› 1uol

X-ray diffraction
1.9Å resolution

Crystal structure of the human p53 core domain mutant M133L/V203A/N239Y/N268D at 1.9 A resolution.

Released:
DOI: 10.2210/pdb1uol/pdb
PDB entry 1uol coloured by chain, front view.
PDB entry 1uol coloured by chain, side view.
PDB entry 1uol coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of a superstable mutant of human p53 core domain. Insights into the mechanism of rescuing oncogenic mutations.
Joerger AC, Allen MD, Fersht AR
J Biol Chem 279 1291-6 (2004)
PMID: 14534297

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

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: SRS BEAMLINE PX14.2
Spacegroup: P212121
Unit cell:
a: 65Å b: 71Å c: 104.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.192 0.23
Expression system: Escherichia coli

Quick links

Citations

12 review citations

Flexible nets. The roles of intrinsic disorder in protein interaction networks.
Dunker et al. (2005)
11 more

19 mentions without citation

Electrochemistry of nonconjugated proteins and glycoproteins. Toward sensors for biomedicine and glycomics.
Paleček et al. (2015)
18 more