_functionubiquitin protein ligase activity
A0071596biological_processubiquitin-dependent protein catabolic process via the N-end rule pathway
A0071629biological_processcytoplasm protein quality control by the ubiquitin-proteasome system
A0072671biological_processmitochondria-associated ubiquitin-dependent protein catabolic process
A0090089biological_processregulation of dipeptide transport
A0120174biological_processstress-induced homeostatically regulated protein degradation pathway
A1904855molecular_functionproteasome regulatory particle binding
A1990116biological_processribosome-associated ubiquitin-dependent protein catabolic process
A1990303cellular_componentUBR1-RAD6 ubiquitin ligase complex
Functional Information from PROSITE/UniProt
site_idPS00183
Number of Residues16
DetailsUBC_1 Ubiquitin-conjugating (UBC) active site signature. FHPNVyan.GeICLdiL
ChainResidueDetails
BPHE77-LEU92

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 Residues146
DetailsDomain: {"description":"UBC core","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"34789879","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by SGV1","evidences":[{"source":"PubMed","id":"16307922","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues73
DetailsZinc finger: {"description":"UBR-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00508","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues104
DetailsZinc finger: {"description":"RING-type; atypical","evidences":[{"source":"PubMed","id":"34789879","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsRegion: {"description":"Ubiquitin-binding loop","evidences":[{"source":"PubMed","id":"34789879","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues332
DetailsRegion: {"description":"Cap helical domain (CHD)","evidences":[{"source":"PubMed","id":"34789879","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues27
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"34789879","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7MEX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7MEY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues1
DetailsM-CSA 939
ChainResidueDetails
BCYS88nucleophile

247536

PDB entries from 2026-01-14

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