› 2bin

X-ray diffraction
1.9Å resolution

human p53 core domain mutant M133L-H168R-V203A-N239Y-N268D

Released:
DOI: 10.2210/pdb2bin/pdb
PDB entry 2bin coloured by chain, front view.
PDB entry 2bin coloured by chain, side view.
PDB entry 2bin coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of p53 cancer mutants and mechanism of rescue by second-site suppressor mutations.
Joerger AC, Ang HC, Veprintsev DB, Blair CM, Fersht AR
J Biol Chem 280 16030-7 (2005)
PMID: 15703170

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: 219 amino acids
Theoretical weight: 24.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04637 (Residues: 94-312; Coverage: 56%)
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 BM14
Spacegroup: P6522
Unit cell:
a: 45.045Å b: 45.045Å c: 331.78Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.199 0.199 0.236
Expression system: Escherichia coli

Quick links

Citations

23 review citations

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

4 mentions without citation

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