1N1G

Crystal structure of Leishmania mexicana Glycerol-3-phosphate dehydrogenase with inhibitor BCP

Summary for 1N1G

• Entry DOI: 10.2210/pdb1n1g/pdb
• Related: 1JDJ 1M66 1M67 1N1E
• Descriptor: glycerol-3-phosphate dehydrogenase, 2-BROMO-6-CHLORO-PURINE, PALMITIC ACID, ... (4 entities in total)
• Functional Keywords: nad binding domain, oxidoreductase
• Biological source: Leishmania mexicana
• Cellular location: Glycosome: P90551
• Total number of polymer chains: 1
• Total formula weight: 40274.61

Authors

Choe, J.,Hol, W.G. (deposition date: 2002-10-17, release date: 2003-10-28, Last modification date: 2024-02-14)

Primary citation

Choe, J.,Suresh, S.,Wisedchaisri, G.,Kennedy, K.J.,Gelb, M.H.,Hol, W.G.
Anomalous differences of light elements in determining precise binding modes of ligands to glycerol-3-phosphate dehydrogenase.
Chem.Biol., 9:1189-1197, 2002

PubMed Abstract: Pathogenic protozoa such as Trypanosome and Leishmania species cause tremendous suffering worldwide. Because of their dependence on glycolysis for energy, the glycolytic enzymes of these organisms, including glycerol-3-phosphate dehydrogenase (GPDH), are considered attractive drug targets. Using the adenine part of NAD as a lead compound, several 2,6-disubstituted purines were synthesized as inhibitors of Leishmania mexicana GPDH (LmGPDH). The electron densities for the inhibitor 2-bromo-6-chloro-purine bound to LmGPDH using a "conventional" wavelength around 1 A displayed a quasisymmetric shape. The anomalous signals from data collected at 1.77 A clearly indicated the positions of the halogen atoms and revealed the multiple binding modes of this inhibitor. Intriguing differences in the observed binding modes of the inhibitor between very similarly prepared crystals illustrate the possibility of crystal-to-crystal variations in protein-ligand complex structures.

PubMed: 12445769
DOI: 10.1016/S1074-5521(02)00243-0

Experimental method

X-RAY DIFFRACTION (2.5 Å)