Function and Biology Details
Reaction catalysed:
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
Biochemical function:
- not assigned
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero hexamer (preferred)
Assembly name:
SMAD2 homotrimer and CREB-binding protein (preferred)
PDBe Complex ID:
PDB-CPX-172407 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Mothers against decapentaplegic homolog 2
Molecule details ›
Chains: A, C, E
Length: 208 amino acids
Theoretical weight: 23.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: MH2 domain
Length: 208 amino acids
Theoretical weight: 23.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
Q15796 (Residues: 262-464; Coverage: 44%)
Sequence domains: MH2 domain
CREB-binding protein
Molecule details ›
Chains: B, D, F
Length: 28 amino acids
Theoretical weight: 3.12 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Length: 28 amino acids
Theoretical weight: 3.12 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: Q92793 (Residues: 1951-1973; Coverage: 1%)
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
PHOTON FACTORY BEAMLINE AR-NE3A
Spacegroup:
P212121
Expression system: Escherichia coli
