› 2jvn

Solution NMR

Domain C of human PARP-1

Released:
DOI: 10.2210/pdb2jvn/pdb
PDB entry 2jvn coloured by chain, ensemble of 10 models, front view.
PDB entry 2jvn coloured by chain, ensemble of 10 models, side view.
PDB entry 2jvn coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
Domain C of human poly(ADP-ribose) polymerase-1 is important for enzyme activity and contains a novel zinc-ribbon motif.
Tao Z, Gao P, Hoffman DW, Liu HW
Biochemistry 47 5804-13 (2008)
PMID: 18452307

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: 126 amino acids
Theoretical weight: 14.5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09874 (Residues: 233-358; Coverage: 12%)
Gene names: ADPRT, PARP1, PPOL
Sequence domains:
Structure domains: Actin; Chain A, domain 4

Ligands and Environments

1 bound ligand:
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

17 review citations

PARP inhibition: PARP1 and beyond.
Rouleau et al. (2010)
16 more

9 mentions without citation

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