PDBe 5lxp

X-ray diffraction
2.07Å resolution

Human PARP14 (ARTD8), catalytic fragment in complex with inhibitor H5

Released:
Source organism: Homo sapiens
Primary publication:
Small Molecule Microarray Based Discovery of PARP14 Inhibitors.
Angew. Chem. Int. Ed. Engl. (2016)
PMID: 27918638

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:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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)
UniProt:
  • 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 I04
Spacegroup: C2
Unit cell:
a: 145.4Å b: 83.68Å c: 35.05Å
α: 90° β: 95.95° γ: 90°
R-values:
R R work R free
0.179 0.178 0.207
Expression system: Escherichia coli BL21(DE3)