› 2xwr

X-ray diffraction
1.68Å resolution

Crystal structure of the DNA-binding domain of human p53 with extended N terminus

Released:
DOI: 10.2210/pdb2xwr/pdb
PDB entry 2xwr coloured by chain, front view.
PDB entry 2xwr coloured by chain, side view.
PDB entry 2xwr coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Interaction of the p53 DNA-binding domain with its n-terminal extension modulates the stability of the p53 tetramer.
Natan E, Baloglu C, Pagel K, Freund SM, Morgner N, Robinson CV, Fersht AR, Joerger AC
J Mol Biol 409 358-68 (2011)
PMID: 21457718

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: 205 amino acids
Theoretical weight: 23.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04637 (Residues: 89-293; Coverage: 52%)
Gene names: P53, TP53
Sequence domains: P53 DNA-binding domain
Structure domains: Immunoglobulin-like

Ligands and Environments

1 bound ligand:
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P21
Unit cell:
a: 51.5Å b: 68.45Å c: 58.89Å
α: 90° β: 99.46° γ: 90°
R-values:
R R work R free
0.175 0.173 0.209
Expression system: Escherichia coli

Quick links

Citations

8 review citations

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

23 mentions without citation

Pathological unfoldomics of uncontrolled chaos: intrinsically disordered proteins and human diseases.
Uversky et al. (2014)
22 more