8hko

X-ray diffraction
2.1Å resolution

Mutated human ADP-ribosyltransferase 2 (PARP2) catalytic domain bound to Rucaparib

Released:
Source organism: Homo sapiens
Entry authors: Wang XY, Zhou J, Xu BL

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-577402 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Poly [ADP-ribose] polymerase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 353 amino acids
Theoretical weight: 39.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UGN5 (Residues: 230-581; Coverage: 60%)
Gene names: ADPRT2, ADPRTL2, PARP2
Sequence domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL02U1
Spacegroup: P21
Unit cell:
a: 39.761Å b: 86.286Å c: 96.047Å
α: 90° β: 90.39° γ: 90°
R-values:
R R work R free
0.166 0.164 0.211
Expression system: Escherichia coli