Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1PN9

Crystal structure of an insect delta-class glutathione S-transferase from a DDT-resistant strain of the malaria vector Anopheles gambiae

Summary for 1PN9
Entry DOI10.2210/pdb1pn9/pdb
DescriptorGlutathione S-transferase 1-6, S-HEXYLGLUTATHIONE (3 entities in total)
Functional Keywordsprotein inhibitor complex, transferase
Biological sourceAnopheles gambiae (African malaria mosquito)
Total number of polymer chains2
Total formula weight47724.47
Authors
Chen, L.,Hall, P.R.,Zhou, X.E.,Ranson, H.,Hemingway, J.,Meehan, E.J. (deposition date: 2003-06-12, release date: 2003-12-09, Last modification date: 2024-04-03)
Primary citationChen, L.,Hall, P.R.,Zhou, X.E.,Ranson, H.,Hemingway, J.,Meehan, E.J.
Structure of an insect delta-class glutathione S-transferase from a DDT-resistant strain of the malaria vector Anopheles gambiae.
Acta Crystallogr.,Sect.D, 59:2211-2217, 2003
Cited by
PubMed Abstract: Glutathione S-transferases (GSTs) are a major family of detoxification enzymes which possess a wide range of substrate specificities. Most organisms possess many GSTs belonging to multiple classes. Interest in GSTs in insects is focused on their role in insecticide resistance; many resistant insects have elevated levels of GST activity. In the malaria vector Anopheles gambiae, elevated GST levels are associated with resistance to the organochlorine insecticide DDT [1,1,1-trichloro-2,2-bis-(p-chlorophenyl)ethane]. This mosquito is the source of an insect GST, agGSTd1-6, which metabolizes DDT and is inhibited by a number of pyrethroid insecticides. The crystal structure of agGSTd1-6 in complex with its inhibitor S-hexyl glutathione has been determined and refined at 2.0 A resolution. The structure adopts a classical GST fold and is similar to those of other insect delta-class GSTs, implying a common conjugation mechanism. A structure-based model for the binding of DDT to agGSTd1-6 reveals two subpockets in the hydrophobic binding site (H-site), each accommodating one planar p-chlorophenyl ring.
PubMed: 14646079
DOI: 10.1107/S0907444903018493
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

239149

PDB entries from 2025-07-23

PDB statisticsPDBj update infoContact PDBjnumon