› 1e1a

X-ray diffraction
1.8Å resolution

Crystal structure of DFPase from Loligo vulgaris

Released:
DOI: 10.2210/pdb1e1a/pdb
PDB entry 1e1a coloured by chain, front view.
PDB entry 1e1a coloured by chain, side view.
PDB entry 1e1a coloured by chain, top view.
Source organism: Loligo vulgaris
Primary publication:
Crystal structure of diisopropylfluorophosphatase from Loligo vulgaris.
Scharff EI, Koepke J, Fritzsch G, Lücke C, Rüterjans H
Structure 9 493-502 (2001)
PMID: 11435114

Function and Biology Details

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

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 BL21
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: 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

Quick links

Citations

14 review citations

Emergence of diverse biochemical activities in evolutionarily conserved structural scaffolds of proteins.
Anantharaman et al. (2003)
13 more

13 mentions without citation

A mechanistic view of enzyme evolution.
Yang et al. (2020)
12 more