X-ray diffraction
1.25Å resolution

Human PARP10 (ARTD10), catalytic fragment in complex with PARP inhibitor Veliparib


Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Protein mono-ADP-ribosyltransferase PARP10 Chains: A, B
Molecule details ›
Chains: A, B
Length: 191 amino acids
Theoretical weight: 21.63 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q53GL7 (Residues: 819-1007; Coverage: 18%)
Gene name: PARP10
Sequence domains: Poly(ADP-ribose) polymerase catalytic domain
Structure domains: Phosphoenolpyruvate Carboxykinase; domain 3

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P21
Unit cell:
a: 52.48Å b: 88.677Å c: 58.405Å
α: 90° β: 104.68° γ: 90°
R R work R free
0.208 0.208 0.213
Expression system: Escherichia coli BL21(DE3)