› 1uk1

X-ray diffraction
3Å resolution

Crystal structure of human poly(ADP-ribose) polymerase complexed with a potent inhibitor

Released:
DOI: 10.2210/pdb1uk1/pdb
PDB entry 1uk1 coloured by chain, front view.
PDB entry 1uk1 coloured by chain, side view.
PDB entry 1uk1 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Rational approaches to discovery of orally active and brain-penetrable quinazolinone inhibitors of poly(ADP-ribose)polymerase.
Hattori K, Kido Y, Yamamoto H, Ishida J, Kamijo K, Murano K, Ohkubo M, Kinoshita T, Iwashita A, Mihara K, Yamazaki S, Matsuoka N, Teramura Y, Miyake H
J Med Chem 47 4151-4 (2004)
PMID: 15293985

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 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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 350 amino acids
Theoretical weight: 39.2 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 FRQ 2 x FRQ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6B
Spacegroup: C2
Unit cell:
a: 179.96Å b: 53.27Å c: 91.47Å
α: 90° β: 113.8° γ: 90°
R-values:
R R work R free
0.234 0.242 0.274
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Poly(ADP-ribose) polymerase and the therapeutic effects of its inhibitors.
Jagtap et al. (2005)
8 more

8 mentions without citation

The natural history of ADP-ribosyltransferases and the ADP-ribosylation system.
Aravind et al. (2015)
7 more