Cryo-EM structure of human DDB1-CRBN-GSPT1 in complex with GT19630. Determined by electron microscopy at 2.9 Å resolution. Released 26 Aug 2026.
Explore 12BP in 3D Show helices and sheets RCSB PDB PDBe
12BP contains 23 α-helices and 106 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 | 530-537 | 8 | 1 |
| β-strand | 549-552 | 4 | 1 |
| β-strand | 554 | 1 | 2 |
| β-strand | 557 | 1 | 2 |
| β-strand | 560-565 | 6 | 1 |
| β-strand | 570 | 1 | 3 |
| α-helix | 576 | 1 | |
| β-strand | 577 | 1 | 3 |
| α-helix | 578 | 1 | |
| β-strand | 589-591 | 3 | 1 |
| β-strand | 594-597 | 4 | 1 |
| β-strand | 617-618 | 2 | 1 |
| β-strand | 623-625 | 3 | 1 |
| β-strand | 628-633 | 6 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-10 | 7 | 13 |
| β-strand | 17-21 | 5 | 14 |
| β-strand | 30-35 | 6 | 14 |
| β-strand | 38-44 | 7 | 14 |
| β-strand | 49-56 | 8 | 14 |
| β-strand | 61-67 | 7 | 15 |
| β-strand | 76-81 | 6 | 15 |
| β-strand | 85-92 | 8 | 15 |
| β-strand | 99-107 | 9 | 15 |
| β-strand | 115 | 1 | 16 |
| β-strand | 121-124 | 4 | 17 |
| β-strand | 130-134 | 5 | 17 |
| β-strand | 136 | 1 | 16 |
| β-strand | 139-144 | 6 | 17 |
| β-strand | 155-158 | 4 | 17 |
| β-strand | 163-169 | 7 | 18 |
| α-helix | 170 | 1 | |
| β-strand | 177-184 | 8 | 18 |
| β-strand | 187-194 | 8 | 18 |
| β-strand | 195-196 | 2 | 19 |
| β-strand | 201-202 | 2 | 19 |
| β-strand | 208 | 1 | 18 |
| β-strand | 212 | 1 | 18 |
| β-strand | 219-221 | 3 | 20 |
| β-strand | 229-232 | 4 | 20 |
| β-strand | 237-241 | 5 | 20 |
| β-strand | 244-248 | 5 | 20 |
| β-strand | 258-263 | 6 | 21 |
| β-strand | 270-275 | 6 | 21 |
| β-strand | 279-288 | 10 | 21 |
| β-strand | 296-307 | 12 | 21 |
| β-strand | 311-318 | 8 | 22 |
| β-strand | 321-326 | 6 | 22 |
| β-strand | 331-336 | 6 | 22 |
| β-strand | 347-353 | 7 | 22 |
| β-strand | 359-365 | 7 | 23 |
| β-strand | 374-379 | 6 | 23 |
| α-helix | 382-384 | 3 | |
| β-strand | 386-391 | 6 | 23 |
| β-strand | 711-716 | 6 | 23 |
| β-strand | 720-727 | 8 | 24 |
| β-strand | 732-742 | 11 | 24 |
| β-strand | 750-751 | 2 | 24 |
| β-strand | 763-765 | 3 | 24 |
| β-strand | 785-795 | 11 | 24 |
| β-strand | 801-806 | 6 | 24 |
| β-strand | 811-819 | 9 | 25 |
| β-strand | 828-835 | 8 | 25 |
| β-strand | 845-854 | 10 | 25 |
| β-strand | 857-864 | 8 | 25 |
| β-strand | 870-876 | 7 | 26 |
| β-strand | 879-884 | 6 | 26 |
| β-strand | 887-893 | 7 | 26 |
| β-strand | 899-906 | 8 | 26 |
| β-strand | 913-917 | 5 | 27 |
| β-strand | 920-924 | 5 | 27 |
| β-strand | 929-935 | 7 | 27 |
| β-strand | 942-949 | 8 | 27 |
| β-strand | 956-959 | 4 | 28 |
| β-strand | 964-969 | 6 | 28 |
| β-strand | 973-979 | 7 | 28 |
| α-helix | 986-989 | 4 | |
| β-strand | 992-999 | 8 | 28 |
| β-strand | 1004-1009 | 6 | 13 |
| β-strand | 1024-1032 | 9 | 13 |
| β-strand | 1037-1043 | 7 | 13 |
| α-helix | 1045-1059 | 15 | |
| α-helix | 1063-1064 | 2 | |
| α-helix | 1070-1074 | 5 | |
| β-strand | 1076-1077 | 2 | 29 |
| β-strand | 1082-1083 | 2 | 29 |
| β-strand | 1086 | 1 | 28 |
| β-strand | 1088-1090 | 3 | 13 |
| α-helix | 1091-1095 | 5 | |
| α-helix | 1096-1098 | 3 | |
| α-helix | 1102-1109 | 8 | |
| α-helix | 1127-1136 | 10 | |
| α-helix | 1137-1139 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 78 | 1 | 4 |
| β-strand | 82-83 | 2 | 4 |
| β-strand | 96-98 | 3 | 4 |
| β-strand | 101 | 1 | 5 |
| α-helix | 104-115 | 12 | |
| β-strand | 119-124 | 6 | 4 |
| β-strand | 127 | 1 | 6 |
| α-helix | 128-130 | 3 | |
