EED in complex with PRC2 allosteric inhibitor compound 22 (MAK683). Determined by X-ray diffraction at 1.6 Å resolution. Released 13 Apr 2022.
Explore 7QK4 in 3D Show helices and sheets RCSB PDB PDBe
7QK4 contains 6 α-helices and 29 β-strands across 2 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 | 82-89 | 8 | 1 |
| α-helix | 94-96 | 3 | |
| β-strand | 98-101 | 4 | 2 |
| α-helix | 106 | 1 | |
| α-helix | 110 | 1 | |
| β-strand | 111-117 | 7 | 2 |
| β-strand | 120-126 | 7 | 2 |
| β-strand | 132-139 | 8 | 2 |
| β-strand | 147-154 | 8 | 3 |
| β-strand | 161-167 | 7 | 3 |
| β-strand | 172-176 | 5 | 3 |
| β-strand | 181-186 | 6 | 3 |
| β-strand | 193-198 | 6 | 4 |
| β-strand | 205-210 | 6 | 4 |
| β-strand | 215-219 | 5 | 4 |
| β-strand | 224-229 | 6 | 4 |
| β-strand | 239-244 | 6 | 5 |
| β-strand | 250-255 | 6 | 5 |
| β-strand | 260-264 | 5 | 5 |
| α-helix | 268-279 | 12 | |
| β-strand | 292-294 | 3 | 4 |
| β-strand | 299-301 | 3 | 5 |
| β-strand | 311-315 | 5 | 6 |
| β-strand | 318-322 | 5 | 6 |
| β-strand | 327-333 | 7 | 6 |
| β-strand | 350-357 | 8 | 6 |
| β-strand | 368-370 | 3 | 7 |
| β-strand | 376-380 | 5 | 7 |
| β-strand | 386-390 | 5 | 7 |
| β-strand | 402-404 | 3 | 7 |
| β-strand | 413-418 | 6 | 1 |
| β-strand | 424-429 | 6 | 1 |
| β-strand | 433-439 | 7 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 41-62 | 22 | |
| α-helix | 65-67 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Polycomb protein EED | A | protein | 366 | Homo sapiens | O75530 (AlphaFold model) |
| Histone-lysine N-methyltransferase EZH2 | B | protein | 29 | Homo sapiens | Q15910 (AlphaFold model) |
>7QK4_1 Polycomb protein EED (chains A) GKCKYSFKCVNSLKEDHNQPLFGVQFNWHSKEGDPLVFATVGSNRVTLYECHSQGEIRLL QSYVDADADENFYTCAWTYDSNTSHPLLAVAGSRGIIRIINPITMQCIKHYVGHGNAINE LKFHPRDPNLLLSVSKDHALRLWNIQTDTLVAIFGGVEGHRDEVLSADYDLLGEKIMSCG MDHSLKLWRINSKRMMNAIKESYDYNPNKTNRPFISQKIHFPDFSTRDIHRNYVDCVRWL GDLILSKSCENAIVCWKPGKMEDDIDKIKPSESNVTILGRFDYSQCDIWYMRFSMDFWQK MLALGNQVGKLYVWDLEVEDPHKAKCTTLTHHKCGAAIRQTSFSRDSSILIAVCDDASIW RWDRLR
>7QK4_2 Histone-lysine N-methyltransferase EZH2 (chains B) SMFSSNRQKILERTEILNQEWKQRRIQPV
| ID | Name | Formula | Copies |
|---|---|---|---|
| EJR | N-[(5-fluoranyl-2,3-dihydro-1-benzofuran-4-yl)methyl]-8-(2-methylpyridin-3-yl)-… | C20 H17 F N6 O | 1 |
Water and common crystallization additives (CL) are not listed.
Discovery of the Clinical Candidate MAK683: An EED-Directed, Allosteric, and Selective PRC2 Inhibitor for the Treatment of Advanced Malignancies. Huang, Y., Sendzik, M., Zhang, J. et al. J Med Chem (2022) 65:5317-5333. DOI 10.1021/acs.jmedchem.1c02148 · PubMed
Other PDB entries of the same protein (UniProt O75530 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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