PDBe 2vuk

X-ray diffraction
1.5Å resolution

STRUCTURE OF THE P53 CORE DOMAIN MUTANT Y220C BOUND TO THE STABILIZING SMALL-MOLECULE DRUG PHIKAN083

Released:
Source organism: Homo sapiens
Primary publication:
Targeted rescue of a destabilized mutant of p53 by an in silico screened drug.
Proc. Natl. Acad. Sci. U.S.A. 105 10360-5 (2008)
PMID: 18650397

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cellular tumor antigen p53 Chains: A, B
Molecule details ›
Chains: A, B
Length: 219 amino acids
Theoretical weight: 24.53 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P04637 (Residues: 94-312; Coverage: 56%)
Gene names: P53, TP53
Sequence domains: P53 DNA-binding domain
Structure domains: Immunoglobulin-like

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P212121
Unit cell:
a: 65.093Å b: 71.234Å c: 105.207Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.186 0.208
Expression system: Escherichia coli BL21