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3L1Z

Crystal structure of the U-BOX domain of human E4B ubiquitin ligase in complex with UBCH5C E2 ubiquitin conjugating enzyme

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000166molecular_functionnucleotide binding
A0000209biological_processprotein polyubiquitination
A0004842molecular_functionubiquitin-protein transferase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006281biological_processDNA repair
A0006511biological_processubiquitin-dependent protein catabolic process
A0006513biological_processprotein monoubiquitination
A0006915biological_processapoptotic process
A0006974biological_processDNA damage response
A0010008cellular_componentendosome membrane
A0016567biological_processprotein ubiquitination
A0016740molecular_functiontransferase activity
A0030514biological_processnegative regulation of BMP signaling pathway
A0036211biological_processprotein modification process
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0051865biological_processprotein autoubiquitination
A0061630molecular_functionubiquitin protein ligase activity
A0061631molecular_functionubiquitin conjugating enzyme activity
A0070062cellular_componentextracellular exosome
A0070936biological_processprotein K48-linked ubiquitination
A0070979biological_processprotein K11-linked ubiquitination
A0085020biological_processprotein K6-linked ubiquitination
A1903955biological_processpositive regulation of protein targeting to mitochondrion
B0000151cellular_componentubiquitin ligase complex
B0004842molecular_functionubiquitin-protein transferase activity
B0016567biological_processprotein ubiquitination
B0034450molecular_functionubiquitin-ubiquitin ligase activity
B0036503biological_processERAD pathway
Functional Information from PROSITE/UniProt
site_idPS00183
Number of Residues16
DetailsUBC_1 Ubiquitin-conjugating (UBC) active site signature. YHPNInsn.GsICLdiL
ChainResidueDetails
ATYR74-LEU89

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":"PROSITE-ProRule","id":"PRU10133","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues73
DetailsDomain: {"description":"U-box"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

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