Structure analysis

Crystal structure of mouse poly(ADP-ribose) glycohydrolase (PARG) catalytic domain mutant E749Q

X-ray diffraction
1.9Å resolution
Source organism: Mus musculus
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 22403.16 Å2
Buried surface area: 819.9 Å2
Dissociation area: 40.88 Å2
Dissociation energy (ΔGdiss): 3.89 kcal/mol
Dissociation entropy (TΔSdiss): 0.6 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-131568
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 22373.22 Å2
Buried surface area: 801.99 Å2
Dissociation area: 41.11 Å2
Dissociation energy (ΔGdiss): 3.88 kcal/mol
Dissociation entropy (TΔSdiss): 0.6 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-131568

Macromolecules

Chains: A, B
Length: 522 amino acids
Theoretical weight: 60.15 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: O88622 (Residues: 439-959; Coverage: 54%)
Gene name: Parg
Pfam:
InterPro:

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