1GUH

Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the MU and PI class enzymes

Summary for 1GUH

• Entry DOI: 10.2210/pdb1guh/pdb
• Descriptor: GLUTATHIONE S-TRANSFERASE A1-1, S-BENZYL-GLUTATHIONE (2 entities in total)
• Functional Keywords: glutathione transferase, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P08263
• Total number of polymer chains: 4
• Total formula weight: 103745.48

Authors

Sinning, I.,Kleywegt, G.J.,Jones, T.A. (deposition date: 1993-02-24, release date: 1993-10-31, Last modification date: 2024-02-07)

Primary citation

Sinning, I.,Kleywegt, G.J.,Cowan, S.W.,Reinemer, P.,Dirr, H.W.,Huber, R.,Gilliland, G.L.,Armstrong, R.N.,Ji, X.,Board, P.G.,Olin, B.,Mannervik, B.,Jones, T.A.
Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes.
J.Mol.Biol., 232:192-212, 1993

PubMed Abstract: 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.

PubMed: 8331657
DOI: 10.1006/jmbi.1993.1376

Experimental method

X-RAY DIFFRACTION (2.6 Å)