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1guh

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[[Image:1guh.gif|left|200px]]<br /><applet load="1guh" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1guh.gif|left|200px]]
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caption="1guh, resolution 2.6&Aring;" />
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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'''<br />
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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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|SITE=
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|LIGAND= <scene name='pdbligand=GSB:S-BENZYL-GLUTATHIONE'>GSB</scene>
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|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]
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|GENE=
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}}
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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'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1GUH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=GSB:'>GSB</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GUH OCA].
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1GUH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GUH OCA].
==Reference==
==Reference==
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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., 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8331657 8331657]
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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., 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:[http://www.ncbi.nlm.nih.gov/pubmed/8331657 8331657]
[[Category: Glutathione transferase]]
[[Category: Glutathione transferase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: transferase(glutathione)]]
[[Category: transferase(glutathione)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:54:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:28:03 2008''

Revision as of 09:28, 20 March 2008


PDB ID 1guh

Drag the structure with the mouse to rotate
, resolution 2.6Å
Ligands:
Activity: Glutathione transferase, with EC number 2.5.1.18
Coordinates: save as pdb, mmCIF, xml



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

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