› 2rp4

Solution NMR

Solution Structure of the oligomerization domain in Dmp53

Released:
DOI: 10.2210/pdb2rp4/pdb
PDB entry 2rp4 coloured by chain, ensemble of 20 models, front view.
PDB entry 2rp4 coloured by chain, ensemble of 20 models, side view.
PDB entry 2rp4 coloured by chain, ensemble of 20 models, top view.
Source organism: Drosophila melanogaster
Primary publication:
Structural evolution of C-terminal domains in the p53 family.
Ou HD, Löhr F, Vogel V, Mäntele W, Dötsch V
EMBO J 26 3463-73 (2007)
PMID: 17581633

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184779 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
P53 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 76 amino acids
Theoretical weight: 8.57 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q8IH92 (Residues: 449-519; Coverage: 14%)
Gene names: CG33336, p53
Sequence domains: Transcription factor P53 - C terminal domain
Structure domains: Transcription factor p53, C-terminal domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli BL21

Quick links

Citations

21 review citations

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

5 mentions without citation

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