Structure analysis

The Crystal Structure of PARP12 from Biortus.

X-ray diffraction
1.75Å resolution
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 9668.11 Å2
Buried surface area: 1629.38 Å2
Dissociation area: 114.51 Å2
Dissociation energy (ΔGdiss): -1.93 kcal/mol
Dissociation entropy (TΔSdiss): -0.28 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-190480
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 9604.37 Å2
Buried surface area: 1006.83 Å2
Dissociation area: 149.8 Å2
Dissociation energy (ΔGdiss): -5.06 kcal/mol
Dissociation entropy (TΔSdiss): 1.33 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-190480

Macromolecules

Chains: A, B
Length: 196 amino acids
Theoretical weight: 22.4 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q9H0J9 (Residues: 489-684; Coverage: 28%)
Gene names: PARP12, ZC3HDC1
Pfam: Poly(ADP-ribose) polymerase catalytic domain

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