› 5zqp

X-ray diffraction
1.99Å resolution

Function and Biology Details

Reaction catalysed: 
NAD(+) + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-574338 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Poly [ADP-ribose] polymerase tankyrase-2 Chain: A
Molecule details ›
Chain: A
Length: 168 amino acids
Theoretical weight: 19.15 KDa
Source organism: Homo sapiens
Expression system: unidentified
UniProt:
  • Canonical: Q9H2K2 (Residues: 947-1114; Coverage: 14%)
Gene names: PARP5B, TANK2, TNKL, TNKS2
Sequence domains: Poly(ADP-ribose) polymerase catalytic domain
Structure domains: Phosphoenolpyruvate Carboxykinase; domain 3
Poly [ADP-ribose] polymerase tankyrase-2 Chain: B
Molecule details ›
Chain: B
Length: 48 amino acids
Theoretical weight: 5.36 KDa
Source organism: Homo sapiens
Expression system: unidentified
UniProt:
  • Canonical: Q9H2K2 (Residues: 1115-1162; Coverage: 4%)
Gene names: PARP5B, TANK2, TNKL, TNKS2
Structure domains: YefM-like fold

Ligands and Environments

4 bound ligands:
Ligand ZN 1 x ZN
Ligand 9H3 1 x 9H3
Ligand PO4 1 x PO4
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B2
Spacegroup: P41212
Unit cell:
a: 67.405Å b: 67.405Å c: 115.092Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.173 0.205
Expression system: unidentified

Quick links

Citations

2 review citations

ADP-Ribosylation as Post-Translational Modification of Proteins: Use of Inhibitors in Cancer Control.
Poltronieri et al. (2021)
1 more