1eem
From Proteopedia
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|PDB= 1eem |SIZE=350|CAPTION= <scene name='initialview01'>1eem</scene>, resolution 2.00Å | |PDB= 1eem |SIZE=350|CAPTION= <scene name='initialview01'>1eem</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eem OCA], [http://www.ebi.ac.uk/pdbsum/1eem PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1eem RCSB]</span> | ||
}} | }} | ||
| Line 38: | Line 41: | ||
[[Category: Rosner, M H.]] | [[Category: Rosner, M H.]] | ||
[[Category: Schulte, G K.]] | [[Category: Schulte, G K.]] | ||
| - | [[Category: GSH]] | ||
| - | [[Category: SO4]] | ||
[[Category: glutathione conjugating]] | [[Category: glutathione conjugating]] | ||
[[Category: gst]] | [[Category: gst]] | ||
[[Category: putative oxidoreductase]] | [[Category: putative oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:01:05 2008'' |
Revision as of 17:01, 30 March 2008
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| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
GLUTATHIONE TRANSFERASE FROM HOMO SAPIENS
Overview
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.
About this Structure
1EEM is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Identification, characterization, and crystal structure of the Omega class glutathione transferases., Board PG, Coggan M, Chelvanayagam G, Easteal S, Jermiin LS, Schulte GK, Danley DE, Hoth LR, Griffor MC, Kamath AV, Rosner MH, Chrunyk BA, Perregaux DE, Gabel CA, Geoghegan KF, Pandit J, J Biol Chem. 2000 Aug 11;275(32):24798-806. PMID:10783391
Page seeded by OCA on Sun Mar 30 20:01:05 2008
Categories: Homo sapiens | Single protein | Board, P. | Chelvanayagam, G. | Chrunyk, B A. | Coggan, M. | Danley, D E. | Easteal, S. | Gabel, C A. | Geoghegan, K F. | Griffor, M C. | Hoth, L R. | Jermiin, L S. | Kamath, A V. | Pandit, J. | Perregaux, D E. | Rosner, M H. | Schulte, G K. | Glutathione conjugating | Gst | Putative oxidoreductase
