› 4f0d

X-ray diffraction
2.7Å resolution

Human ARTD15/PARP16 IN COMPLEX WITH 3-AMINOBENZAMIDE

Released:
DOI: 10.2210/pdb4f0d/pdb
PDB entry 4f0d coloured by chain, front view.
PDB entry 4f0d coloured by chain, side view.
PDB entry 4f0d coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of human ADP-ribose transferase ARTD15/PARP16 reveals a novel putative regulatory domain.
Karlberg T, Thorsell AG, Kallas Å, Schüler H
J Biol Chem 287 24077-81 (2012)
PMID: 22661712

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-185408 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein mono-ADP-ribosyltransferase PARP16 Chains: A, B
Molecule details ›
Chains: A, B
Length: 277 amino acids
Theoretical weight: 31.11 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8N5Y8 (Residues: 5-279; Coverage: 85%)
Gene names: ARTD15, C15orf30, PARP16
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand 3AB 1 x 3AB
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: C2221
Unit cell:
a: 117.824Å b: 195.349Å c: 60.412Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.248 0.246 0.287
Expression system: Escherichia coli

Quick links

Citations

6 review citations

PARP-1 mechanism for coupling DNA damage detection to poly(ADP-ribose) synthesis.
Langelier et al. (2013)
5 more

7 mentions without citation

Structural biology of the writers, readers, and erasers in mono- and poly(ADP-ribose) mediated signaling.
Karlberg et al. (2013)
6 more