Function and Biology Details
Reaction catalysed:
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine(36) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(36)
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure analysis Details
Assemblies composition:
Assembly name:
Histone-lysine N-methyltransferase SETMAR (preferred)
PDBe Complex ID:
PDB-CPX-176100 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-lysine N-methyltransferase SETMAR
Molecule details ›
Chains: A, B
Length: 239 amino acids
Theoretical weight: 28.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Transposase (partial DDE domain)
Structure domains: Ribonuclease H-like superfamily/Ribonuclease H
Length: 239 amino acids
Theoretical weight: 28.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
Q53H47 (Residues: 446-684; Coverage: 35%)
Sequence domains: Transposase (partial DDE domain)
Structure domains: Ribonuclease H-like superfamily/Ribonuclease H
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
APS BEAMLINE 19-ID
Spacegroup:
P6122
Expression system: Escherichia coli
