6U4Y: EZH2-EED Complex in an Oligomeric State
Crystal Structure of an EZH2-EED Complex in an Oligomeric State. Determined by X-ray diffraction at 2.91 Å resolution. Released 8 Jul 2020.
- Method
- X-ray diffraction
- Resolution
- 2.91 Å
- Organism
- Homo sapiens
- Chains
- 6
- Atoms
- 12,736
- Mol. weight
- 203.66 kDa
- Released
- 8 Jul 2020
Explore 6U4Y in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6U4Y contains 48 α-helices and 102 β-strands across 6 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, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 13-60 | 48 | |
| α-helix | 65-68 | 4 | |
| β-strand | 82-87 | 6 | 1 |
| α-helix | 92-93 | 2 | |
| β-strand | 94-97 | 4 | 1 |
| β-strand | 99-101 | 3 | 2 |
| α-helix | 102-103 | 2 | |
| α-helix | 144-151 | 8 | |
| α-helix | 168-179 | 12 | |
| α-helix | 222-230 | 9 | |
| α-helix | 232-234 | 3 | |
| α-helix | 239-248 | 10 | |
Chain B: 9 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 13-60 | 48 | |
| β-strand | 65 | 1 | 3 |
| α-helix | 66-68 | 3 | |
| β-strand | 82-87 | 6 | 4 |
| α-helix | 91-93 | 3 | |
| β-strand | 94-97 | 4 | 4 |
| β-strand | 99-101 | 3 | 5 |
| α-helix | 102-107 | 6 | |
| β-strand | 112-113 | 2 | 6 |
| β-strand | 118-119 | 2 | 6 |
| α-helix | 144-151 | 8 | |
| α-helix | 168-178 | 11 | |
| α-helix | 221-230 | 10 | |
| α-helix | 232-234 | 3 | |
| α-helix | 237-247 | 11 | |
Chain C: 9 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 18-61 | 44 | |
| α-helix | 65-68 | 4 | |
| β-strand | 82-87 | 6 | 7 |
| α-helix | 92-93 | 2 | |
| β-strand | 94-97 | 4 | 7 |
| β-strand | 99-101 | 3 | 8 |
| α-helix | 102-107 | 6 | |
| α-helix | 145-151 | 7 | |
| α-helix | 168-178 | 11 | |
| α-helix | 221-230 | 10 | |
| α-helix | 232-234 | 3 | |
| α-helix | 237-248 | 12 | |
Chain D: 6 helices, 29 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 82-90 | 9 | 1 |
| β-strand | 96-101 | 6 | 2 |
| α-helix | 106 | 1 | |
| α-helix | 110-111 | 2 | |
| β-strand | 112-117 | 6 | 2 |
| β-strand | 120-126 | 7 | 2 |
| α-helix | 128-130 | 3 | |
| β-strand | 132-140 | 9 | 2 |
| β-strand | 147-154 | 8 | 9 |
| β-strand | 161-167 | 7 | 9 |
| β-strand | 172-176 | 5 | 9 |
| β-strand | 181-186 | 6 | 9 |
| β-strand | 193-198 | 6 | 10 |
| β-strand | 205-210 | 6 | 10 |
| β-strand | 215-219 | 5 | 10 |
| β-strand | 224-229 | 6 | 10 |
| β-strand | 239-244 | 6 | 11 |
| β-strand | 250-255 | 6 | 11 |
| β-strand | 260-264 | 5 | 11 |
| α-helix | 268-278 | 11 | |
| β-strand | 292-294 | 3 | 10 |
| β-strand | 299-301 | 3 | 11 |
| β-strand | 311-315 | 5 | 12 |
| β-strand | 318-322 | 5 | 12 |
