PDBe 4pjv

X-ray diffraction
2.5Å resolution

Structure of PARP2 catalytic domain bound to inhibitor BMN 673

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (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: Poly(ADP-ribose) polymerase catalytic domain
Structure domains:

Ligands and Environments

2 bound ligands:

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