PDBe 3d08

X-ray diffraction
1.4Å resolution

Human p53 core domain with hot spot mutation R249S and second-site suppressor mutation H168R

Released:

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cellular tumor antigen p53 Chain: A
Molecule details ›
Chain: A
Length: 200 amino acids
Theoretical weight: 22.45 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:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P6522
Unit cell:
a: 46.287Å b: 46.287Å c: 327.445Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.199 0.198 0.212
Expression system: Escherichia coli