4a9z

X-ray diffraction
2.29Å resolution

CRYSTAL STRUCTURE OF HUMAN P63 TETRAMERIZATION DOMAIN

Released:
Source organism: Homo sapiens
Entry authors: Muniz JRC, Coutandin D, Salah E, Chaikuad A, Vollmar M, Weigelt J, Arrowsmith CH, Edwards AM, Bountra C, Dotsch V, von Delft F, Knapp S

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tumor protein 63 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 61 amino acids
Theoretical weight: 7.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9H3D4 (Residues: 397-455; Coverage: 9%)
Gene names: KET, P63, P73H, P73L, TP63, TP73L
Sequence domains: P53 tetramerisation motif
Structure domains: p53-like tetramerisation domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P3121
Unit cell:
a: 80.85Å b: 80.85Å c: 68.37Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.197 0.194 0.246
Expression system: Escherichia coli BL21(DE3)