› 3gth

X-ray diffraction
1.98Å resolution

D71G/E101G/M234I mutant in organophosphorus hydrolase from Deinococcus radiodurans

Released:
DOI: 10.2210/pdb3gth/pdb
PDB entry 3gth coloured by chain, front view.
PDB entry 3gth coloured by chain, side view.
PDB entry 3gth coloured by chain, top view.
Source organism: Deinococcus radiodurans
Primary publication:
Structure-based and random mutagenesis approaches increase the organophosphate-degrading activity of a phosphotriesterase homologue from Deinococcus radiodurans.
Hawwa R, Larsen SD, Ratia K, Mesecar AD
J Mol Biol 393 36-57 (2009)
PMID: 19631223

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
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: 337 amino acids
Theoretical weight: 36.15 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

2 bound ligands:
Ligand FMT 3 x FMT
Ligand CO 2 x CO
1 modified residue:
Ligand KCX 1 x KCX

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P3121
Unit cell:
a: 60.7Å b: 60.7Å c: 205Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.354 0.207 0.249
Expression system: Escherichia coli

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Citations

6 review citations

Enzyme promiscuity: a mechanistic and evolutionary perspective.
Khersonsky et al. (2010)
5 more