Ternary structure of intramolecular bivalent glue degrader IBG1 bound to BRD4 and DCAF16:DDB1deltaBPB. Determined by electron microscopy at 3.77 Å resolution. Released 17 May 2023.
Explore 8OV6 in 3D Show helices and sheets RCSB PDB PDBe
8OV6 contains 37 α-helices and 70 β-strands across 3 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-10 | 7 | 1 |
| β-strand | 18-21 | 4 | 2 |
| β-strand | 30-35 | 6 | 2 |
| β-strand | 38-44 | 7 | 2 |
| β-strand | 49-56 | 8 | 2 |
| β-strand | 61-67 | 7 | 3 |
| β-strand | 76-81 | 6 | 3 |
| β-strand | 85-94 | 10 | 3 |
| β-strand | 97-107 | 11 | 3 |
| β-strand | 121-124 | 4 | 4 |
| β-strand | 130-136 | 7 | 4 |
| β-strand | 139-144 | 6 | 4 |
| β-strand | 155-158 | 4 | 4 |
| β-strand | 164-169 | 6 | 5 |
| β-strand | 177-184 | 8 | 5 |
| β-strand | 187-196 | 10 | 5 |
| β-strand | 201-204 | 4 | 5 |
| β-strand | 210-211 | 2 | 5 |
| β-strand | 218-221 | 4 | 6 |
| β-strand | 229-232 | 4 | 6 |
| β-strand | 237-241 | 5 | 6 |
| β-strand | 244-248 | 5 | 6 |
| α-helix | 251-255 | 5 | |
| β-strand | 258-263 | 6 | 7 |
| β-strand | 270-275 | 6 | 7 |
| β-strand | 279-289 | 11 | 7 |
| β-strand | 295-307 | 13 | 7 |
| β-strand | 313-318 | 6 | 8 |
| β-strand | 321-325 | 5 | 8 |
| β-strand | 332-336 | 5 | 8 |
| β-strand | 347-352 | 6 | 8 |
| β-strand | 361-365 | 5 | 9 |
| β-strand | 374-379 | 6 | 9 |
| α-helix | 382-384 | 3 | |
| β-strand | 386-392 | 7 | 9 |
| β-strand | 710-712 | 3 | 9 |
| β-strand | 716 | 1 | 9 |
| β-strand | 720-727 | 8 | 10 |
| β-strand | 732-742 | 11 | 10 |
| β-strand | 750-751 | 2 | 10 |
| α-helix | 756-758 | 3 | |
| β-strand | 762-765 | 4 | 10 |
| β-strand | 785-795 | 11 | 10 |
| β-strand | 801-806 | 6 | 10 |
| α-helix | 807-808 | 2 | |
| β-strand | 812-819 | 8 | 11 |
| β-strand | 828-834 | 7 | 11 |
| β-strand | 846-854 | 9 | 11 |
| β-strand | 857-866 | 10 | 11 |
| β-strand | 870-876 | 7 | 12 |
| β-strand | 879-884 | 6 | 12 |
| β-strand | 887-893 | 7 | 12 |
| β-strand | 899-903 | 5 | 12 |
| β-strand | 911-913 | 3 | 13 |
| β-strand | 916-917 | 2 | 13 |
| β-strand | 920-925 | 6 | 13 |
| β-strand | 928 | 1 | 14 |
| β-strand | 930-936 | 7 | 13 |
| β-strand | 941-947 | 7 | 13 |
| β-strand | 952 | 1 | 14 |
| β-strand | 954-959 | 6 | 15 |
| β-strand | 964-969 | 6 | 15 |
| β-strand | 973-979 | 7 | 15 |
| α-helix | 987-989 | 3 | |
| β-strand | 991 | 1 | 13 |
| β-strand | 992-998 | 7 | 15 |
| β-strand | 1004-1008 | 5 | 1 |
| β-strand | 1025-1032 | 8 | 1 |
| β-strand | 1037-1042 | 6 | 1 |
| α-helix | 1045-1058 | 14 | |
| α-helix | 1070-1073 | 4 | |
| β-strand | 1076-1077 | 2 | 16 |
| β-strand | 1082-1083 | 2 | 16 |
| β-strand | 1086 | 1 | 15 |
| β-strand | 1088-1090 | 3 | 1 |
| α-helix | 1091-1095 | 5 | |
| α-helix | 1096-1098 | 3 | |
| α-helix | 1102-1109 | 8 | |
| α-helix | 1126-1137 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 48-61 | 14 | |
| β-strand | 66-67 | 2 | 17 |
| α-helix | 68-70 | 3 | |
| α-helix | 74-76 | 3 | |
| α-helix | 88-95 | 8 | |
| β-strand | 99-100 | 2 | 17 |
| α-helix | 107-111 | 5 | |
| α-helix | 116-119 | 4 | |
| α-helix | 131-138 | 8 | |
