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5AIE

Not4 ring domain in complex with Ubc4

Functional Information from GO Data
ChainGOidnamespacecontents
A0004842molecular_functionubiquitin-protein transferase activity
A0030014cellular_componentCCR4-NOT complex
B0000166molecular_functionnucleotide binding
B0000209biological_processprotein polyubiquitination
B0004842molecular_functionubiquitin-protein transferase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0006511biological_processubiquitin-dependent protein catabolic process
B0016567biological_processprotein ubiquitination
B0016740molecular_functiontransferase activity
B0030674molecular_functionprotein-macromolecule adaptor activity
B0034605biological_processcellular response to heat
B0043130molecular_functionubiquitin binding
B0043162biological_processubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway
B0061631molecular_functionubiquitin conjugating enzyme activity
B0070628molecular_functionproteasome binding
B0071629biological_processcytoplasm protein quality control by the ubiquitin-proteasome system
B0072344biological_processrescue of stalled cytosolic ribosome
B0072671biological_processmitochondria-associated ubiquitin-dependent protein catabolic process
B1990116biological_processribosome-associated ubiquitin-dependent protein catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1083
ChainResidue
ACYS33
ACYS36
ACYS57
ACYS60

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1084
ChainResidue
ACYS50
ACYS52
ACYS74
ACYS77

Functional Information from PROSITE/UniProt
site_idPS00183
Number of Residues16
DetailsUBC_1 Ubiquitin-conjugating (UBC) active site signature. YHPNInan.GnICLdiL
ChainResidueDetails
BTYR75-LEU90

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues45
DetailsZinc finger: {"description":"RING-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00175","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues146
DetailsDomain: {"description":"UBC core","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues21
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues11
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsActive site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

250835

PDB entries from 2026-03-18

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