PDBe 4hhy

X-ray diffraction
2.36Å resolution

Crystal structure of PARP catalytic domain in complex with novel inhibitors

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:
monomeric (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: 355 amino acids
Theoretical weight: 39.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P09874 (Residues: 660-1011; Coverage: 35%)
Gene names: ADPRT, PARP1, PPOL
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P212121
Unit cell:
a: 103.797Å b: 107.549Å c: 143.107Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.24 0.237 0.299
Expression system: Escherichia coli BL21(DE3)