› 3zy0

X-ray diffraction
1.9Å resolution

Crystal structure of a truncated variant of the human p63 tetramerization domain lacking the C-terminal helix

Released:
DOI: 10.2210/pdb3zy0/pdb
PDB entry 3zy0 coloured by chain, front view.
PDB entry 3zy0 coloured by chain, side view.
PDB entry 3zy0 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure and kinetic stability of the p63 tetramerization domain.
Natan E, Joerger AC
OpenAccess logo J Mol Biol 415 503-13 (2012)
PMID: 22100306

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190572 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tumor protein 63 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 32 amino acids
Theoretical weight: 3.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9H3D4 (Residues: 398-427; Coverage: 4%)
Gene names: KET, P63, P73H, P73L, TP63, TP73L
Sequence domains: P53 tetramerisation motif

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 8 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P1
Unit cell:
a: 30.14Å b: 33.13Å c: 34.68Å
α: 105.33° β: 102.07° γ: 110.15°
R-values:
R R work R free
0.206 0.204 0.252
Expression system: Escherichia coli

Quick links

Citations

8 review citations

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

3 mentions without citation

Structure and kinetic stability of the p63 tetramerization domain.
Natan et al. (2012)
2 more