1guh

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[[Image:1guh.gif|left|200px]]
[[Image:1guh.gif|left|200px]]
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{{Structure
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|PDB= 1guh |SIZE=350|CAPTION= <scene name='initialview01'>1guh</scene>, resolution 2.6&Aring;
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The line below this paragraph, containing "STRUCTURE_1guh", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=GSB:S-BENZYL-GLUTATHIONE'>GSB</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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{{STRUCTURE_1guh| PDB=1guh | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1guh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1guh OCA], [http://www.ebi.ac.uk/pdbsum/1guh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1guh RCSB]</span>
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'''STRUCTURE DETERMINATION AND REFINEMENT OF HUMAN ALPHA CLASS GLUTATHIONE TRANSFERASE A1-1, AND A COMPARISON WITH THE MU AND PI CLASS ENZYMES'''
'''STRUCTURE DETERMINATION AND REFINEMENT OF HUMAN ALPHA CLASS GLUTATHIONE TRANSFERASE A1-1, AND A COMPARISON WITH THE MU AND PI CLASS ENZYMES'''
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[[Category: Kleywegt, G J.]]
[[Category: Kleywegt, G J.]]
[[Category: Sinning, I.]]
[[Category: Sinning, I.]]
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[[Category: transferase(glutathione)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:51:33 2008''
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Revision as of 15:01, 2 May 2008

Template:STRUCTURE 1guh

STRUCTURE DETERMINATION AND REFINEMENT OF HUMAN ALPHA CLASS GLUTATHIONE TRANSFERASE A1-1, AND A COMPARISON WITH THE MU AND PI CLASS ENZYMES


Overview

The crystal structure of human alpha class glutathione transferase A1-1 has been determined and refined to a resolution of 2.6 A. There are two copies of the dimeric enzyme in the asymmetric unit. Each monomer is built from two domains. A bound inhibitor, S-benzyl-glutathione, is primarily associated with one of these domains via a network of hydrogen bonds and salt-links. In particular, the sulphur atom of the inhibitor forms a hydrogen bond to the hydroxyl group of Tyr9 and the guanido group of Arg15. The benzyl group of the inhibitor is completely buried in a hydrophobic pocket. The structure shows an overall similarity to the mu and pi class enzymes particularly in the glutathione-binding domain". The main difference concerns the extended C terminus of the alpha class enzyme which forms an extra alpha-helix that blocks one entrance to the active site and makes up part of the substrate binding site.

About this Structure

1GUH is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes., Sinning I, Kleywegt GJ, Cowan SW, Reinemer P, Dirr HW, Huber R, Gilliland GL, Armstrong RN, Ji X, Board PG, et al., J Mol Biol. 1993 Jul 5;232(1):192-212. PMID:8331657 Page seeded by OCA on Fri May 2 18:01:26 2008

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