› 2j1y

X-ray diffraction
1.69Å resolution

Human p53 core domain mutant M133L-V203A-N239Y-G245S-N268D

Released:
DOI: 10.2210/pdb2j1y/pdb
PDB entry 2j1y coloured by chain, front view.
PDB entry 2j1y coloured by chain, side view.
PDB entry 2j1y coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for understanding oncogenic p53 mutations and designing rescue drugs.
Joerger AC, Ang HC, Fersht AR
Proc Natl Acad Sci U S A 103 15056-61 (2006)
PMID: 17015838

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, C, D
Molecule details ›
Chains: A, B, C, D
Length: 200 amino acids
Theoretical weight: 22.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
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 4 x ZN
Ligand CA 4 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX10.1
Spacegroup: P21
Unit cell:
a: 68.514Å b: 73.076Å c: 84.76Å
α: 90° β: 90.05° γ: 90°
R-values:
R R work R free
0.189 0.189 0.218
Expression system: Escherichia coli

Quick links

Citations

52 review citations

TP53 mutations in human cancers: origins, consequences, and clinical use.
Olivier et al. (2010)
51 more

6 mentions without citation

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