3WJ8: Crystal Structure Of Dl-2-haloacid Dehalogenase Mutant With 2-bromo-2- Methylpropionate

Several pathways of biotic dechlorination can be found in enzymes, each characterized by different chlorine isotopic fractionation, which can thus serve as a signature of a particular mechanism. Unlike other dehalogenases, DL-2-haloacid dehalogenase, DL-DEX, converts both enantiomers of the substrate. Chlorine isotope effects for this enzyme are larger than in the case of other dehalogenases. Recently, the 3D structure of this enzyme became available and enabled us to model these isotope effects and seek their origin. We show that the elevated values of the chlorine kinetic isotope effects originate in part in the processes of binding and migration within the enzyme active site that precede the dehalogenation step.
PDB ID: 3WJ8Download
MMDB ID: 115385
PDB Deposition Date: 2013/10/7
Updated in MMDB: 2013/11
Experimental Method:
x-ray diffraction
Resolution: 2.7  Å
Source Organism:
Similar Structures:
Biological Unit for 3WJ8: dimeric; determined by author and by software (PISA)
Molecular Components in 3WJ8
Label Count Molecule
Proteins (2 molecules)
Dl-2-haloacid Dehalogenase
Molecule annotation
Chemicals (6 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB