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Human enhancer of zeste (drosophila) homolog 2(EZH2)

Analyse Human enhancer of zeste (drosophila) homolog 2(EZH2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4MI0
Type: protein
Length: 208 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histone-lysine N-methyltransferase EZH2
EC: 2.1.1.43
UniProt: Q15910
Ligands: ZN, UNX
Pockets: 2 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 12% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histone-lysine N-methyltransferase EZH2 (EC 2.1.1.43)	protein	208	12% helix, 25% strand	Q15910

Ligands and binding sites

ZN · Zinc ion · metal · 6 copies · chains A
UNX · Unknown atom or ion · ion · 4 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	64	0.49	0.84	18	empty
2	101	0.45	0.79	23	empty

Compared structures

4MI0 · Human Enhancer of Zeste (Drosophila) Homolog 2(EZH2) · the same entry in another collection · chain A against A, TM-score 1.00
Q15910 · AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase EZH2 (Q15910) · a predicted model of the same protein · chain A against A, TM-score 0.86

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q15910
Elsewhere: RCSB PDB 4MI0 · PDBe 4MI0 · UniProt Q15910

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