1p6c

X-ray diffraction
2Å resolution

crystal structure of phosphotriesterase triple mutant H254G/H257W/L303T complexed with diisopropylmethylphosphonate

Released:

Function and Biology Details

Reaction catalysed:
An aryl dialkyl phosphate + H(2)O = dialkyl phosphate + an aryl alcohol
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Parathion hydrolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 336 amino acids
Theoretical weight: 36.33 KDa
Source organism: Flavobacterium sp.
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A433 (Residues: 30-365; Coverage: 100%)
Gene name: opd
Sequence domains: Phosphotriesterase family
Structure domains: Metal-dependent hydrolases

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 130.4Å b: 91.9Å c: 69.7Å
α: 90° β: 90.9° γ: 90°
R-values:
R R work R free
0.185 0.181 0.246
Expression system: Escherichia coli