› 6f5b

X-ray diffraction
2.8Å resolution

Structure of ARTD2/PARP2 WGR domain bound to double stranded DNA with 5'phosphate

Released:
DOI: 10.2210/pdb6f5b/pdb
PDB entry 6f5b coloured by chain, front view.
PDB entry 6f5b coloured by chain, side view.
PDB entry 6f5b coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for DNA break recognition by ARTD2/PARP2.
Obaji E, Haikarainen T, Lehtiö L
Nucleic Acids Res 46 12154-12165 (2018)
PMID: 30321391

Function and Biology Details

Reaction catalysed: 
NAD(+) + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-119880 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct DNA molecule
Macromolecules (2 distinct):
Poly [ADP-ribose] polymerase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 131 amino acids
Theoretical weight: 15.28 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UGN5 (Residues: 90-218; Coverage: 22%)
Gene names: ADPRT2, ADPRTL2, PARP2
Sequence domains: WGR domain
DNA (5'-D(P*GP*CP*CP*TP*AP*TP*AP*GP*GP*C)-3') Chains: C, D, E, F
Molecule details ›
Chains: C, D, E, F
Length: 10 nucleotides
Theoretical weight: 3.05 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P212121
Unit cell:
a: 63.16Å b: 84.36Å c: 95.96Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.208 0.274
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

6 review citations

Poly(ADP-ribose) polymerase inhibition: past, present and future.
Curtin et al. (2020)
5 more

5 mentions without citation

PARP family enzymes: regulation and catalysis of the poly(ADP-ribose) posttranslational modification.
Langelier et al. (2018)
4 more