5EKW: A. Thaliana Igpd2 In Complex With The Racemate Of The Triazole- Phosphonate Inhibitor, C348

Citation:
Abstract
Programs of drug discovery generally exploit one enantiomer of a chiral compound for lead development following the principle that enantiomer recognition is central to biological specificity. However, chiral promiscuity has been identified for a number of enzyme families, which have shown that mirror-image packing can enable opposite enantiomers to be accommodated in an enzyme's active site. Reported here is a series of crystallographic studies of complexes between an enzyme and a potent experimental herbicide whose chiral center forms an essential part of the inhibitor pharmacophore. Initial studies with a racemate at 1.85 A resolution failed to identify the chirality of the bound inhibitor, however, by extending the resolution to 1.1 A and by analyzing high-resolution complexes with the enantiopure compounds, we determined that both enantiomers make equivalent pseudosymmetric interactions in the active site, thus mimicking an achiral reaction intermediate.
PDB ID: 5EKWDownload
MMDB ID: 143711
PDB Deposition Date: 2015/11/4
Updated in MMDB: 2016/10
Experimental Method:
x-ray diffraction
Resolution: 1.1  Å
Source Organism:
Similar Structures:
Biological Unit for 5EKW: 24-meric; determined by author and by software (PISA)
Molecular Components in 5EKW
Label Count Molecule
Proteins (24 molecules)
24
Imidazoleglycerol-phosphate Dehydratase 2, Chloroplastic(Gene symbol: HISN5B)
Molecule annotation
Chemicals (257 molecules)
1
24
2
24
3
141
4
44
5
24
* Click molecule labels to explore molecular sequence information.

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