› 1aie

X-ray diffraction
1.5Å resolution

P53 TETRAMERIZATION DOMAIN CRYSTAL STRUCTURE

Released:
DOI: 10.2210/pdb1aie/pdb
PDB entry 1aie coloured by chain, front view.
PDB entry 1aie coloured by chain, side view.
PDB entry 1aie coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystallization and structure solution of p53 (residues 326-356) by molecular replacement using an NMR model as template.
Mittl PR, Chène P, Grütter MG
Acta Crystallogr D Biol Crystallogr 54 86-9 (1998)
PMID: 9761820

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138138 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cellular tumor antigen p53 Chain: A
Molecule details ›
Chain: A
Length: 31 amino acids
Theoretical weight: 3.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P04637 (Residues: 326-356; Coverage: 8%)
Gene names: P53, TP53
Sequence domains: P53 tetramerisation motif

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF
Spacegroup: P422
Unit cell:
a: 45.5Å b: 45.5Å c: 33.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.191 0.252
Expression system: Escherichia coli BL21

Quick links

Citations

7 review citations

Structural biology of the tumor suppressor p53.
Joerger et al. (2008)
6 more

37 mentions without citation

Absence of a simple code: how transcription factors read the genome.
Slattery et al. (2014)
36 more