2j21

X-ray diffraction
1.6Å resolution

Human p53 core domain mutant M133L-V203A-N239Y-N268D-R282W

Released:
Source organism: Homo sapiens
Primary publication:
Structural basis for understanding oncogenic p53 mutations and designing rescue drugs.
Proc Natl Acad Sci U S A 103 15056-61 (2006)
PMID: 17015838

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
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: 24.62 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:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX10.1
Spacegroup: P212121
Unit cell:
a: 64.813Å b: 71.398Å c: 104.978Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.198 0.224
Expression system: Escherichia coli