1gss: Difference between revisions

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[[Image:1gss.gif|left|200px]]
[[Image:1gss.gif|left|200px]]


{{Structure
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|LIGAND= <scene name='pdbligand=SHC:S-HEXYLCYSTEINE'>SHC</scene>
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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_1gss| PDB=1gss  | SCENE= }}  
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gss FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gss OCA], [http://www.ebi.ac.uk/pdbsum/1gss PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gss RCSB]</span>
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'''THREE-DIMENSIONAL STRUCTURE OF CLASS PI GLUTATHIONE S-TRANSFERASE FROM HUMAN PLACENTA IN COMPLEX WITH S-HEXYLGLUTATHIONE AT 2.8 ANGSTROMS RESOLUTION'''
'''THREE-DIMENSIONAL STRUCTURE OF CLASS PI GLUTATHIONE S-TRANSFERASE FROM HUMAN PLACENTA IN COMPLEX WITH S-HEXYLGLUTATHIONE AT 2.8 ANGSTROMS RESOLUTION'''
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==About this Structure==
==About this Structure==
1GSS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GSS OCA].  
1GSS is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GSS OCA].  


==Reference==
==Reference==
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[[Category: Parker, M W.]]
[[Category: Parker, M W.]]
[[Category: Reinemer, P.]]
[[Category: Reinemer, P.]]
[[Category: transferase(glutathione)]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 17:57:50 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:50:36 2008''

Revision as of 17:57, 2 May 2008

File:1gss.gif

Template:STRUCTURE 1gss

THREE-DIMENSIONAL STRUCTURE OF CLASS PI GLUTATHIONE S-TRANSFERASE FROM HUMAN PLACENTA IN COMPLEX WITH S-HEXYLGLUTATHIONE AT 2.8 ANGSTROMS RESOLUTION


OverviewOverview

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 StructureAbout this Structure

1GSS is a Single protein structure. Full crystallographic information is available from OCA.

ReferenceReference

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 17:57:50 2008

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