Function and Biology Details
Reaction catalysed:
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139062 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Transcription initiation factor IIB
Molecule details ›
Chain: A
Length: 206 amino acids
Theoretical weight: 23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
Sequence domains: Transcription factor TFIIB repeat
Structure domains: Cyclin-like
Length: 206 amino acids
Theoretical weight: 23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
- Canonical:
Q00403 (Residues: 111-316; Coverage: 65%)
Sequence domains: Transcription factor TFIIB repeat
Structure domains: Cyclin-like
Tegument protein VP16
Molecule details ›
Chain: B
Length: 26 amino acids
Theoretical weight: 2.91 KDa
Source organism: Human alphaherpesvirus 1 strain 17
Expression system: Escherichia coli
UniProt:
Sequence domains: Herpes simplex virus virion protein 16 C terminal
Length: 26 amino acids
Theoretical weight: 2.91 KDa
Source organism: Human alphaherpesvirus 1 strain 17
Expression system: Escherichia coli
UniProt:
- Canonical: P06492 (Residues: 465-490; Coverage: 5%)
Sequence domains: Herpes simplex virus virion protein 16 C terminal
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Refinement method:
The model was calculated using HADDOCK
Expression systems:
- Escherichia coli BL21
- Escherichia coli