| β-strand | 327-333 | 7 | 12 |
| α-helix | 340-342 | 3 | |
| β-strand | 350-357 | 8 | 12 |
| β-strand | 369-370 | 2 | 13 |
| β-strand | 376-380 | 5 | 13 |
| β-strand | 386-390 | 5 | 13 |
| α-helix | 396-398 | 3 | |
| β-strand | 402-404 | 3 | 13 |
| β-strand | 413-418 | 6 | 1 |
| β-strand | 424-429 | 6 | 1 |
| β-strand | 433-439 | 7 | 1 |
Chain E: 9 helices, 30 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 82-90 | 9 | 4 |
| β-strand | 96-101 | 6 | 5 |
| β-strand | 105 | 1 | 3 |
| α-helix | 106 | 1 | |
| α-helix | 110-111 | 2 | |
| β-strand | 112-117 | 6 | 5 |
| β-strand | 120-126 | 7 | 5 |
| α-helix | 128-130 | 3 | |
| β-strand | 132-140 | 9 | 5 |
| β-strand | 147-154 | 8 | 14 |
| β-strand | 161-167 | 7 | 14 |
| β-strand | 171-176 | 6 | 14 |
| β-strand | 181-187 | 7 | 14 |
| β-strand | 193-198 | 6 | 15 |
| β-strand | 205-210 | 6 | 15 |
| β-strand | 215-219 | 5 | 15 |
| β-strand | 224-229 | 6 | 15 |
| β-strand | 239-244 | 6 | 16 |
| β-strand | 250-255 | 6 | 16 |
| β-strand | 260-264 | 5 | 16 |
| α-helix | 268-278 | 11 | |
| α-helix | 290-291 | 2 | |
| β-strand | 292-294 | 3 | 15 |
| β-strand | 299-301 | 3 | 16 |
| β-strand | 311-315 | 5 | 17 |
| β-strand | 318-322 | 5 | 17 |
| β-strand | 327-333 | 7 | 17 |
| α-helix | 340-342 | 3 | |
| β-strand | 350-357 | 8 | 17 |
| β-strand | 369-370 | 2 | 18 |
| β-strand | 376-380 | 5 | 18 |
| β-strand | 386-390 | 5 | 18 |
| α-helix | 396-398 | 3 | |
| α-helix | 400-401 | 2 | |
| β-strand | 402-404 | 3 | 18 |
| α-helix | 412 | 1 | |
| β-strand | 413-418 | 6 | 4 |
| β-strand | 424-429 | 6 | 4 |
| β-strand | 433-439 | 7 | 4 |
Chain F: 6 helices, 31 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 82-90 | 9 | 7 |
| β-strand | 96-101 | 6 | 8 |
| α-helix | 105-106 | 2 | |
| β-strand | 107 | 1 | 19 |
| β-strand | 109 | 1 | 19 |
| α-helix | 110-111 | 2 | |
| β-strand | 112-117 | 6 | 8 |
| β-strand | 120-126 | 7 | 8 |
| α-helix | 128-130 | 3 | |
| β-strand | 132-140 | 9 | 8 |
| β-strand | 147-155 | 9 | 20 |
| β-strand | 160-167 | 8 | 20 |
| β-strand | 172-176 | 5 | 20 |
| β-strand | 181-186 | 6 | 20 |
| β-strand | 193-198 | 6 | 21 |
| β-strand | 205-210 | 6 | 21 |
| β-strand | 215-219 | 5 | 21 |
| β-strand | 224-229 | 6 | 21 |
| β-strand | 239-244 | 6 | 22 |
| β-strand | 250-255 | 6 | 22 |
| β-strand | 260-264 | 5 | 22 |
| α-helix | 268-279 | 12 | |
| β-strand | 292-294 | 3 | 21 |
| β-strand | 299-301 | 3 | 22 |
| β-strand | 311-315 | 5 | 23 |
| β-strand | 318-323 | 6 | 23 |
| β-strand | 327-333 | 7 | 23 |
| α-helix | 340-342 | 3 | |
| β-strand | 350-357 | 8 | 23 |
| β-strand | 369-370 | 2 | 24 |
