› 4l7o

X-ray diffraction
2Å resolution

Human artd3 (parp3) - catalytic domain in complex with inhibitor STO1542

Released:
DOI: 10.2210/pdb4l7o/pdb
PDB entry 4l7o coloured by chain, front view.
PDB entry 4l7o coloured by chain, side view.
PDB entry 4l7o coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Chemical probes to study ADP-ribosylation: synthesis and biochemical evaluation of inhibitors of the human ADP-ribosyltransferase ARTD3/PARP3.
Lindgren AE, Karlberg T, Ekblad T, Spjut S, Thorsell AG, Andersson CD, Nhan TT, Hellsten V, Weigelt J, Linusson A, Schüler H, Elofsson M
J Med Chem 56 9556-68 (2013)
PMID: 24188023

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195358 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein mono-ADP-ribosyltransferase PARP3 Chain: A
Molecule details ›
Chain: A
Length: 357 amino acids
Theoretical weight: 39.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9Y6F1 (Residues: 178-532; Coverage: 67%)
Gene names: ADPRT3, ADPRTL3, PARP3
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand 1VD 1 x 1VD
Ligand DMS 1 x DMS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P21
Unit cell:
a: 54.519Å b: 56.918Å c: 56.84Å
α: 90° β: 112.43° γ: 90°
R-values:
R R work R free
0.165 0.163 0.21
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 citation in other articles

PARP3 controls TGFβ and ROS driven epithelial-to-mesenchymal transition and stemness by stimulating a TG2-Snail-E-cadherin axis.
Karicheva et al. (2016)
3 more