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Crystal structure of the EZH2 set domain

Analyse Crystal structure of the EZH2 set domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4MI5
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, SO4
Pockets: 3 · best druggability 0.47

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
SO4 · Sulfate ion · ion · chains A

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

Pockets

3 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	148	0.47	0.77	25	empty
2	66	0.45	0.83	21	empty
3	88	0.43	0.79	23	empty

Compared structures

4MI5 · Crystal structure of the EZH2 SET domain · 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 0.84

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 4MI5 · PDBe 4MI5 · UniProt Q15910

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