› 4ijt

X-ray diffraction
1.78Å resolution

Human p53 core domain with hot spot mutation R273H (form II)

Released:
DOI: 10.2210/pdb4ijt/pdb
PDB entry 4ijt coloured by chain, front view.
PDB entry 4ijt coloured by chain, side view.
PDB entry 4ijt 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 Chain: A
Molecule details ›
Chain: A
Length: 200 amino acids
Theoretical weight: 22.49 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

3 bound ligands:
Ligand ZN 2 x ZN
Ligand DTT 1 x DTT
Ligand EDO 3 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P61
Unit cell:
a: 74.937Å b: 74.937Å c: 73.308Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.163 0.162 0.194
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 review citations

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

4 mentions without citation

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