4MI0: Histone-lysine N-methyltransferase EZH2

Name: PDB 4MI0: Human Enhancer of Zeste (Drosophila) Homolog 2(EZH2)
Published: 2013-09-25
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: transferase

Human Enhancer of Zeste (Drosophila) Homolog 2(EZH2). Determined by X-ray diffraction at 2.0 Å resolution. Released 25 Sept 2013.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 1
Atoms: 1,661
Mol. weight: 27.1 kDa
Ligands: ZN
Released: 25 Sept 2013

Explore 4MI0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4MI0 contains 7 α-helices and 18 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: 7 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	535-538	4
β-strand	543	1	1
β-strand	556	1	1
β-strand	565	1	2
α-helix	572-575	4
β-strand	578	1	3
β-strand	601	1	2
α-helix	605-608	4
β-strand	614-618	5	4
β-strand	624-628	5	4
β-strand	632	1	5
β-strand	637-640	4	3
β-strand	644-647	4	6
α-helix	648-656	9
β-strand	666-668	3	6
β-strand	673-676	4	6
α-helix	683-686	4
β-strand	688-689	2	7
β-strand	695-702	8	3
β-strand	705-712	8	3
β-strand	716	1	5
α-helix	720	1
β-strand	721	1	4
α-helix	722	1
β-strand	723-724	2	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Histone-lysine N-methyltransferase EZH2	A	protein	233	Homo sapiens	Q15910 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4MI0_1 Histone-lysine N-methyltransferase EZH2 (chains A)
YQPCDHPRQPCDSSCPCVIAQNFCEKFCQCSSECQNRFPGCRCKAQCNTKQCPCYLAVRE
CDPDLCLTCGAADHWDSKNVSCKNCSIQRGSKKHLLLAPSDVAGWGIFIKDPVQKNEFIS
EYCGEIISQDEADRRGKVYDKYMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKV
MMVNGDHRIGIFAKRAIQTGEELFFDYRYSQADALKYVGIEREMEIPHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	6

Water and common crystallization additives (UNX) are not listed.

Primary citation

Structure of the catalytic domain of EZH2 reveals conformational plasticity in cofactor and substrate binding sites and explains oncogenic mutations. Wu, H., Zeng, H., Dong, A. et al. PLoS One (2013) 8:e83737-e83737. DOI 10.1371/journal.pone.0083737 · 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…
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
5H17 2.3 Å, EED in complex with PRC2 allosteric inhibitor EED210

Browse structure collections

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