› 2wgx

X-ray diffraction
1.75Å resolution

HUMAN P53 CORE DOMAIN MUTANT M133L-V203A-Y236F-N239Y-T253I-N268D

Released:
DOI: 10.2210/pdb2wgx/pdb
PDB entry 2wgx coloured by chain, front view.
PDB entry 2wgx coloured by chain, side view.
PDB entry 2wgx coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Stabilising the DNA-binding domain of p53 by rational design of its hydrophobic core.
Khoo KH, Joerger AC, Freund SM, Fersht AR
Protein Eng Des Sel 22 421-30 (2009)
PMID: 19515728

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: 219 amino acids
Theoretical weight: 24.59 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 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P212121
Unit cell:
a: 65.328Å b: 71.075Å c: 104.915Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.17 0.199
Expression system: Escherichia coli

Quick links

Citations

5 review citations

The tumor suppressor p53: from structures to drug discovery.
Joerger et al. (2010)
4 more

3 mentions without citation

Stabilising the DNA-binding domain of p53 by rational design of its hydrophobic core.
Khoo et al. (2009)
2 more