› 1qw7

X-ray diffraction
1.9Å resolution

Structure of an Engineered Organophosphorous Hydrolase with Increased Activity Toward Hydrolysis of Phosphothiolate Bonds

Released:
DOI: 10.2210/pdb1qw7/pdb
PDB entry 1qw7 coloured by chain, front view.
PDB entry 1qw7 coloured by chain, side view.
PDB entry 1qw7 coloured by chain, top view.
Source organism: Brevundimonas diminuta
Primary publication:
Structural and mutational studies of organophosphorus hydrolase reveal a cryptic and functional allosteric-binding site.
Grimsley JK, Calamini B, Wild JR, Mesecar AD
Arch Biochem Biophys 442 169-79 (2005)
PMID: 16188223

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141251 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Parathion hydrolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 336 amino acids
Theoretical weight: 36.39 KDa
Source organism: Brevundimonas diminuta
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A434 (Residues: 30-365; Coverage: 100%)
Gene name: opd
Sequence domains: Phosphotriesterase family
Structure domains: Metal-dependent hydrolases

Ligands and Environments

3 bound ligands:
Ligand CO 4 x CO
Ligand NA 2 x NA
Ligand EBP 2 x EBP
1 modified residue:
Ligand KCX 2 x KCX

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: C2
Unit cell:
a: 126.719Å b: 89.879Å c: 68.337Å
α: 90° β: 91.73° γ: 90°
R-values:
R R work R free
0.179 0.179 0.23
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Organophosphorus Nerve Agents: Types, Toxicity, and Treatments.
Mukherjee et al. (2020)
1 more

8 mentions without citation

Enzymes for Detoxification of Various Mycotoxins: Origins and Mechanisms of Catalytic Action.
Lyagin et al. (2019)
7 more