› 6bhv

X-ray diffraction
2.3Å resolution

Human PARP-1 bound to NAD+ analog benzamide adenine dinucleotide (BAD)

Released:
DOI: 10.2210/pdb6bhv/pdb
PDB entry 6bhv coloured by chain, front view.
PDB entry 6bhv coloured by chain, side view.
PDB entry 6bhv coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
NAD+ analog reveals PARP-1 substrate-blocking mechanism and allosteric communication from catalytic center to DNA-binding domains.
Langelier MF, Zandarashvili L, Aguiar PM, Black BE, Pascal JM
Nat Commun 9 844 (2018)
PMID: 29487285

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-140785 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Poly [ADP-ribose] polymerase 1, processed C-terminus Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 271 amino acids
Theoretical weight: 30 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09874 (Residues: 788-1012; Coverage: 22%)
Gene names: ADPRT, PARP1, PPOL
Sequence domains: Poly(ADP-ribose) polymerase catalytic domain
Structure domains: Phosphoenolpyruvate Carboxykinase; domain 3

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 12.3.1
Spacegroup: P1
Unit cell:
a: 44.51Å b: 75.356Å c: 85.607Å
α: 98.66° β: 104.94° γ: 106.73°
R-values:
R R work R free
0.199 0.198 0.222
Expression system: Escherichia coli

Quick links

Citations

38 review citations

Poly(ADP-ribosyl)ation by PARP1: reaction mechanism and regulatory proteins.
Alemasova et al. (2019)
37 more

27 mentions without citation

PARP family enzymes: regulation and catalysis of the poly(ADP-ribose) posttranslational modification.
Langelier et al. (2018)
26 more