1EEM

GLUTATHIONE TRANSFERASE FROM HOMO SAPIENS

Summary for 1EEM

• Entry DOI: 10.2210/pdb1eem/pdb
• Descriptor: GLUTATHIONE-S-TRANSFERASE, SULFATE ION, GLUTATHIONE, ... (4 entities in total)
• Functional Keywords: gst, glutathione conjugating, putative oxidoreductase, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytosol : P78417
• Total number of polymer chains: 1
• Total formula weight: 28099.30

Authors

Board, P.,Coggan, M.,Chelvanayagam, G.,Easteal, S.,Jermiin, L.S.,Schulte, G.K.,Danley, D.E.,Hoth, L.R.,Griffor, M.C.,Kamath, A.V.,Rosner, M.H.,Chrunyk, B.A.,Perregaux, D.E.,Gabel, C.A.,Geoghegan, K.F.,Pandit, J. (deposition date: 2000-02-01, release date: 2000-08-11, Last modification date: 2018-04-04)

Primary citation

Board, P.G.,Coggan, M.,Chelvanayagam, G.,Easteal, S.,Jermiin, L.S.,Schulte, G.K.,Danley, D.E.,Hoth, L.R.,Griffor, M.C.,Kamath, A.V.,Rosner, M.H.,Chrunyk, B.A.,Perregaux, D.E.,Gabel, C.A.,Geoghegan, K.F.,Pandit, J.
Identification, characterization, and crystal structure of the Omega class glutathione transferases.
J.Biol.Chem., 275:24798-24806, 2000

PubMed Abstract: A new class of glutathione transferases has been discovered by analysis of the expressed sequence tag data base and sequence alignment. Glutathione S-transferases (GSTs) of the new class, named Omega, exist in several mammalian species and Caenorhabditis elegans. In humans, GSTO 1-1 is expressed in most tissues and exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities characteristic of the glutaredoxins. The structure of GSTO 1-1 has been determined at 2.0-A resolution and has a characteristic GST fold (Protein Data Bank entry code ). The Omega class GSTs exhibit an unusual N-terminal extension that abuts the C terminus to form a novel structural unit. Unlike other mammalian GSTs, GSTO 1-1 appears to have an active site cysteine that can form a disulfide bond with glutathione.

PubMed: 10783391
DOI: 10.1074/jbc.M001706200

Experimental method

X-RAY DIFFRACTION (2 Å)