› 2pcx

X-ray diffraction
1.54Å resolution

Crystal structure of p53DBD(R282Q) at 1.54-angstrom Resolution

Released:
DOI: 10.2210/pdb2pcx/pdb
PDB entry 2pcx coloured by chain, front view.
PDB entry 2pcx coloured by chain, side view.
PDB entry 2pcx coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Impact of low-frequency hotspot mutation R282Q on the structure of p53 DNA-binding domain as revealed by crystallography at 1.54 angstroms resolution.
Tu C, Tan YH, Shaw G, Zhou Z, Bai Y, Luo R, Ji X
Acta Crystallogr D Biol Crystallogr 64 471-7 (2008)
PMID: 18453682

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: 220 amino acids
Theoretical weight: 24.81 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P04637 (Residues: 94-292; Coverage: 51%)
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: RIGAKU
Spacegroup: P1
Unit cell:
a: 34.9Å b: 35.2Å c: 41.6Å
α: 111.8° β: 94.9° γ: 112.4°
R-values:
R R work R free
0.193 0.191 0.232
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 citation in other articles

p28, a first in class peptide inhibitor of cop1 binding to p53.
Yamada et al. (2013)
5 more

8 mentions without citation

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