Structure analysis

Crystal structure of constitutively active PARP-2

X-ray diffraction
2.7Å resolution
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
Download    3D Visualisation
Multimeric state: monomeric
Accessible surface area: 12077.62 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-193721
Assembly 2
Download    3D Visualisation
Multimeric state: monomeric
Accessible surface area: 12641.93 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-193721
Assembly 3
Download    3D Visualisation
Multimeric state: monomeric
Accessible surface area: 12404.84 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-193721
Assembly 4
Download    3D Visualisation
Multimeric state: monomeric
Accessible surface area: 12203.48 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-193721

Macromolecules

Chains: A, B, C, D
Length: 280 amino acids
Theoretical weight: 31.68 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UGN5 (Residues: 348-583; Coverage: 41%)
Gene names: ADPRT2, ADPRTL2, PARP2
Pfam: Poly(ADP-ribose) polymerase catalytic domain
InterPro: Poly(ADP-ribose) polymerase, catalytic domain
CATH: Phosphoenolpyruvate Carboxykinase; domain 3

Search similar proteins