Research workbench

Crystal structure of EHMT1

Analyse Crystal structure of EHMT1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6BY9
Type: protein
Length: 268 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histone-lysine N-methyltransferase EHMT1
EC: 2.1.1.-, 2.1.1.43
UniProt: Q9H9B1
Ligands: UNX

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histone-lysine N-methyltransferase EHMT1 (EC 2.1.1.-, 2.1.1.43)	protein	268	51% helix, 1% strand	Q9H9B1

Ligands and binding sites

UNX · Unknown atom or ion · ion · 2 copies · chains A

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

Compared structures

6BY9 · Crystal structure of EHMT1 · the same entry in another collection · chain A against A, TM-score 1.00
Q9H9B1 · AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase EHMT1 (Q9H9B1) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q9H9B1
Elsewhere: RCSB PDB 6BY9 · PDBe 6BY9 · UniProt Q9H9B1

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.