› 4mzi

X-ray diffraction
1.25Å resolution

Crystal structure of a human mutant p53

Released:
DOI: 10.2210/pdb4mzi/pdb
PDB entry 4mzi coloured by chain, front view.
PDB entry 4mzi coloured by chain, side view.
PDB entry 4mzi coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Reversal of the DNA-binding-induced loop L1 conformational switch in an engineered human p53 protein.
Emamzadah S, Tropia L, Vincenti I, Falquet B, Halazonetis TD
J Mol Biol 426 936-44 (2014)
PMID: 24374182

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: 22.53 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04637 (Residues: 93-292; 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: P212121
Unit cell:
a: 44.707Å b: 62.428Å c: 73.701Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.198 0.201
Expression system: Escherichia coli

Quick links

Citations

6 review citations

p53 Proteoforms and Intrinsic Disorder: An Illustration of the Protein Structure-Function Continuum Concept.
Uversky VN. (2016)
5 more

6 mentions without citation

Utilizing network pharmacology and molecular docking to explore the underlying mechanism of Guizhi Fuling Wan in treating endometriosis.
Wang et al. (2021)
5 more