| β-strand | 132 | 1 | 6 |
| β-strand | 135-143 | 9 | 4 |
| β-strand | 155 | 1 | 5 |
| β-strand | 158-172 | 15 | 4 |
| β-strand | 178-184 | 7 | 4 |
| α-helix | 204-206 | 3 | |
| α-helix | 221-231 | 11 | |
| α-helix | 232-235 | 4 | |
| α-helix | 250-264 | 15 | |
| α-helix | 277-287 | 11 | |
| α-helix | 292-300 | 9 | |
| α-helix | 304-315 | 12 | |
| β-strand | 320-322 | 3 | 7 |
| β-strand | 332-333 | 2 | 7 |
| α-helix | 334-336 | 3 | |
| β-strand | 337-338 | 2 | 8 |
| β-strand | 341 | 1 | 9 |
| β-strand | 344 | 1 | 9 |
| β-strand | 348-351 | 4 | 10 |
| β-strand | 355-358 | 4 | 10 |
| β-strand | 361-362 | 2 | 8 |
| β-strand | 371-375 | 5 | 11 |
| β-strand | 384-385 | 2 | 12 |
| β-strand | 386-390 | 5 | 11 |
| β-strand | 397-400 | 4 | 11 |
| β-strand | 402-404 | 3 | 12 |
| β-strand | 413-414 | 2 | 12 |
| β-strand | 417 | 1 | 11 |
| β-strand | 423-425 | 3 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Eukaryotic peptide chain release factor GTP-binding subunit ERF3A | X | protein | 218 | Homo sapiens | P15170 (AlphaFold model) |
| Protein cereblon | Z | protein | 406 | Homo sapiens | Q96SW2 (AlphaFold model) |
| DNA damage-binding protein 1 | Y | protein | 836 | Homo sapiens | Q16531 (AlphaFold model) |
>12BP_1 Eukaryotic peptide chain release factor GTP-binding subunit ERF3A (chains X) MGSSHHHHHHSSGLVPRGSHMGPIRLPIVDKYKDMGTVVLGKLESGSICKGQQLVMMPNK HNVEVLGILSDDVETDTVAPGENLKIRLKGIEEEEILPGFILCDPNNLCHSGRTFDAQIV IIEHKSIICPGYNAVLHIHTCIEEVEITALICLVDKKSGEKSKTRPRFVKQDQVCIARLR TAGTICLETFKDFPQMGRFTLRDEGKTIAIGKVLKLVP
>12BP_2 Protein cereblon (chains Z) SNMEAKKPNIINFDTSLPTSHTYLGADMEEFHGRTLHDDDSCQVIPVLPQVMMILIPGQT LPLQLFHPQEVSMVRNLIQKDRTFAVLAYSNVQEREAQFGTTAEIYAYREEQDFGIEIVK VKAIGRQRFKVLELRTQSDGIQQAKVQILPECVLPSTMSAVQLESLNKCQIFPSKPVSRE DQCSYKWWQKYQKRKFHCANLTSWPRWLYSLYDAETLMDRIKKQLREWDENLKDDSLPSN PIDFSYRVAACLPIDDVLRIQLLKIGSAIQRLRCELDIMNKCTSLCCKQCQETEITTKNE IFSLSLCGPMAAYVNPHGYVHETLTVYKACNLNLIGRPSTEHSWFPGYAWTVAQCKICAS HIGWKFTATKKDMSPQKFWGLTRSALLPTIPDTEDEISPDKVILCL
>12BP_3 DNA damage-binding protein 1 (chains Y) MSYNYVVTAQKPTAVNGCVTGHFTSAEDLNLLIAKNTRLEIYVVTAEGLRPVKEVGMYGK IAVMELFRPKGESKDLLFILTAKYNACILEYKQSGESIDIITRAHGNVQDRIGRPSETGI IGIIDPECRMIGLRLYDGLFKVIPLDRDNKELKAFNIRLEELHVIDVKFLYGCQAPTICF VYQDPQGRHVKTYEVSLREKEFNKGPWKQENVEAEASMVIAVPEPFGGAIIIGQESITYH NGDKYLAIAPPIIKQSTIVCHNRVDPNGSRYLLGDMEGRLFMLLLEKEEQMDGTVTLKDL RVELLGETSIAECLTYLDNGVVFVGSRLGDSQLVKLNVDSNEQGSYVVAMETFTNLGPIV DMCVVDLERQGQGQLVTCSGAFKEGSLRIIRNGIGGNGNSGEIQKLHIRTVPLYESPRKI CYQEVSQCFGVLSSRIEVQDTSGGTTALRPSASTQALSSSVSSSKLFSSSTAPHETSFGE EVEVHNLLIIDQHTFEVLHAHQFLQNEYALSLVSCKLGKDPNTYFIVGTAMVYPEEAEPK QGRIVVFQYSDGKLQTVAEKEVKGAVYSMVEFNGKLLASINSTVRLYEWTTEKELRTECN HYNNIMALYLKTKGDFILVGDLMRSVLLLAYKPMEGNFEEIARDFNPNWMSAVEILDDDN FLGAENAFNLFVCQKDSAATTDEERQHLQEVGLFHLGEFVNVFCHGSLVMQNLGETSTPT QGSVLFGTVNGMIGLVTSLSESWYNLLLDMQNRLNKVIKSVGKIEHSFWRSFHTERKTEP ATGFIDGDLIESFLDISRPKMQEVVANLQYDDGSGMKREATADDLIKVVEELTRIH
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1DBR | 2-[(3S)-2,6-dioxopiperidin-3-yl]-1-oxo-N-[(4-{[2-(9H-pyrido[2,3-b]indol-9-yl)ac… | C35 H30 N6 O5 | 1 |
| ZN | Zinc ion | Zn | 1 |
Dual MYC and GSPT1 Protein Degrader for MYC-Driven Hematologic Malignancies. Nishida, Y., Impedovo, V., Ayoub, E. et al. Blood (2026). DOI 10.1182/blood.2025030170 · PubMed
Other PDB entries of the same protein (UniProt P15170 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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