PDBe 2k8f

Solution NMR

Structural Basis for the Regulation of p53 Function by p300

Released:

Function and Biology Details

Reaction catalysed:
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Histone acetyltransferase p300 Chain: A
Molecule details ›
Chain: A
Length: 90 amino acids
Theoretical weight: 9.96 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q09472 (Residues: 1723-1812; Coverage: 4%)
Gene names: EP300, P300
Sequence domains: TAZ zinc finger
Structure domains: TAZ domain
Cellular tumor antigen p53 Chain: B
Molecule details ›
Chain: B
Length: 39 amino acids
Theoretical weight: 4.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04637 (Residues: 1-39; Coverage: 10%)
Gene names: P53, TP53
Sequence domains: P53 transactivation motif

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 80%
Refinement method: DGSA-distance geometry simulated annealing, molecular dynamics, torsion angle dynamics
Chemical shifts: BMR15944  
Expression system: Escherichia coli