PDBe 4gv7

X-ray diffraction
2.89Å resolution

Human ARTD1 (PARP1) - Catalytic domain in complex with inhibitor ME0328

Released:
Source organism: Homo sapiens
Entry authors: Karlberg T, Thorsell AG, Lindgren AEG, Ekblad T, Spjut S, Andersson CD, Weigelt J, Linusson A, Elofsson M, Schuler H

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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Poly [ADP-ribose] polymerase 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 358 amino acids
Theoretical weight: 40.2 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:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P21
Unit cell:
a: 87.05Å b: 49.43Å c: 183.51Å
α: 90° β: 101.82° γ: 90°
R-values:
R R work R free
0.215 0.211 0.286
Expression system: Escherichia coli