› 4iby

X-ray diffraction
1.45Å resolution

Human p53 core domain with hot spot mutation R273H and second-site suppressor mutation S240R

Released:
DOI: 10.2210/pdb4iby/pdb
PDB entry 4iby coloured by chain, front view.
PDB entry 4iby coloured by chain, side view.
PDB entry 4iby coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural studies of p53 inactivation by DNA-contact mutations and its rescue by suppressor mutations via alternative protein-DNA interactions.
Eldar A, Rozenberg H, Diskin-Posner Y, Rohs R, Shakked Z
Nucleic Acids Res 41 8748-59 (2013)
PMID: 23863845

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
Molecule details ›
Chains: A, B
Length: 200 amino acids
Theoretical weight: 22.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
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

2 bound ligands:
Ligand ZN 2 x ZN
Ligand EDO 7 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P21
Unit cell:
a: 43.524Å b: 69.212Å c: 67.195Å
α: 90° β: 96.61° γ: 90°
R-values:
R R work R free
0.171 0.169 0.2
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

The p53 Pathway: Origins, Inactivation in Cancer, and Emerging Therapeutic Approaches.
Joerger et al. (2016)
8 more

3 mentions without citation

Structural studies of p53 inactivation by DNA-contact mutations and its rescue by suppressor mutations via alternative protein-DNA interactions.
Eldar et al. (2013)
2 more