2riq

X-ray diffraction
1.7Å resolution

Crystal Structure of the Third Zinc-binding domain of human PARP-1

Released:

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-140788 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Poly [ADP-ribose] polymerase 1, processed C-terminus Chain: A
Molecule details ›
Chain: A
Length: 160 amino acids
Theoretical weight: 18.39 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09874 (Residues: 216-366; Coverage: 15%)
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: NSLS BEAMLINE X12C
Spacegroup: C2221
Unit cell:
a: 71.841Å b: 85.652Å c: 67.758Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.178 0.23
Expression system: Escherichia coli