› 2ioi

X-ray diffraction
1.55Å resolution

Crystal structure of the mouse p53 core domain at 1.55 A

Released:
DOI: 10.2210/pdb2ioi/pdb
PDB entry 2ioi coloured by chain, front view.
PDB entry 2ioi coloured by chain, side view.
PDB entry 2ioi coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
High-resolution structure of the p53 core domain: implications for binding small-molecule stabilizing compounds.
Ho WC, Luo C, Zhao K, Chai X, Fitzgerald MX, Marmorstein R
Acta Crystallogr D Biol Crystallogr 62 1484-93 (2006)
PMID: 17139084

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-135466 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cellular tumor antigen p53 Chain: A
Molecule details ›
Chain: A
Length: 201 amino acids
Theoretical weight: 22.81 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P02340 (Residues: 92-292; Coverage: 52%)
Gene names: P53, Tp53, Trp53
Sequence domains: P53 DNA-binding domain
Structure domains: Immunoglobulin-like

Ligands and Environments

2 bound ligands:
Ligand ZN 1 x ZN
Ligand TRS 1 x TRS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: C2
Unit cell:
a: 92.316Å b: 44.688Å c: 63.051Å
α: 90° β: 126.25° γ: 90°
R-values:
R R work R free
0.184 0.184 0.228
Expression system: Escherichia coli BL21

Quick links

Citations

4 review citations

Structural biology of the tumor suppressor p53.
Joerger et al. (2008)
3 more

4 mentions without citation

Minimal functional sites allow a classification of zinc sites in proteins.
Andreini et al. (2011)
3 more