PDBe 1e1a

X-ray diffraction
1.8Å resolution

Crystal structure of DFPase from Loligo vulgaris

Released:

Function and Biology Details

Reaction catalysed:
Diisopropyl fluorophosphate + H(2)O = diisopropyl phosphate + fluoride. 
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Diisopropyl-fluorophosphatase Chain: A
Molecule details ›
Chain: A
Length: 314 amino acids
Theoretical weight: 35.12 KDa
Source organism: Loligo vulgaris
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q7SIG4 (Residues: 1-314; Coverage: 100%)
Sequence domains: SMP-30/Gluconolaconase/LRE-like region
Structure domains: TolB, C-terminal domain

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P212121
Unit cell:
a: 42.9Å b: 81.7Å c: 86.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.176 0.218
Expression system: Escherichia coli BL21