Structure analysis

Human PARP14 (ARTD8), catalytic fragment in complex with inhibitor H10

X-ray diffraction
2.17Å 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: 9753.9 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-175097
Assembly 2
Download    3D Visualisation
Multimeric state: monomeric
Accessible surface area: 9802.84 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-175097

Macromolecules

Chains: A, B
Length: 193 amino acids
Theoretical weight: 22.12 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q460N5 (Residues: 1611-1801; Coverage: 11%)
Gene names: BAL2, KIAA1268, PARP14
Pfam: Poly(ADP-ribose) polymerase catalytic domain
InterPro: Poly(ADP-ribose) polymerase, catalytic domain
CATH: Phosphoenolpyruvate Carboxykinase; domain 3

Search similar proteins