| β-strand | 376-380 | 5 | 24 |
| β-strand | 386-390 | 5 | 24 |
| α-helix | 396-398 | 3 | |
| β-strand | 402-404 | 3 | 24 |
| β-strand | 413-418 | 6 | 7 |
| β-strand | 424-429 | 6 | 7 |
| β-strand | 433-439 | 7 | 7 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Histone-lysine N-methyltransferase EZH2 | A, B, C | protein | 224 | Homo sapiens | Q15910 (AlphaFold model) |
| Polycomb protein EED | D, E, F | protein | 366 | Homo sapiens | O75530 (AlphaFold model) |
Sequence of entity 1 (A, B, C), FASTA
>6U4Y_1 Histone-lysine N-methyltransferase EZH2 (chains A, B, C)
SGQTGKKSEKGPVCWRKRVKSEYMRLRQLKRFRRADEVKSMFSSNRQKILERTEILNQEW
KQRRIQPVHILSSVSSLRGTRECSVTSDLDFPTQVIPLKTLNAVASVPIMYSWSPLQQNF
MVEDETVLHNIPYMGDEVLDQDGTFIEELIKNYDGKVHGDRECGFINDEIFVELVNALGQ
YNGSSGSDKIFEAISSMFPDKGTAEELKEKYKELTEQQLPGALP
Sequence of entity 2 (D, E, F), FASTA
>6U4Y_2 Polycomb protein EED (chains D, E, F)
GSCKYSFKCVNSLKEDHNQPLFGVQFNWHSKEGDPLVFATVGSNRVTLYECHSQGEIRLL
QSYVDADADENFYTCAWTYDSNTSHPLLAVAGSRGIIRIINPITMQCIKHYVGHGNAINE
LKFHPRDPNLLLSVSKDHALRLWNIQTDTLVAIFGGVEGHRDEVLSADYDLLGEKIMSCG
MDHSLKLWRINSKRMMNAIKESYDYNPNKTNRPFISQKIHFPDFSTRDIHRNYVDCVRWL
GDLILSKSCENAIVCWKPGKMEDDIDKIKPSESNVTILGRFDYSQCDIWYMRFSMDFWQK
MLALGNQVGKLYVWDLEVEDPHKAKCTTLTHHKCGAAIRQTSFSRDSSILIAVCDDASIW
RWDRLR
Primary citation
A partially disordered region connects gene repression and activation functions of EZH2. Jiao, L., Shubbar, M., Yang, X. et al. Proc Natl Acad Sci U S A (2020) 117:16992-17002. DOI 10.1073/pnas.1914866117 · PubMed
Other PDB entries of the same protein (UniProt Q15910 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 5U5T 1.6 Å, Crystal structure of EED in complex with H3K27Me3 peptide and…
- 7QK4 1.6 Å, EED in complex with PRC2 allosteric inhibitor compound 22 (MAK683)
- 7QJG 1.8 Å, EED in complex with PRC2 allosteric inhibitor compound 6
- 7QJU 1.8 Å, EED in complex with PRC2 allosteric inhibitor compound 7
- 5H14 1.9 Å, EED in complex with an allosteric PRC2 inhibitor EED666
- 5H19 1.9 Å, EED in complex with PRC2 allosteric inhibitor EED162
- 5U62 1.9 Å, Crystal structure of EED in complex with H3K27Me3 peptide and…
- 4MI0 2.0 Å, Human Enhancer of Zeste (Drosophila) Homolog 2(EZH2)
- 4MI5 2.0 Å, Crystal structure of the EZH2 SET domain
- 5WUK 2.03 Å, Crystal structure of EED [G255D] in complex with EZH2 peptide and EED226 compound
- 6LO2 2.21 Å, Crystal structure of EED in complex with EZH2 peptide and compound 11#
- 5H15 2.27 Å, EED in complex with PRC2 allosteric inhibitor EED709
Browse structure collections
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