1gss
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1gss.gif|left|200px]] | + | [[Image:1gss.gif|left|200px]] |
| - | + | ||
| - | '''THREE-DIMENSIONAL STRUCTURE OF CLASS PI GLUTATHIONE S-TRANSFERASE FROM HUMAN PLACENTA IN COMPLEX WITH S-HEXYLGLUTATHIONE AT 2.8 ANGSTROMS RESOLUTION''' | + | {{Structure |
| + | |PDB= 1gss |SIZE=350|CAPTION= <scene name='initialview01'>1gss</scene>, resolution 2.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THREE-DIMENSIONAL STRUCTURE OF CLASS PI GLUTATHIONE S-TRANSFERASE FROM HUMAN PLACENTA IN COMPLEX WITH S-HEXYLGLUTATHIONE AT 2.8 ANGSTROMS RESOLUTION''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1GSS is a [ | + | 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]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/1522586 1522586] |
[[Category: Glutathione transferase]] | [[Category: Glutathione transferase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 22: | Line 31: | ||
[[Category: transferase(glutathione)]] | [[Category: transferase(glutathione)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:27:23 2008'' |
Revision as of 09:27, 20 March 2008
| |||||||
| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | Glutathione transferase, with EC number 2.5.1.18 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THREE-DIMENSIONAL STRUCTURE OF CLASS PI GLUTATHIONE S-TRANSFERASE FROM HUMAN PLACENTA IN COMPLEX WITH S-HEXYLGLUTATHIONE AT 2.8 ANGSTROMS RESOLUTION
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
1GSS is a Single protein structure of sequence from [1]. 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 Thu Mar 20 11:27:23 2008
