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AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase EZH2 (Q61188)

Analyse AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase EZH2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: Q61188
Type: protein
Length: 746 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x5881B09f2D8e743400698633641fc1cD2Ed2BE6F
UniProt: Q61188

Structure

1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	746	—	Q61188

Compared structures

2QXV · Structural basis of EZH2 recognition by EED · an experimental structure of the same protein · chain A against B, TM-score 0.04
2QXV · Structural basis of EZH2 recognition by eed · an experimental structure of the same protein · chain A against B, TM-score 0.04

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 Q61188
Elsewhere: UniProt Q61188 · AlphaFold DB Q61188

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