X-ray diffraction
2.71Å resolution

Human PARP14 (ARTD8), catalytic fragment in complex with an N-aryl piperazine inhibitor


Function and Biology Details

Biochemical function:
  • not assigned
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 PARP14 Chains: A, B
Molecule details ›
Chains: A, B
Length: 193 amino acids
Theoretical weight: 22.12 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q460N5 (Residues: 1611-1801; Coverage: 11%)
Gene names: BAL2, KIAA1268, PARP14
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 I03
Spacegroup: C2
Unit cell:
a: 83.43Å b: 90.36Å c: 80.07Å
α: 90° β: 116.42° γ: 90°
R R work R free
0.228 0.227 0.258
Expression system: Escherichia coli BL21(DE3)