› 3d05

X-ray diffraction
1.7Å resolution

Human p53 core domain with hot spot mutation R249S (II)

Released:
DOI: 10.2210/pdb3d05/pdb
PDB entry 3d05 coloured by chain, front view.
PDB entry 3d05 coloured by chain, side view.
PDB entry 3d05 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of restoring sequence-specific DNA binding and transactivation to mutant p53 by suppressor mutations.
Suad O, Rozenberg H, Brosh R, Diskin-Posner Y, Kessler N, Shimon LJ, Frolow F, Liran A, Rotter V, Shakked Z
J Mol Biol 385 249-65 (2009)
PMID: 18996393

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 Chain: A
Molecule details ›
Chain: A
Length: 200 amino acids
Theoretical weight: 22.44 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 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P6522
Unit cell:
a: 44.374Å b: 44.374Å c: 330.026Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.221 0.218 0.264
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Mutant p53: one name, many proteins.
Freed-Pastor et al. (2012)
6 more

3 mentions without citation

Structural and Drug Targeting Insights on Mutant p53.
Gomes et al. (2021)
2 more