› 8fyy

X-ray diffraction
2.8Å resolution

Crystal structure of human PARP1 ART domain bound to inhibitor UKTT5 (compound 10)

Released:
DOI: 10.2210/pdb8fyy/pdb
PDB entry 8fyy coloured by chain, front view.
PDB entry 8fyy coloured by chain, side view.
PDB entry 8fyy coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Novel modifications of PARP inhibitor veliparib increase PARP1 binding to DNA breaks.
Velagapudi UK, Rouleau-Turcotte É, Billur R, Shao X, Patil M, Black BE, Pascal J, Talele TT
Biochem J (2024)
PMID: 38372302

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140785 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Poly [ADP-ribose] polymerase 1, processed C-terminus Chain: A
Molecule details ›
Chain: A
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

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC, FRU
Carbohydrate polymer
3 bound ligands:
Ligand YH0 1 x YH0
Ligand DMS 1 x DMS
Ligand PEG 1 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P6122
Unit cell:
a: 92.732Å b: 92.732Å c: 136.359Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.202 0.199 0.273
Expression system: Escherichia coli

Quick links