Co-crystal structure of Compound 1 in complex with the bromodomain of human SMARCA4 and pVHL:ElonginC:ElonginB. Determined by X-ray diffraction at 3.73 Å resolution. Released 26 Jul 2023.
Explore 8G1Q in 3D Show helices and sheets RCSB PDB PDBe
8G1Q contains 20 α-helices and 24 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 | 12-19 | 8 | 1 |
| α-helix | 29-35 | 7 | |
| β-strand | 45 | 1 | 1 |
| β-strand | 50 | 1 | 1 |
| α-helix | 57-60 | 4 | |
| β-strand | 68 | 1 | 2 |
| β-strand | 71 | 1 | 2 |
| α-helix | 72 | 1 | |
| β-strand | 73-76 | 4 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 18 | 1 | 3 |
| β-strand | 29-30 | 2 | 1 |
| β-strand | 32 | 1 | 3 |
| α-helix | 33-36 | 4 | |
| α-helix | 41-43 | 3 | |
| α-helix | 69-83 | 15 | |
| α-helix | 90-94 | 5 | |
| α-helix | 97-99 | 3 | |
| α-helix | 100-108 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 71-78 | 8 | 4 |
| β-strand | 84 | 1 | 5 |
| β-strand | 87-89 | 3 | 6 |
| β-strand | 95-97 | 3 | 6 |
| β-strand | 101 | 1 | 5 |
| β-strand | 106-112 | 7 | 4 |
| β-strand | 117-118 | 2 | 6 |
| β-strand | 120 | 1 | 7 |
| β-strand | 121 | 1 | 5 |
| β-strand | 127 | 1 | 7 |
| β-strand | 129-130 | 2 | 4 |
| β-strand | 133 | 1 | 4 |
| β-strand | 136 | 1 | 6 |
| α-helix | 145-146 | 2 | |
| β-strand | 147-152 | 6 | 4 |
| α-helix | 158-167 | 10 | |
| α-helix | 172-177 | 6 | |
| α-helix | 182-189 | 8 | |
| α-helix | 194-202 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1458-1470 | 13 | |
| 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 |
|---|---|---|---|---|---|
| Transcription activator BRG1 | H | protein | 124 | Homo sapiens | P51532 (AlphaFold model) |
| 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 | 162 | Homo sapiens | P40337 (AlphaFold model) |
>8G1Q_1 Transcription activator BRG1 (chains H) SPAEKLSPNPPNLTKKMKKIVDAVIKYKDSSSGRQLSEVFIQLPSRKELPEYYELIRKPV DFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTSVRQKIE KEDD
>8G1Q_2 Elongin-B (chains A) MDVFLMIRRHKTTIFTDAKESSTVFELKRIVEGILKRPPDEQRLYKDDQLLDDGKTLGEC GFTSQTARPQAPATVGLAFRADDTFEALCIEPFSSPPELPDVMK
>8G1Q_3 Elongin-C (chains B) MYVKLISSDGHEFIVKREHALTSGTIKAMLSGPGQFAENETNEVNFREIPSHVLSKVCMY FTYKVRYTNSSTEIPEFPIAPEIALELLMAANFLDC
>8G1Q_4 von Hippel-Lindau disease tumor suppressor (chains C) GSMEAGRPRPVLRSVNSREPSQVIFCNRSPRVVLPVWLNFDGEPQPYPTLPPGTGRRIHS YRGHLWLFRDAGTHDGLLVNQTELFVPSLNVDGQPIFANITLPVYTLKERCLQVVRSLVK PENYRRLDIVRSLYEDLEDHPNVQKDLERLTQERIAHQRMGD
| ID | Name | Formula | Copies |
|---|---|---|---|
| YHB | N-(2-{4-[(6M)-3-amino-6-(2-hydroxyphenyl)pyridazin-4-yl]piperazin-1-yl}pyridine… | C43 H50 N10 O5 S | 1 |
Water and common crystallization additives (PEG, NA) are not listed.
Affinity and cooperativity modulate ternary complex formation to drive targeted protein degradation. Wurz, R.P., Rui, H., Dellamaggiore, K. et al. Nat Commun (2023) 14:4177-4177. DOI 10.1038/s41467-023-39904-5 · PubMed
Other PDB entries of the same protein (UniProt P51532 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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