› 2ybg

X-ray diffraction
1.9Å resolution

Structure of Lys120-acetylated p53 core domain

Released:
DOI: 10.2210/pdb2ybg/pdb
PDB entry 2ybg coloured by chain, front view.
PDB entry 2ybg coloured by chain, side view.
PDB entry 2ybg coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Acetylation of lysine 120 of p53 endows DNA-binding specificity at effective physiological salt concentration.
Arbely E, Natan E, Brandt T, Allen MD, Veprintsev DB, Robinson CV, Chin JW, Joerger AC, Fersht AR
Proc Natl Acad Sci U S A 108 8251-6 (2011)
PMID: 21525412

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138105 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cellular tumor antigen p53 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 200 amino acids
Theoretical weight: 22.55 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04637 (Residues: 94-293; Coverage: 51%)
Gene names: P53, TP53
Sequence domains: P53 DNA-binding domain
Structure domains: Immunoglobulin-like

Ligands and Environments

1 bound ligand:
Ligand ZN 4 x ZN
1 modified residue:
Ligand ALY 4 x ALY

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21
Unit cell:
a: 68.926Å b: 69.581Å c: 83.494Å
α: 90° β: 90.12° γ: 90°
R-values:
R R work R free
0.177 0.174 0.226
Expression system: Escherichia coli

Quick links

Citations

13 review citations

The multiple mechanisms that regulate p53 activity and cell fate.
Hafner et al. (2019)
12 more

3 mentions without citation

The structural and functional signatures of proteins that undergo multiple events of post-translational modification.
Pejaver et al. (2014)
2 more