9C5V
Cryo EM structure of a DCAF2:degrader:BRD4 ternary complex
This is a non-PDB format compatible entry.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| B | 0000781 | cellular_component | chromosome, telomeric region |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003684 | molecular_function | damaged DNA binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005615 | cellular_component | extracellular space |
| B | 0005634 | cellular_component | nucleus |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005730 | cellular_component | nucleolus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006281 | biological_process | DNA repair |
| B | 0006289 | biological_process | nucleotide-excision repair |
| B | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
| B | 0006974 | biological_process | DNA damage response |
| B | 0007056 | biological_process | spindle assembly involved in female meiosis |
| B | 0007283 | biological_process | spermatogenesis |
| B | 0008283 | biological_process | cell population proliferation |
| B | 0010498 | biological_process | proteasomal protein catabolic process |
| B | 0010506 | biological_process | regulation of autophagy |
| B | 0016567 | biological_process | protein ubiquitination |
| B | 0019076 | biological_process | viral release from host cell |
| B | 0030174 | biological_process | regulation of DNA-templated DNA replication initiation |
| B | 0030674 | molecular_function | protein-macromolecule adaptor activity |
| B | 0031297 | biological_process | replication fork processing |
| B | 0031464 | cellular_component | Cul4A-RING E3 ubiquitin ligase complex |
| B | 0031465 | cellular_component | Cul4B-RING E3 ubiquitin ligase complex |
| B | 0032814 | biological_process | regulation of natural killer cell activation |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0034644 | biological_process | cellular response to UV |
| B | 0035861 | cellular_component | site of double-strand break |
| B | 0040029 | biological_process | epigenetic regulation of gene expression |
| B | 0042127 | biological_process | regulation of cell population proliferation |
| B | 0042752 | biological_process | regulation of circadian rhythm |
| B | 0042981 | biological_process | regulation of apoptotic process |
| B | 0043161 | biological_process | proteasome-mediated ubiquitin-dependent protein catabolic process |
| B | 0044725 | biological_process | epigenetic programming in the zygotic pronuclei |
| B | 0044877 | molecular_function | protein-containing complex binding |
| B | 0045070 | biological_process | positive regulation of viral genome replication |
| B | 0045722 | biological_process | positive regulation of gluconeogenesis |
| B | 0045732 | biological_process | positive regulation of protein catabolic process |
| B | 0045995 | biological_process | regulation of embryonic development |
| B | 0046726 | biological_process | positive regulation by virus of viral protein levels in host cell |
| B | 0048511 | biological_process | rhythmic process |
| B | 0051702 | biological_process | biological process involved in interaction with symbiont |
| B | 0060964 | biological_process | regulation of miRNA-mediated gene silencing |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0070914 | biological_process | UV-damage excision repair |
| B | 0071987 | molecular_function | WD40-repeat domain binding |
| B | 0080008 | cellular_component | Cul4-RING E3 ubiquitin ligase complex |
| B | 0080135 | biological_process | regulation of cellular response to stress |
| B | 0097602 | molecular_function | cullin family protein binding |
| B | 0160072 | molecular_function | ubiquitin ligase complex scaffold activity |
| B | 1901987 | biological_process | regulation of cell cycle phase transition |
| B | 1901990 | biological_process | regulation of mitotic cell cycle phase transition |
| B | 1902412 | biological_process | regulation of mitotic cytokinesis |
| B | 1904178 | biological_process | negative regulation of adipose tissue development |
| B | 2000036 | biological_process | regulation of stem cell population maintenance |
| C | 0000209 | biological_process | protein polyubiquitination |
| C | 0005515 | molecular_function | protein binding |
| C | 0005654 | cellular_component | nucleoplasm |
| C | 0016567 | biological_process | protein ubiquitination |
| C | 0032436 | biological_process | positive regulation of proteasomal ubiquitin-dependent protein catabolic process |
| C | 0032814 | biological_process | regulation of natural killer cell activation |
| C | 0080008 | cellular_component | Cul4-RING E3 ubiquitin ligase complex |
Functional Information from PROSITE/UniProt
| site_id | PS00028 |
| Number of Residues | 22 |
| Details | ZINC_FINGER_C2H2_1 Zinc finger C2H2 type domain signature. Caps.CagdLenlyfqshHhhh..H |
| Chain | Residue | Details |
| A | CYS450-HIS471 |
| site_id | PS00633 |
| Number of Residues | 60 |
| Details | BROMODOMAIN_1 Bromodomain signature. AwpFqqpvDavklnlpDYYkiIktpMdmgtIkkrlenny..Ywnaqeciqdfnt.MftNCyiY |
| Chain | Residue | Details |
| D | ALA80-TYR139 |
| site_id | PS00678 |
| Number of Residues | 15 |
| Details | WD_REPEATS_1 Trp-Asp (WD) repeats signature. LVTAagDqTAKFWDV |
| Chain | Residue | Details |
| A | LEU113-VAL127 | |
| A | VAL231-LEU245 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 42 |
| Details | Repeat: {"description":"WD 1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 39 |
| Details | Repeat: {"description":"WD 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 40 |
| Details | Repeat: {"description":"WD 3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 39 |
| Details | Repeat: {"description":"WD 4"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 41 |
| Details | Repeat: {"description":"WD 5"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 41 |
| Details | Repeat: {"description":"WD 6"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 40 |
| Details | Repeat: {"description":"WD 7"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 6 |
| Details | Motif: {"description":"DDB1-binding motif"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 343 |
| Details | Region: {"description":"WD repeat beta-propeller A"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q9ESW0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 106 |
| Details | Domain: {"description":"Bromo 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00035","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 1 |
| Details | Site: {"description":"Acetylated histone binding","evidences":[{"source":"PubMed","id":"22464331","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
