› 1saf

Solution NMR

HIGH RESOLUTION SOLUTION NMR STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-DIMENSIONAL NMR (SAD STRUCTURES)

Released:
DOI: 10.2210/pdb1saf/pdb
PDB entry 1saf coloured by chain, ensemble of 76 models, front view.
PDB entry 1saf coloured by chain, ensemble of 76 models, side view.
PDB entry 1saf coloured by chain, ensemble of 76 models, top view.
Source organism: Homo sapiens
Primary publication:
Refined solution structure of the oligomerization domain of the tumour suppressor p53.
Clore GM, Ernst J, Clubb R, Omichinski JG, Kennedy WM, Sakaguchi K, Appella E, Gronenborn AM
Nat Struct Biol 2 321-33 (1995)
PMID: 7796267

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-528766 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cellular tumor antigen p53 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 42 amino acids
Theoretical weight: 4.95 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P04637 (Residues: 319-360; Coverage: 11%)
Gene names: P53, TP53
Sequence domains: P53 tetramerisation motif
Structure domains: p53-like tetramerisation domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores

Quick links

Citations

25 review citations

The multiple mechanisms that regulate p53 activity and cell fate.
Hafner et al. (2019)
24 more

3 mentions without citation

Structural diversity of p63 and p73 isoforms.
Osterburg et al. (2022)
2 more