Function and Biology Details
Reaction catalysed:
(1a) a [histone H3]-N(6),N(6),N(6)-trimethyl-L-lysine(9) + 2-oxoglutarate + O(2) = a [histone H3]-N(6),N(6)-dimethyl-L-lysine(9) + succinate + formaldehyde + CO(2)
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Lysine-specific demethylase 4B (preferred)
PDBe Complex ID:
PDB-CPX-131802 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysine-specific demethylase 4B
Molecule details ›
Chains: A, B
Length: 119 amino acids
Theoretical weight: 13.37 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Jumonji domain-containing protein 2A Tudor domain
Structure domains:
Length: 119 amino acids
Theoretical weight: 13.37 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
O94953 (Residues: 917-1031; Coverage: 11%)
Sequence domains: Jumonji domain-containing protein 2A Tudor domain
Structure domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
APS BEAMLINE 21-ID-F
Spacegroup:
P31
Expression system: Escherichia coli
