Function and Biology Details
Reactions catalysed:
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine(9) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(9)
S-adenosyl-L-methionine + a [histone H3]-N(6),N(6)-dimethyl-L-lysine(9) = S-adenosyl-L-homocysteine + a [histone H3]-N(6),N(6),N(6)-trimethyl-L-lysine(9)
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:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129896 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-lysine N-methyltransferase, H3 lysine-9 specific
Molecule details ›
Chain: A
Length: 70 amino acids
Theoretical weight: 8.3 KDa
Source organism: Schizosaccharomyces pombe
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Chromo (CHRromatin Organisation MOdifier) domain
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Length: 70 amino acids
Theoretical weight: 8.3 KDa
Source organism: Schizosaccharomyces pombe
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
O60016 (Residues: 2-69; Coverage: 14%)
Sequence domains: Chromo (CHRromatin Organisation MOdifier) domain
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Refinement method:
molecular dynamics/simulated annealing torsion angle dynamics cartesian dynamics
Expression system: Escherichia coli BL21(DE3)
