Loading
PDBj
English日本語简体中文繁體中文한국어
✖
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help
SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9LTO

Cryo-EM structure of DDB1-DDA1-DET1-Ube2e2 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004842molecular_functionubiquitin-protein transferase activity
A0005515molecular_functionprotein binding
A0006513biological_processprotein monoubiquitination
A0006974biological_processDNA damage response
A0016567biological_processprotein ubiquitination
A0032020biological_processISG15-protein conjugation
A0042296molecular_functionISG15 transferase activity
A0061631molecular_functionubiquitin conjugating enzyme activity
A0070534biological_processprotein K63-linked ubiquitination
A0070936biological_processprotein K48-linked ubiquitination
A0070979biological_processprotein K11-linked ubiquitination
A1900087biological_processpositive regulation of G1/S transition of mitotic cell cycle
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0016567biological_processprotein ubiquitination
B0031461cellular_componentcullin-RING ubiquitin ligase complex
B0031464cellular_componentCul4A-RING E3 ubiquitin ligase complex
B0031625molecular_functionubiquitin protein ligase binding
B0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
B0044877molecular_functionprotein-containing complex binding
B0065003biological_processprotein-containing complex assembly
B0080008cellular_componentCul4-RING E3 ubiquitin ligase complex
B1990756molecular_functionubiquitin-like ligase-substrate adaptor activity
D0000209biological_processprotein polyubiquitination
D0005515molecular_functionprotein binding
D0005654cellular_componentnucleoplasm
D0016567biological_processprotein ubiquitination
D0031464cellular_componentCul4A-RING E3 ubiquitin ligase complex
D0031465cellular_componentCul4B-RING E3 ubiquitin ligase complex
D0032814biological_processregulation of natural killer cell activation
D0080008cellular_componentCul4-RING E3 ubiquitin ligase complex
S0000109cellular_componentnucleotide-excision repair complex
S0000781cellular_componentchromosome, telomeric region
S0003677molecular_functionDNA binding
S0003684molecular_functiondamaged DNA binding
S0005515molecular_functionprotein binding
S0005576cellular_componentextracellular region
S0005634cellular_componentnucleus
S0005654cellular_componentnucleoplasm
S0005730cellular_componentnucleolus
S0005737cellular_componentcytoplasm
S0006281biological_processDNA repair
S0006289biological_processnucleotide-excision repair
S0006511biological_processubiquitin-dependent protein catabolic process
S0006974biological_processDNA damage response
S0007056biological_processspindle assembly involved in female meiosis
S0007283biological_processspermatogenesis
S0008283biological_processcell population proliferation
S0010498biological_processproteasomal protein catabolic process
S0010506biological_processregulation of autophagy
S0016567biological_processprotein ubiquitination
S0019076biological_processviral release from host cell
S0030174biological_processregulation of DNA-templated DNA replication initiation
S0030674molecular_functionprotein-macromolecule adaptor activity
S0031297biological_processreplication fork processing
S0031464cellular_componentCul4A-RING E3 ubiquitin ligase complex
S0031465cellular_componentCul4B-RING E3 ubiquitin ligase complex
S0032814biological_processregulation of natural killer cell activation
S0032991cellular_componentprotein-containing complex
S0034644biological_processcellular response to UV
S0035861cellular_componentsite of double-strand break
S0040029biological_processepigenetic regulation of gene expression
S0042127biological_processregulation of cell population proliferation
S0042752biological_processregulation of circadian rhythm
S0042981biological_processregulation of apoptotic process
S0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
S0044725biological_processepigenetic programming in the zygotic pronuclei
S0044877molecular_functionprotein-containing complex binding
S0045070biological_processpositive regulation of viral genome replication
S0045722biological_processpositive regulation of gluconeogenesis
S0045732biological_processpositive regulation of protein catabolic process
S0045995biological_processregulation of embryonic development
S0046726biological_processpositive regulation by virus of viral protein levels in host cell
S0051702biological_processbiological process involved in interaction with symbiont
S0060964biological_processregulation of miRNA-mediated gene silencing
S0070062cellular_componentextracellular exosome
S0070914biological_processUV-damage excision repair
S0071987molecular_functionWD40-repeat domain binding
S0080008cellular_componentCul4-RING E3 ubiquitin ligase complex
S0080135biological_processregulation of cellular response to stress
S0097602molecular_functioncullin family protein binding
S0160072molecular_functionubiquitin ligase complex scaffold activity
S1901987biological_processregulation of cell cycle phase transition
S1901990biological_processregulation of mitotic cell cycle phase transition
S1902412biological_processregulation of mitotic cytokinesis
S1904178biological_processnegative regulation of adipose tissue development
S2000036biological_processregulation of stem cell population maintenance
Functional Information from PROSITE/UniProt
site_idPS00183
Number of Residues16
DetailsUBC_1 Ubiquitin-conjugating (UBC) active site signature. YHCNInsq.GvICLdiL
ChainResidueDetails
ATYR128-LEU143
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
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_FI2
Number of Residues343
DetailsRegion: {"description":"WD repeat beta-propeller A"}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q9ESW0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

254227

PDB entries from 2026-05-27

PDB statisticsPDBj update infoContact PDBjnumon