› 4pjv

X-ray diffraction
2.5Å resolution

Structure of PARP2 catalytic domain bound to inhibitor BMN 673

Released:
DOI: 10.2210/pdb4pjv/pdb
PDB entry 4pjv coloured by chain, front view.
PDB entry 4pjv coloured by chain, side view.
PDB entry 4pjv coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for the inhibition of poly(ADP-ribose) polymerases 1 and 2 by BMN 673, a potent inhibitor derived from dihydropyridophthalazinone.
Aoyagi-Scharber M, Gardberg AS, Yip BK, Wang B, Shen Y, Fitzpatrick PA
Acta Crystallogr F Struct Biol Commun 70 1143-9 (2014)
PMID: 25195882

Function and Biology Details

Reaction catalysed: 
NAD(+) + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor
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-193721 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Poly [ADP-ribose] polymerase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 368 amino acids
Theoretical weight: 41.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UGN5 (Residues: 235-579; Coverage: 59%)
Gene names: ADPRT2, ADPRTL2, PARP2
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand 2YQ 2 x 2YQ
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P1
Unit cell:
a: 52.86Å b: 57.74Å c: 69.29Å
α: 77.28° β: 79.99° γ: 63.88°
R-values:
R R work R free
0.218 0.214 0.287
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Understanding specific functions of PARP-2: new lessons for cancer therapy.
Ali et al. (2016)
5 more

7 mentions without citation

Histone Parylation factor 1 contributes to the inhibition of PARP1 by cancer drugs.
Rudolph et al. (2021)
6 more