› 3li4

X-ray diffraction
1.35Å resolution

Diisopropyl fluorophosphatase (DFPase), N120D,N175D,D229N mutant

Released:
DOI: 10.2210/pdb3li4/pdb
PDB entry 3li4 coloured by chain, front view.
PDB entry 3li4 coloured by chain, side view.
PDB entry 3li4 coloured by chain, top view.
Source organism: Loligo vulgaris
Primary publication:
Structural characterization of the catalytic calcium-binding site in diisopropyl fluorophosphatase (DFPase)--comparison with related beta-propeller enzymes.
Blum MM, Chen JC
Chem Biol Interact 187 373-9 (2010)
PMID: 20206152

Function and Biology Details

Biochemical function:
Biological process:
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: 314 amino acids
Theoretical weight: 35.12 KDa
Source organism: Loligo vulgaris
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7SIG4 (Residues: 1-314; Coverage: 100%)
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: ESRF BEAMLINE BM30A
Spacegroup: P212121
Unit cell:
a: 42.7Å b: 81.4Å c: 86.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.214 0.232
Expression system: Escherichia coli

Quick links

Citations

7 review citations

New insights about enzyme evolution from large scale studies of sequence and structure relationships.
Brown et al. (2014)
6 more