1pn9
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=GTX:S-HEXYLGLUTATHIONE'>GTX</scene> | |LIGAND= <scene name='pdbligand=GTX:S-HEXYLGLUTATHIONE'>GTX</scene> | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </span> |
|GENE= GST1-6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7165 Anopheles gambiae]) | |GENE= GST1-6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7165 Anopheles gambiae]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pn9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pn9 OCA], [http://www.ebi.ac.uk/pdbsum/1pn9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pn9 RCSB]</span> | ||
}} | }} | ||
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[[Category: Ranson, H.]] | [[Category: Ranson, H.]] | ||
[[Category: Zhou, X E.]] | [[Category: Zhou, X E.]] | ||
| - | [[Category: GTX]] | ||
[[Category: protein inhibitor complex]] | [[Category: protein inhibitor complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:01:58 2008'' |
Revision as of 20:02, 30 March 2008
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| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | GST1-6 (Anopheles gambiae) | ||||||
| Activity: | Glutathione transferase, with EC number 2.5.1.18 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of an insect delta-class glutathione S-transferase from a DDT-resistant strain of the malaria vector Anopheles gambiae
Overview
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.
About this Structure
1PN9 is a Single protein structure of sequence from Anopheles gambiae. Full crystallographic information is available from OCA.
Reference
Structure of an insect delta-class glutathione S-transferase from a DDT-resistant strain of the malaria vector Anopheles gambiae., Chen L, Hall PR, Zhou XE, Ranson H, Hemingway J, Meehan EJ, Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2211-7. Epub 2003, Nov 27. PMID:14646079
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