› 2iav

X-ray diffraction
1.07Å resolution

Crystal structure of squid ganglion DFPase H287A mutant

Released:
DOI: 10.2210/pdb2iav/pdb
PDB entry 2iav coloured by chain, front view.
PDB entry 2iav coloured by chain, side view.
PDB entry 2iav coloured by chain, top view.
Source organism: Loligo vulgaris
Primary publication:
Mutational and structural studies of the diisopropylfluorophosphatase from Loligo vulgaris shed new light on the catalytic mechanism of the enzyme.
Katsemi V, Lücke C, Koepke J, Löhr F, Maurer S, Fritzsch G, Rüterjans H
Biochemistry 44 9022-33 (2005)
PMID: 15966726

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181980 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Diisopropyl-fluorophosphatase Chain: A
Molecule details ›
Chain: A
Length: 312 amino acids
Theoretical weight: 34.79 KDa
Source organism: Loligo vulgaris
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q7SIG4 (Residues: 3-314; Coverage: 99%)
Sequence domains: SMP-30/Gluconolactonase/LRE-like region
Structure domains: TolB, C-terminal domain

Ligands and Environments

1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P212121
Unit cell:
a: 43.07Å b: 81.996Å c: 86.627Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.182 0.196
Expression system: Escherichia coli BL21

Quick links

Citations

7 review citations

Catalytic mechanisms for phosphotriesterases.
Bigley et al. (2013)
6 more

1 mention without citation

Similar Active Sites and Mechanisms Do Not Lead to Cross-Promiscuity in Organophosphate Hydrolysis: Implications for Biotherapeutic Engineering.
Purg et al. (2017)