› 3l3m

X-ray diffraction
2.5Å resolution

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-140785 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Poly [ADP-ribose] polymerase 1, processed C-terminus Chain: A
Molecule details ›
Chain: A
Length: 350 amino acids
Theoretical weight: 39.17 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:
Ligand A92 1 x A92
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P321
Unit cell:
a: 94.205Å b: 94.205Å c: 68.856Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.205 0.202 0.275
Expression system: Escherichia coli

Quick links

Citations

7 review citations

PARP-1 mechanism for coupling DNA damage detection to poly(ADP-ribose) synthesis.
Langelier et al. (2013)
6 more

20 mentions without citation

Structural biology of the writers, readers, and erasers in mono- and poly(ADP-ribose) mediated signaling.
Karlberg et al. (2013)
19 more