Crystal structure of Eed in complex with a trimethylated histone H3K27 peptide. Determined by X-ray diffraction at 1.8 Å resolution. Released 15 Sept 2009.
Explore 3IIW in 3D Show helices and sheets RCSB PDB PDBe
3IIW 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 | 110-111 | 2 | |
| β-strand | 112-117 | 6 | 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 | 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 | 268-279 | 12 | |
| 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 | |
| α-helix | 399 | 1 | |
| 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 | 365 | Homo sapiens | O75530 (AlphaFold model) |
| Histone H3 peptide | B | protein | 11 |
>3IIW_1 Polycomb protein EED (chains A) KCKYSFKCVNSLKEDHNQPLFGVQFNWHSKEGDPLVFATVGSNRVTLYECHSQGEIRLLQ SYVDADADENFYTCAWTYDSNTSHPLLAVAGSRGIIRIINPITMQCIKHYVGHGNAINEL KFHPRDPNLLLSVSKDHALRLWNIQTDTLVAIFGGVEGHRDEVLSADYDLLGEKIMSCGM DHSLKLWRINSKRMMNAIKESYDYNPNKTNRPFISQKIHFPDFSTRDIHRNYVDCVRWLG DLILSKSCENAIVCWKPGKMEDDIDKIKPSESNVTILGRFDYSQCDIWYMRFSMDFWQKM LALGNQVGKLYVWDLEVEDPHKAKCTTLTHHKCGAAIRQTSFSRDSSILIAVCDDASIWR WDRLR
>3IIW_2 Histone H3 peptide (chains B) TKAARKSAPAT
Role of the polycomb protein EED in the propagation of repressive histone marks. Margueron, R., Justin, N., Ohno, K. et al. Nature (2009) 461:762-767. DOI 10.1038/nature08398 · 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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