4a63

X-ray diffraction
2.27Å resolution

Crystal structure of the p73-ASPP2 complex at 2.6A resolution

Released:
Source organism: Homo sapiens
Primary publication:
Structural basis for ASPP2 recognition by the tumor suppressor p73.
J Mol Biol 423 515-27 (2012)
PMID: 22917970

Function and Biology Details

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
monomeric
PDBe Complex ID:
PDB-CPX-127441 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tumor protein p73 Chains: A, C, E, G, I, K
Molecule details ›
Chains: A, C, E, G, I, K
Length: 208 amino acids
Theoretical weight: 23.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O15350 (Residues: 112-311; Coverage: 31%)
Gene names: P73, TP73
Sequence domains: P53 DNA-binding domain
Structure domains: Immunoglobulin-like
Apoptosis-stimulating of p53 protein 2 Chains: B, D, F, H, J, L
Molecule details ›
Chains: B, D, F, H, J, L
Length: 239 amino acids
Theoretical weight: 26.95 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q13625 (Residues: 892-1128; Coverage: 21%)
Gene names: ASPP2, BBP, TP53BP2
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Unit cell:
a: 132.81Å b: 170.1Å c: 177.555Å
α: 90° β: 91.98° γ: 90°
R-values:
R R work R free
0.217 0.215 0.244
Expression system: Escherichia coli BL21(DE3)