Structure analysis

Structure of diisopropyl fluorophosphatase (DFPase), mutant D229N / N175D

X-ray diffraction
2Å resolution
Source organism: Loligo vulgaris
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 13145.89 Å2
Buried surface area: 183.43 Å2
Dissociation area: 46.51 Å2
Dissociation energy (ΔGdiss): 10.32 kcal/mol
Dissociation entropy (TΔSdiss): 0.05 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-181980

Macromolecules

Chain: A
Length: 314 amino acids
Theoretical weight: 35.12 KDa
Source organism: Loligo vulgaris
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7SIG4 (Residues: 1-314; Coverage: 100%)
Pfam: SMP-30/Gluconolactonase/LRE-like region
InterPro:
CATH: TolB, C-terminal domain

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