PDBe 4opx

X-ray diffraction
3.31Å resolution

Structure of Human PARP-1 bound to a DNA double strand break in complex with (2R)-5-fluoro-2-methyl-2,3-dihydro-1-benzofuran-7-carboxamide

Released:

Function and Biology Details

Reaction catalysed:
NAD(+) + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
1 distinct DNA molecule
Macromolecules (3 distinct):
Poly [ADP-ribose] polymerase 1 Chains: A, D
Molecule details ›
Chains: A, D
Length: 267 amino acids
Theoretical weight: 30.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09874 (Residues: 1-97, 207-366; Coverage: 25%)
Gene names: ADPRT, PARP1, PPOL
Sequence domains:
Structure domains: Zinc finger, PARP-type
Poly [ADP-ribose] polymerase 1 Chains: C, F
Molecule details ›
Chains: C, F
Length: 505 amino acids
Theoretical weight: 57.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09874 (Residues: 518-1014; Coverage: 49%)
Gene names: ADPRT, PARP1, PPOL
Sequence domains:
Structure domains:
DNA (26-MER) Chains: M, N
Molecule details ›
Chains: M, N
Length: 26 nucleotides
Theoretical weight: 7.99 KDa

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P212121
Unit cell:
a: 65.15Å b: 112.91Å c: 295.29Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.304 0.303 0.325
Expression system: Escherichia coli