Function and Biology Details
Reaction catalysed:
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)
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Histone-lysine N-methyltransferase SUVR4 (preferred)
PDBe Complex ID:
PDB-CPX-186667 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-lysine N-methyltransferase SUVR4
Molecule details ›
Chain: A
Length: 109 amino acids
Theoretical weight: 12.16 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
Sequence domains: Ubiquitin-binding WIYLD domain
Structure domains: Histone-lysine N methyltransferase , C-terminal domain-like
Length: 109 amino acids
Theoretical weight: 12.16 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
- Canonical:
Q8W595 (Residues: 1-89; Coverage: 18%)
Sequence domains: Ubiquitin-binding WIYLD domain
Structure domains: Histone-lysine N methyltransferase , C-terminal domain-like
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Chemical shift assignment:
95%
Refinement method:
torsion angle dynamics
Expression system: Escherichia coli
