› 4j2m

X-ray diffraction
1.79Å resolution

Molecular Engineering of Organophosphate Hydrolysis Activity from a Weak Promiscuous Lactonase Template

Released:
DOI: 10.2210/pdb4j2m/pdb
PDB entry 4j2m coloured by chain, front view.
PDB entry 4j2m coloured by chain, side view.
PDB entry 4j2m coloured by chain, top view.
Source organism: Deinococcus radiodurans
Primary publication:
Molecular engineering of organophosphate hydrolysis activity from a weak promiscuous lactonase template.
Meier MM, Rajendran C, Malisi C, Fox NG, Xu C, Schlee S, Barondeau DP, Höcker B, Sterner R, Raushel FM
J Am Chem Soc 135 11670-7 (2013)
PMID: 23837603

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-193304 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphotriesterase, putative Chain: A
Molecule details ›
Chain: A
Length: 323 amino acids
Theoretical weight: 34.69 KDa
Source organism: Deinococcus radiodurans
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9RVU2 (Residues: 1-323; Coverage: 100%)
Gene name: DR_0930
Sequence domains: Phosphotriesterase family
Structure domains: Metal-dependent hydrolases

Ligands and Environments

1 bound ligand:
Ligand CO 2 x CO
1 modified residue:
Ligand KCX 1 x KCX

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P3121
Unit cell:
a: 61.779Å b: 61.779Å c: 203.707Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.221 0.22 0.25
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Expanding the enzyme universe: accessing non-natural reactions by mechanism-guided directed evolution.
Renata et al. (2015)
7 more

1 mention without citation

Molecular engineering of organophosphate hydrolysis activity from a weak promiscuous lactonase template.
Meier et al. (2013)