6BN9
Crystal structure of DDB1-CRBN-BRD4(BD1) complex bound to dBET70 PROTAC
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003676 | molecular_function | nucleic acid binding |
A | 0005634 | cellular_component | nucleus |
B | 0005515 | molecular_function | protein binding |
B | 0005634 | cellular_component | nucleus |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0016020 | cellular_component | membrane |
B | 0016567 | biological_process | protein ubiquitination |
B | 0030177 | biological_process | positive regulation of Wnt signaling pathway |
B | 0031333 | biological_process | negative regulation of protein-containing complex assembly |
B | 0031334 | biological_process | positive regulation of protein-containing complex assembly |
B | 0031464 | cellular_component | Cul4A-RING E3 ubiquitin ligase complex |
B | 0034766 | biological_process | negative regulation of monoatomic ion transmembrane transport |
B | 0035641 | biological_process | locomotory exploration behavior |
B | 0043161 | biological_process | proteasome-mediated ubiquitin-dependent protein catabolic process |
B | 0044325 | molecular_function | transmembrane transporter binding |
B | 0046872 | molecular_function | metal ion binding |
B | 0048471 | cellular_component | perinuclear region of cytoplasm |
B | 1902607 | biological_process | negative regulation of large conductance calcium-activated potassium channel activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue ZN B 501 |
Chain | Residue |
B | CYS323 |
B | CYS326 |
B | CYS391 |
B | CYS394 |
Functional Information from PROSITE/UniProt
site_id | PS00633 |
Number of Residues | 60 |
Details | BROMODOMAIN_1 Bromodomain signature. AwpFqqpvDavklnlpDYYkiIktpMdmgtIkkrlenny..Ywnaqeciqdfnt.MftNCyiY |
Chain | Residue | Details |
C | ALA80-TYR139 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | SITE: Acetylated histone binding => ECO:0000269|PubMed:22464331 |
Chain | Residue | Details |
C | ASN140 | |
B | GLN327 | |
B | SER379 | |
B | PHE381 | |
B | THR387 | |
B | LYS392 | |
B | ALA395 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
C | LYS99 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q9ESW0 |
Chain | Residue | Details |
A | THR1125 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
A | LYS1121 |