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1EEM

GLUTATHIONE TRANSFERASE FROM HOMO SAPIENS

1EEM の概要
エントリーDOI10.2210/pdb1eem/pdb
分子名称GLUTATHIONE-S-TRANSFERASE, SULFATE ION, GLUTATHIONE, ... (4 entities in total)
機能のキーワードgst, glutathione conjugating, putative oxidoreductase, transferase
由来する生物種Homo sapiens (human)
細胞内の位置Cytoplasm, cytosol : P78417
タンパク質・核酸の鎖数1
化学式量合計28099.30
構造登録者
主引用文献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
Cited by
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
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2 Å)
構造検証レポート
Validation report summary of 1eem
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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