Structure analysis

PARP15 catalytic domain in complex with OUL252

X-ray diffraction
1.35Å resolution
Source organism: Homo sapiens
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
Download    3D Visualisation
Multimeric state: homo dimer
Accessible surface area: 19085.19 Å2
Buried surface area: 2333.4 Å2
Dissociation area: 1,031.09 Å2
Dissociation energy (ΔGdiss): 7.29 kcal/mol
Dissociation entropy (TΔSdiss): 12.73 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-175096

Macromolecules

Chains: A, B
Length: 221 amino acids
Theoretical weight: 25.44 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q460N3 (Residues: 481-678; Coverage: 29%)
Gene names: BAL3, PARP15
Pfam: Poly(ADP-ribose) polymerase catalytic domain
InterPro: Poly(ADP-ribose) polymerase, catalytic domain

Search similar proteins