PDBe 1wok

X-ray diffraction
3Å resolution

Crystal structure of catalytic domain of human poly(ADP-ribose) polymerase complexed with a quinoxaline-type inhibitor

Released:

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Poly [ADP-ribose] polymerase 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 350 amino acids
Theoretical weight: 39.2 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09874 (Residues: 662-1011; Coverage: 35%)
Gene names: ADPRT, PARP1, PPOL
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B2
Spacegroup: P21
Unit cell:
a: 90.05Å b: 77.08Å c: 113.72Å
α: 90° β: 117.43° γ: 90°
R-values:
R R work R free
0.233 0.233 0.288
Expression system: Escherichia coli