Complex structure of EED and trimethylated H3K4. Determined by X-ray diffraction at 1.58 Å resolution. Released 15 Dec 2009.
Explore 3K26 in 3D Show helices and sheets RCSB PDB PDBe
3K26 contains 9 α-helices and 29 β-strands across 1 chain. 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 | 83-89 | 7 | 1 |
| β-strand | 96-101 | 6 | 2 |
| α-helix | 105-106 | 2 | |
| α-helix | 110 | 1 | |
| β-strand | 111-117 | 7 | 2 |
| β-strand | 120-126 | 7 | 2 |
| α-helix | 128-130 | 3 | |
| β-strand | 132-139 | 8 | 2 |
| β-strand | 147-154 | 8 | 3 |
| β-strand | 161-167 | 7 | 3 |
| β-strand | 171-175 | 5 | 3 |
| β-strand | 182-187 | 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 | 268-278 | 11 | |
| α-helix | 282-284 | 3 | |
| α-helix | 288-291 | 4 | |
| 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 |
| α-helix | 340-342 | 3 | |
| β-strand | 350-357 | 8 | 6 |
| β-strand | 369-370 | 2 | 7 |
| β-strand | 376-380 | 5 | 7 |
| β-strand | 386-390 | 5 | 7 |
| α-helix | 396-398 | 3 | |
| β-strand | 400-404 | 5 | 7 |
| α-helix | 412 | 1 | |
| β-strand | 413-418 | 6 | 1 |
| β-strand | 424-429 | 6 | 1 |
| β-strand | 433-438 | 6 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Polycomb protein EED | A | protein | 366 | Homo sapiens | O75530 (AlphaFold model) |
| Histone peptide | B | protein | 12 |
>3K26_1 Polycomb protein EED (chains A) KKCKYSFKCVNSLKEDHNQPLFGVQFNWHSKEGDPLVFATVGSNRVTLYECHSQGEIRLL QSYVDADADENFYTCAWTYDSNTSHPLLAVAGSRGIIRIINPITMQCIKHYVGHGNAINE LKFHPRDPNLLLSVSKDHALRLWNIQTDTLVAIFGGVEGHRDEVLSADYDLLGEKIMSCG MDHSLKLWRINSKRMMNAIKESYDYNPNKTNRPFISQKIHFPDFSTRDIHRNYVDCVRWL GDLILSKSCENAIVCWKPGKMEDDIDKIKPSESNVTILGRFDYSQCDIWYMRFSMDFWQK MLALGNQVGKLYVWDLEVEDPHKAKCTTLTHHKCGAAIRQTSFSRDSSILIAVCDDASIW RWDRLR
>3K26_2 HISTONE PEPTIDE (chains B) ARTKKQTARKST
Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Xu, C., Bian, C., Yang, W. et al. Proc Natl Acad Sci U S A (2010) 107:19266-19271. DOI 10.1073/pnas.1008937107 · 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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