| α-helix | 143-156 | 14 | |
| α-helix | 179-190 | 12 | |
| α-helix | 201-215 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 61-65 | 5 | |
| α-helix | 66-70 | 5 | |
| α-helix | 71-76 | 6 | |
| α-helix | 81-83 | 3 | |
| α-helix | 89-92 | 4 | |
| α-helix | 97-100 | 4 | |
| α-helix | 107-115 | 9 | |
| α-helix | 123-139 | 17 | |
| α-helix | 145-161 | 17 | |
| α-helix | 350-364 | 15 | |
| α-helix | 374-376 | 3 | |
| α-helix | 379-381 | 3 | |
| α-helix | 390-393 | 4 | |
| α-helix | 400-408 | 9 | |
| α-helix | 415-432 | 18 | |
| α-helix | 438-454 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DDB1deltaBPB | A | protein | 836 | Homo sapiens | Q16531 (AlphaFold model) |
| DDB1- and CUL4-associated factor 16 | B | protein | 218 | Homo sapiens | Q9NXF7 (AlphaFold model) |
| Bromodomain-containing protein 4 | C | protein | 419 | Homo sapiens | O60885 (AlphaFold model) |
>8OV6_1 DDB1deltaBPB (chains A) MSYNYVVTAQKPTAVNGCVTGHFTSAEDLNLLIAKNTRLEIYVVTAEGLRPVKEVGMYGK IAVMELFRPKGESKDLLFILTAKYNACILEYKQSGESIDIITRAHGNVQDRIGRPSETGI IGIIDPECRMIGLRLYDGLFKVIPLDRDNKELKAFNIRLEELHVIDVKFLYGCQAPTICF VYQDPQGRHVKTYEVSLREKEFNKGPWKQENVEAEASMVIAVPEPFGGAIIIGQESITYH NGDKYLAIAPPIIKQSTIVCHNRVDPNGSRYLLGDMEGRLFMLLLEKEEQMDGTVTLKDL RVELLGETSIAECLTYLDNGVVFVGSRLGDSQLVKLNVDSNEQGSYVVAMETFTNLGPIV DMCVVDLERQGQGQLVTCSGAFKEGSLRIIRNGIGGNGNSGEIQKLHIRTVPLYESPRKI CYQEVSQCFGVLSSRIEVQDTSGGTTALRPSASTQALSSSVSSSKLFSSSTAPHETSFGE EVEVHNLLIIDQHTFEVLHAHQFLQNEYALSLVSCKLGKDPNTYFIVGTAMVYPEEAEPK QGRIVVFQYSDGKLQTVAEKEVKGAVYSMVEFNGKLLASINSTVRLYEWTTEKELRTECN HYNNIMALYLKTKGDFILVGDLMRSVLLLAYKPMEGNFEEIARDFNPNWMSAVEILDDDN FLGAENAFNLFVCQKDSAATTDEERQHLQEVGLFHLGEFVNVFCHGSLVMQNLGETSTPT QGSVLFGTVNGMIGLVTSLSESWYNLLLDMQNRLNKVIKSVGKIEHSFWRSFHTERKTEP ATGFIDGDLIESFLDISRPKMQEVVANLQYDDGSGMKREATADDLIKVVEELTRIH
>8OV6_2 DDB1- and CUL4-associated factor 16 (chains B) GGMGPRNPSPDHLSESESEEEENISYLNESSGEEWDSSEEEDSMVPNLSPLESLAWQVKC LLKYSTTWKPLNPNSWLYHAKLLDPSTPVHILREIGLRLSHCSHCVPKLEPIPEWPPLAS CGVPPFQKPLTSPSRLSRDHATLNGALQFATKQLSRTLSRATPIPEYLKQIPNSCVSGCC CGWLTKTVKETTRTEPINTTYSYTDFQKAVNKLLTASL
>8OV6_3 Bromodomain-containing protein 4 (chains C) GSTNPPPPETSNPNKPKRQTNQLQYLLRVVLKTLWKHQFAWPFQQPVDAVKLNLPDYYKI IKTPMDMGTIKKRLENNYYWNAQECIQDFNTMFTNCYIYNKPGDDIVLMAEALEKLFLQK INELPTEETEIMIVQAKGRGRGRKETGTAKPGVSTVPNTTQASTPPQTQTPQPNPPPVQA TPHPFPAVTPDLIVQTPVMTVVPPQPLQTPPPVPPQPQPPPAPAPQPVQSHPPIIAATPQ PVKTKKGVKRKADTTTPTTIDPIHEPPSLPPEPKTTKLGQRRESSRPVKPPKKDVPDSQQ HPAPEKSSKVSEQLKCCSGILKEMFAKKHAAYAWPFYKPVDVEALGLHDYCDIIKHPMDM STIKSKLEAREYRDAQEFGADVRLMFSNCYKYNPPDHEVVAMARKLQDVFEMRFAKMPD
| ID | Name | Formula | Copies |
|---|---|---|---|
| U79 | methyl 2-[(9~{S})-7-[4-[4-[[4-[(3-cyano-4-methyl-1~{H}-indol-7-yl)sulfamoyl]phe… | C44 H38 N8 O5 S2 | 1 |
| ZN | Zinc ion | Zn | 1 |
Targeted protein degradation via intramolecular bivalent glues. Hsia, O., Hinterndorfer, M., Cowan, A.D. et al. Nature (2024) 627:204-211. DOI 10.1038/s41586-024-07089-6 · PubMed
Other PDB entries of the same protein (UniProt Q16531 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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