1aqv

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[[Image:1aqv.gif|left|200px]]
[[Image:1aqv.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1aqv |SIZE=350|CAPTION= <scene name='initialview01'>1aqv</scene>, resolution 1.94&Aring;
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The line below this paragraph, containing "STRUCTURE_1aqv", 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=ILG:GLUTAMYL+GROUP'>ILG</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=PBB:S-(4-BROMOBENZYL)CYSTEINE'>PBB</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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or leave the SCENE parameter empty for the default display.
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|GENE= GTP_HUMAN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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-->
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|DOMAIN=
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{{STRUCTURE_1aqv| PDB=1aqv | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1aqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aqv OCA], [http://www.ebi.ac.uk/pdbsum/1aqv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1aqv RCSB]</span>
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}}
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'''GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH P-BROMOBENZYLGLUTATHIONE'''
'''GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH P-BROMOBENZYLGLUTATHIONE'''
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[[Category: Prade, L.]]
[[Category: Prade, L.]]
[[Category: Reuter, W.]]
[[Category: Reuter, W.]]
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[[Category: class pi]]
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[[Category: Class pi]]
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[[Category: complex (transferase/peptide)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:36:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:45:47 2008''
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Revision as of 07:36, 2 May 2008

Image:1aqv.gif

Template:STRUCTURE 1aqv

GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH P-BROMOBENZYLGLUTATHIONE


Overview

The three-dimensional structure of human class pi glutathione S-transferase from placenta (hGSTP1-1), a homodimeric enzyme, has been solved by Patterson search methods and refined at 2.8 A resolution to a final crystallographic R-factor of 19.6% (8.0 to 2.8 A resolution). Subunit folding topology, subunit overall structure and subunit association closely resembles the structure of porcine class pi glutathione S-transferase. The binding site of a competitive inhibitor, S-hexylglutathione, is analyzed and the locations of the binding regions for glutathione (G-site) and electrophilic substrates (H-site) are determined. The specific interactions between protein and the inhibitor's glutathione peptide are the same as those observed between glutathione sulfonate and the porcine isozyme. The H-site is located adjacent to the G-site, with the hexyl moiety lying above a segment (residues 8 to 10) connecting strand beta 1 and helix alpha A where it is in hydrophobic contact with Tyr7, Phe8, Val10, Val35 and Tyr106. Catalytic models are discussed on the basis of the molecular structure.

About this Structure

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

Reference

Three-dimensional structure of class pi glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 A resolution., Reinemer P, Dirr HW, Ladenstein R, Huber R, Lo Bello M, Federici G, Parker MW, J Mol Biol. 1992 Sep 5;227(1):214-26. PMID:1522586 Page seeded by OCA on Fri May 2 10:36:00 2008

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OCA

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