2ab6: Difference between revisions

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|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=GSM:L-GAMMA-GLUTAMYL-S-METHYLCYSTEINYLGLYCINE'>GSM</scene>
|LIGAND= <scene name='pdbligand=GSM:L-GAMMA-GLUTAMYL-S-METHYLCYSTEINYLGLYCINE'>GSM</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= GSTM2, GST4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
|GENE= GSTM2, GST4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
|DOMAIN=
|RELATEDENTRY=[[1gtu|1GTU]], [[1xw5|1XW5]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ab6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ab6 OCA], [http://www.ebi.ac.uk/pdbsum/2ab6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ab6 RCSB]</span>
}}
}}


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[[Category: Listowsky, I.]]
[[Category: Listowsky, I.]]
[[Category: Patskovsky, Y.]]
[[Category: Patskovsky, Y.]]
[[Category: GSM]]
[[Category: conjugation]]
[[Category: conjugation]]
[[Category: detoxification]]
[[Category: detoxification]]
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[[Category: transferase]]
[[Category: transferase]]


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Revision as of 01:50, 31 March 2008

File:2ab6.gif


PDB ID 2ab6

Drag the structure with the mouse to rotate
, resolution 2.50Å
Ligands:
Gene: GSTM2, GST4 (Homo sapiens)
Activity: Glutathione transferase, with EC number 2.5.1.18
Related: 1GTU, 1XW5


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



HUMAN GLUTATHIONE S-TRANSFERASE M2-2 (E.C.2.5.1.18) complexed with S-METHYLGLUTATHIONE


OverviewOverview

Human glutathione-S-transferase M2-2 (hGSTM2-2) was expressed in Escherichia coli and purified by GSH-affinity chromatography. The recombinant enzyme and the protein isolated from human tissue were indistinguishable based on physicochemical, enzymatic and immunological criteria. The catalytically active dimeric hGSTM2-2 was crystallized without GSH or other active-site ligands in two crystal forms. Diffraction from form A crystals extends to 2.5 A and is consistent with the space group P21 (a = 53.9, b = 81.5, c = 55.6 A, beta = 109.26 A) with two monomers in the asymmetric unit. Diffraction from form B crystals extends to 3 A and is consistent with a space group P212121 (a = 57.2, b = 80.7, c = 225.9 A) with two dimers in the asymmetric unit. This is the first report of ligand-free mu-class GST crystals, and a comparison with liganded complexes will provide insight into the structural consequences of substrate binding which are thought to be important for catalysis.

About this StructureAbout this Structure

2AB6 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Expression, crystallization and preliminary X-ray analysis of ligand-free human glutathione S-transferase M2-2., Patskovska LN, Fedorov AA, Patskovsky YV, Almo SC, Listowsky I, Acta Crystallogr D Biol Crystallogr. 1998 May 1;54(Pt 3):458-60. PMID:9761928

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