Crystal structure of PRT3789 in complex with the bromodomain of human BRG1 (SMARCA4) and pVHL:ElonginC:ElonginB. Determined by X-ray diffraction at 2.11 Å resolution. Released 1 Oct 2025.
Explore 9DTX in 3D Show helices and sheets RCSB PDB PDBe
9DTX contains 30 α-helices and 29 β-strands across 4 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 | 2-9 | 8 | 1 |
| β-strand | 10 | 1 | 2 |
| β-strand | 12-19 | 8 | 1 |
| β-strand | 23 | 1 | 3 |
| α-helix | 24-35 | 12 | |
| α-helix | 39-41 | 3 | |
| β-strand | 42-46 | 5 | 1 |
| β-strand | 49-50 | 2 | 1 |
| α-helix | 51-52 | 2 | |
| β-strand | 56 | 1 | 3 |
| α-helix | 57-60 | 4 | |
| α-helix | 64-66 | 3 | |
| β-strand | 68 | 1 | 4 |
| β-strand | 71 | 1 | 4 |
| α-helix | 72 | 1 | |
| β-strand | 73-79 | 7 | 1 |
| β-strand | 80-81 | 2 | 5 |
| β-strand | 84-85 | 2 | 5 |
| α-helix | 86-87 | 2 | |
| β-strand | 90 | 1 | 2 |
| α-helix | 91-98 | 8 | |
| α-helix | 101-103 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 18-22 | 5 | 1 |
| β-strand | 28-32 | 5 | 1 |
| α-helix | 33-36 | 4 | |
| α-helix | 40-46 | 7 | |
| β-strand | 59-61 | 3 | 1 |
| α-helix | 67-83 | 17 | |
| α-helix | 89-94 | 6 | |
| α-helix | 97-110 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 71-78 | 8 | 6 |
| α-helix | 83 | 1 | |
| β-strand | 84-89 | 6 | 7 |
| β-strand | 95-97 | 3 | 7 |
| β-strand | 101 | 1 | 7 |
| β-strand | 106-112 | 7 | 6 |
| β-strand | 116-121 | 6 | 7 |
| β-strand | 127 | 1 | 7 |
| β-strand | 129-130 | 2 | 6 |
| β-strand | 133 | 1 | 6 |
| β-strand | 136 | 1 | 7 |
| α-helix | 145-146 | 2 | |
| β-strand | 147-152 | 6 | 6 |
| α-helix | 158-169 | 12 | |
| α-helix | 172-177 | 6 | |
| α-helix | 182-189 | 8 | |
| α-helix | 194-204 | 11 | |
| α-helix | 206-208 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1451 | 1 | |
| α-helix | 1453-1455 | 3 | |
| α-helix | 1456-1471 | 16 | |
| β-strand | 1473 | 1 | 8 |
| β-strand | 1480 | 1 | 8 |
| α-helix | 1481-1485 | 5 | |
| α-helix | 1488-1490 | 3 | |
| α-helix | 1495-1500 | 6 | |
| α-helix | 1507-1515 | 9 | |
| α-helix | 1522-1539 | 18 | |
| α-helix | 1545-1566 | 22 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Elongin-B | A | protein | 104 | Homo sapiens | Q15370 (AlphaFold model) |
| Elongin-C | B | protein | 96 | Homo sapiens | Q15369 (AlphaFold model) |
| von Hippel-Lindau disease tumor suppressor | C | protein | 161 | Homo sapiens | P40337 (AlphaFold model) |
| Transcription activator BRG1 | D | protein | 138 | Homo sapiens | P51532 (AlphaFold model) |
>9DTX_1 Elongin-B (chains A) MDVFLMIRRHKTTIFTDAKESSTVFELKRIVEGILKRPPDEQRLYKDDQLLDDGKTLGEC GFTSQTARPQAPATVGLAFRADDTFEALCIEPFSSPPELPDVMK
>9DTX_2 Elongin-C (chains B) MYVKLISSDGHEFIVKREHALTSGTIKAMLSGPGQFAENETNEVNFREIPSHVLSKVCMY FTYKVRYTNSSTEIPEFPIAPEIALELLMAANFLDC
>9DTX_3 von Hippel-Lindau disease tumor suppressor (chains C) GMEAGRPRPVLRSVNSREPSQVIFCNRSPRVVLPVWLNFDGEPQPYPTLPPGTGRRIHSY RGHLWLFRDAGTHDGLLVNQTELFVPSLNVDGQPIFANITLPVYTLKERCLQVVRSLVKP ENYRRLDIVRSLYEDLEDHPNVQKDLERLTQERIAHQRMGD
>9DTX_4 Transcription activator BRG1 (chains D) GGLNDIFEAQKIEWHEAEKLSPNPPNLTKKMKKIVDAVIKYKDSSSGRQLSEVFIQLPSR KELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSI VLQSVFTSVRQKIEKEDD
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1BB4 | (4R)-4-hydroxy-1-[(2R)-2-(3-{[(2S)-1-{(3R)-3-[(2M,6aS,11S)-2-(2-hydroxyphenyl)-… | C47 H58 N10 O6 S | 1 |
Water and common crystallization additives (CL, EDO, GOL) are not listed.
PRT3789 Is a First-in-Human SMARCA2-Selective Degrader That Induces Synthetic Lethality in SMARCA4-Mutated Cancers. Hulse, M., Wang, M., Xu, C. et al. Cancer Res (2026) 86:213-235. DOI 10.1158/0008-5472.CAN-25-1141 · PubMed
Other PDB entries of the same protein (UniProt Q15370 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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