9DTX: PRT3789

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.

Method
X-ray diffraction
Resolution
2.11 Å
Organism
Homo sapiens
Chains
4
Atoms
4,199
Mol. weight
58.5 kDa
Ligands
A1BB4
Released
1 Oct 2025

Explore 9DTX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 9 helices, 13 β-strands

ElementResiduesLengthSheet
β-strand2-981
β-strand1012
β-strand12-1981
β-strand2313
α-helix24-3512
α-helix39-413
β-strand42-4651
β-strand49-5021
α-helix51-522
β-strand5613
α-helix57-604
α-helix64-663
β-strand6814
β-strand7114
α-helix721
β-strand73-7971
β-strand80-8125
β-strand84-8525
α-helix86-872
β-strand9012
α-helix91-988
α-helix101-1033
Chain B: 5 helices, 3 β-strands
ElementResiduesLengthSheet
β-strand18-2251
β-strand28-3251
α-helix33-364
α-helix40-467
β-strand59-6131
α-helix67-8317
α-helix89-946
α-helix97-11014
Chain C: 7 helices, 11 β-strands
ElementResiduesLengthSheet
β-strand71-7886
α-helix831
β-strand84-8967
β-strand95-9737
β-strand10117
β-strand106-11276
β-strand116-12167
β-strand12717
β-strand129-13026
β-strand13316
β-strand13617
α-helix145-1462
β-strand147-15266
α-helix158-16912
α-helix172-1776
α-helix182-1898
α-helix194-20411
α-helix206-2083
Chain D: 9 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix14511
α-helix1453-14553
α-helix1456-147116
β-strand147318
β-strand148018
α-helix1481-14855
α-helix1488-14903
α-helix1495-15006
α-helix1507-15159
α-helix1522-153918
α-helix1545-156622

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Elongin-BAprotein104Homo sapiensQ15370 (AlphaFold model)
Elongin-CBprotein96Homo sapiensQ15369 (AlphaFold model)
von Hippel-Lindau disease tumor suppressorCprotein161Homo sapiensP40337 (AlphaFold model)
Transcription activator BRG1Dprotein138Homo sapiensP51532 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9DTX_1 Elongin-B (chains A)
MDVFLMIRRHKTTIFTDAKESSTVFELKRIVEGILKRPPDEQRLYKDDQLLDDGKTLGEC
GFTSQTARPQAPATVGLAFRADDTFEALCIEPFSSPPELPDVMK
Sequence of entity 2 (B), FASTA
>9DTX_2 Elongin-C (chains B)
MYVKLISSDGHEFIVKREHALTSGTIKAMLSGPGQFAENETNEVNFREIPSHVLSKVCMY
FTYKVRYTNSSTEIPEFPIAPEIALELLMAANFLDC
Sequence of entity 3 (C), FASTA
>9DTX_3 von Hippel-Lindau disease tumor suppressor (chains C)
GMEAGRPRPVLRSVNSREPSQVIFCNRSPRVVLPVWLNFDGEPQPYPTLPPGTGRRIHSY
RGHLWLFRDAGTHDGLLVNQTELFVPSLNVDGQPIFANITLPVYTLKERCLQVVRSLVKP
ENYRRLDIVRSLYEDLEDHPNVQKDLERLTQERIAHQRMGD
Sequence of entity 4 (D), FASTA
>9DTX_4 Transcription activator BRG1 (chains D)
GGLNDIFEAQKIEWHEAEKLSPNPPNLTKKMKKIVDAVIKYKDSSSGRQLSEVFIQLPSR
KELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSI
VLQSVFTSVRQKIEKEDD

Ligands and cofactors

IDNameFormulaCopies
A1BB4(4R)-4-hydroxy-1-[(2R)-2-(3-{[(2S)-1-{(3R)-3-[(2M,6aS,11S)-2-(2-hydroxyphenyl)-…C47 H58 N10 O6 S1

Water and common crystallization additives (CL, EDO, GOL) are not listed.

Primary citation

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:

Browse structure collections

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