› 2wtt

X-ray diffraction
2.3Å resolution

Structure of the human p73 tetramerization domain (crystal form II)

Released:
DOI: 10.2210/pdb2wtt/pdb
PDB entry 2wtt coloured by chain, front view.
PDB entry 2wtt coloured by chain, side view.
PDB entry 2wtt coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural evolution of p53, p63, and p73: implication for heterotetramer formation.
Joerger AC, Rajagopalan S, Natan E, Veprintsev DB, Robinson CV, Fersht AR
Proc Natl Acad Sci U S A 106 17705-10 (2009)
PMID: 19815500

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127444 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tumor protein p73 Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P
Length: 51 amino acids
Theoretical weight: 6.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O15350 (Residues: 350-399; Coverage: 8%)
Gene names: P73, TP73
Sequence domains: P53 tetramerisation motif
Structure domains: p53-like tetramerisation domain

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 32 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P212121
Unit cell:
a: 56.12Å b: 84Å c: 169.79Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.233 0.23 0.287
Expression system: Escherichia coli

Quick links

Citations

27 review citations

The p53 Pathway: Origins, Inactivation in Cancer, and Emerging Therapeutic Approaches.
Joerger et al. (2016)
26 more

6 mentions without citation

Structural evolution of p53, p63, and p73: implication for heterotetramer formation.
Joerger et al. (2009)
5 more