Function and Biology Details
Reactions catalysed:
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine(4) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(4)
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine(27) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(27)
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130140 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Bromodomain-containing protein 4
Molecule details ›
Chain: A
Length: 83 amino acids
Theoretical weight: 9.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Bromodomain extra-terminal - transcription regulation
Structure domains: Substrate Binding Domain Of Dnak; Chain:A; Domain 2
Length: 83 amino acids
Theoretical weight: 9.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
O60885 (Residues: 601-683; Coverage: 6%)
Sequence domains: Bromodomain extra-terminal - transcription regulation
Structure domains: Substrate Binding Domain Of Dnak; Chain:A; Domain 2
Histone-lysine N-methyltransferase NSD3
Molecule details ›
Chain: B
Length: 12 amino acids
Theoretical weight: 1.43 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
Length: 12 amino acids
Theoretical weight: 1.43 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
- Canonical: Q9BZ95 (Residues: 152-163; Coverage: 1%)
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Chemical shift assignment:
83%
Refinement method:
torsion angle dynamics, simulated annealing
Expression systems:
- Escherichia coli
- Not provided
