› 5nqe

X-ray diffraction
2.71Å resolution

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

Released:
DOI: 10.2210/pdb5nqe/pdb
PDB entry 5nqe coloured by chain, front view.
PDB entry 5nqe coloured by chain, side view.
PDB entry 5nqe coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Design and synthesis of potent inhibitors of the mono(ADP-ribosyl)transferase, PARP14.
Upton K, Meyers M, Thorsell AG, Karlberg T, Holechek J, Lease R, Schey G, Wolf E, Lucente A, Schüler H, Ferraris D
Bioorg Med Chem Lett 27 2907-2911 (2017)
PMID: 28495083

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175097 (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:
Ligand 94Z 2 x 94Z
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-values:
R R work R free
0.228 0.227 0.258
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

The role of ADP-ribose metabolism in metabolic regulation, adipose tissue differentiation, and metabolism.
Szántó et al. (2020)
4 more

1 mention without citation

Research Progress on PARP14 as a Drug Target.
Qin et al. (2019)