› 5ccm

X-ray diffraction
2.3Å resolution

Function and Biology Details

Reaction catalysed: 
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine(4) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(4)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190659 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-lysine N-methyltransferase SMYD3 Chain: A
Molecule details ›
Chain: A
Length: 428 amino acids
Theoretical weight: 49.15 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9H7B4 (Residues: 1-428; Coverage: 100%)
Gene names: SMYD3, ZMYND1, ZNFN3A1
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand ZN 3 x ZN
Ligand SAM 1 x SAM
Ligand 4ZX 1 x 4ZX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 60.484Å b: 65.852Å c: 107.358Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.2 0.255
Expression system: Escherichia coli

Quick links

Citations

19 review citations

Epigenetics and beyond: targeting writers of protein lysine methylation to treat disease.
Bhat et al. (2021)
18 more

8 mentions without citation

Inhibitors of Protein Methyltransferases and Demethylases.
Kaniskan et al. (2018)
7 more