Function and Biology Details
Reaction catalysed:
S-adenosyl-L-methionine + a [histone H3]-L-lysine(9) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(9)
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Histone-lysine N-methyltransferase EHMT1 (preferred)
PDBe Complex ID:
PDB-CPX-190698 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-lysine N-methyltransferase EHMT1
Molecule details ›
Chains: A, B
Length: 237 amino acids
Theoretical weight: 26.18 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Ankyrin repeats (3 copies)
Structure domains: Ankyrin repeat-containing domain
Length: 237 amino acids
Theoretical weight: 26.18 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
Q9H9B1 (Residues: 765-999; Coverage: 18%)
Sequence domains: Ankyrin repeats (3 copies)
Structure domains: Ankyrin repeat-containing domain
