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4WZ3

Crystal structure of the complex between LubX/LegU2/Lpp2887 U-box 1 and Homo sapiens UBE2D2

Functional Information from GO Data
ChainGOidnamespacecontents
A0000151cellular_componentubiquitin ligase complex
A0000209biological_processprotein polyubiquitination
A0004842molecular_functionubiquitin-protein transferase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005829cellular_componentcytosol
A0006511biological_processubiquitin-dependent protein catabolic process
A0016567biological_processprotein ubiquitination
A0016740molecular_functiontransferase activity
A0019787molecular_functionubiquitin-like protein transferase activity
A0031625molecular_functionubiquitin protein ligase binding
A0032991cellular_componentprotein-containing complex
A0036211biological_processprotein modification process
A0051865biological_processprotein autoubiquitination
A0061630molecular_functionubiquitin protein ligase activity
A0061631molecular_functionubiquitin conjugating enzyme activity
A0070062cellular_componentextracellular exosome
A0070936biological_processprotein K48-linked ubiquitination
B0000209biological_processprotein polyubiquitination
B0004842molecular_functionubiquitin-protein transferase activity
B0005576cellular_componentextracellular region
B0005737cellular_componentcytoplasm
B0006515biological_processprotein quality control for misfolded or incompletely synthesized proteins
B0016567biological_processprotein ubiquitination
B0016740molecular_functiontransferase activity
B0030018cellular_componentZ disc
B0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
B0043657cellular_componenthost cell
B0045862biological_processpositive regulation of proteolysis
B0051087molecular_functionprotein-folding chaperone binding
B0061630molecular_functionubiquitin protein ligase activity
B0071218biological_processcellular response to misfolded protein
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Glycyl thioester intermediate => ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133
ChainResidueDetails
ASER85

222036

PDB entries from 2024-07-03

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