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3L1Y

Crystal structure of human UBC4 E2 conjugating enzyme

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
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
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
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

239149

PDB entries from 2025-07-23

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