3K27: Complex structure of EED and trimethylated H3K9

Complex structure of EED and trimethylated H3K9. Determined by X-ray diffraction at 1.76 Å resolution. Released 15 Dec 2009.

Method: X-ray diffraction
Resolution: 1.76 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,354
Mol. weight: 43.32 kDa
Released: 15 Dec 2009

Explore 3K27 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3K27 contains 8 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.

Chain A: 8 helices, 29 β-strands

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
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

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Polycomb protein EED	A	protein	366	Homo sapiens	O75530 (AlphaFold model)
Histone peptide	B	protein	9

Sequence of entity 1 (A), FASTA

>3K27_1 Polycomb protein EED (chains A)
KKCKYSFKCVNSLKEDHNQPLFGVQFNWHSKEGDPLVFATVGSNRVTLYECHSQGEIRLL
QSYVDADADENFYTCAWTYDSNTSHPLLAVAGSRGIIRIINPITMQCIKHYVGHGNAINE
LKFHPRDPNLLLSVSKDHALRLWNIQTDTLVAIFGGVEGHRDEVLSADYDLLGEKIMSCG
MDHSLKLWRINSKRMMNAIKESYDYNPNKTNRPFISQKIHFPDFSTRDIHRNYVDCVRWL
GDLILSKSCENAIVCWKPGKMEDDIDKIKPSESNVTILGRFDYSQCDIWYMRFSMDFWQK
MLALGNQVGKLYVWDLEVEDPHKAKCTTLTHHKCGAAIRQTSFSRDSSILIAVCDDASIW
RWDRLR

Sequence of entity 2 (B), FASTA

>3K27_2 HISTONE PEPTIDE (chains B)
KQTARKSTG

Primary citation

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:

5U69 1.28 Å, Polycomb protein EED in complex with inhibitor: (3R,4S)-1-[(2-methoxyphenyl)methyl]-N,N-d…
5U8F 1.34 Å, Polycomb protein EED in complex with inhibitor: (3R,4S)-1-[(1S)-7-fluoro-2,3-dihydro-1H-i…
5U8A 1.45 Å, Polycomb protein EED in complex with inhibitor: (3R,4S)-1-[(2-bromo-6-fluorophenyl)methyl…
6SFB 1.52 Å, EED in complex with a triazolopyrimidine
3K26 1.58 Å, Complex structure of EED and trimethylated H3K4
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)
7P3C 1.61 Å, EED in complex with compound 4
6V3Y 1.63 Å, Crystal structure of EED in complex with PALI1-K1219me3 peptide
5U6D 1.64 Å, Polycomb protein EED in complex with inhibitor: 2-[4-(4-{(3S,4R)-4-(dimethylamino)-1-[(2-…
6V3X 1.7 Å, Crystal structure of EED in complex with PALI1-K1241me3 peptide
5TTW 1.74 Å, Crystal Structure of EED in Complex with UNC4859

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