› 5dsy

X-ray diffraction
2.7Å resolution

Crystal structure of constitutively active PARP-2

Released:
DOI: 10.2210/pdb5dsy/pdb
PDB entry 5dsy coloured by chain, front view.
PDB entry 5dsy coloured by chain, side view.
PDB entry 5dsy coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
PARP-1 Activation Requires Local Unfolding of an Autoinhibitory Domain.
Dawicki-McKenna JM, Langelier MF, DeNizio JE, Riccio AA, Cao CD, Karch KR, McCauley M, Steffen JD, Black BE, Pascal JM
Mol Cell 60 755-768 (2015)
PMID: 26626480

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193721 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Poly [ADP-ribose] polymerase 2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 280 amino acids
Theoretical weight: 31.68 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UGN5 (Residues: 348-583; Coverage: 41%)
Gene names: ADPRT2, ADPRTL2, PARP2
Sequence domains: Poly(ADP-ribose) polymerase catalytic domain
Structure domains: Phosphoenolpyruvate Carboxykinase; domain 3

Ligands and Environments

1 bound ligand:
Ligand UHB 4 x UHB
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 12.3.1
Spacegroup: P212121
Unit cell:
a: 92.163Å b: 119.9Å c: 120.739Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.193 0.248
Expression system: Escherichia coli

Quick links

Citations

48 review citations

PARP inhibitors: Synthetic lethality in the clinic.
Lord et al. (2017)
47 more

6 mentions without citation

PARP-1 Activation Requires Local Unfolding of an Autoinhibitory Domain.
Dawicki-McKenna et al. (2015)
5 more