› 2vge

X-ray diffraction
2.1Å resolution

Crystal structure of the C-terminal region of human iASPP

Released:
DOI: 10.2210/pdb2vge/pdb
PDB entry 2vge coloured by chain, front view.
PDB entry 2vge coloured by chain, side view.
PDB entry 2vge coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Biochemical and structural studies of ASPP proteins reveal differential binding to p53, p63, and p73.
Robinson RA, Lu X, Jones EY, Siebold C
Structure 16 259-68 (2008)
PMID: 18275817

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186713 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RelA-associated inhibitor Chain: A
Molecule details ›
Chain: A
Length: 229 amino acids
Theoretical weight: 25.31 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8WUF5 (Residues: 607-828; Coverage: 27%)
Gene names: IASPP, NKIP1, PPP1R13BL, PPP1R13L, RAI
Sequence domains:
Structure domains: Ankyrin repeat-containing domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21212
Unit cell:
a: 59.969Å b: 67.545Å c: 50.49Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.208 0.257
Expression system: Escherichia coli

Quick links

Citations

11 review citations

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

10 mentions without citation

Insight into the structural basis of pro- and antiapoptotic p53 modulation by ASPP proteins.
Ahn et al. (2009)
9 more