1LBK

Crystal structure of a recombinant glutathione transferase, created by replacing the last seven residues of each subunit of the human class pi isoenzyme with the additional C-terminal helix of human class alpha isoenzyme

1LBK の概要

• エントリーDOI: 10.2210/pdb1lbk/pdb
• 分子名称: Glutathione S-transferase class pi chimaera (CODA), 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, GLUTATHIONE, ... (5 entities in total)
• 機能のキーワード: glutathione transferase p1-1, chimaera, recombinant protein, substrate specificity, transferase
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm: P08263
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47578.41

構造登録者

Kong, G.K.W.,Micaloni, C.,Mazzetti, A.P.,Nuccetelli, M.,Antonini, G.,Stella, L.,McKinstry, W.J.,Polekhina, G.,Rossjohn, J.,Federici, G.,Ricci, G.,Parker, M.W.,Lo Bello, M. (登録日: 2002-04-04, 公開日: 2002-04-17, 最終更新日: 2023-08-16)

• 主引用文献: Micaloni, C.,Kong, G.K.W.,Mazzetti, A.P.,Nuccetelli, M.,Antonini, G.,Stella, L.,McKinstry, W.J.,Polekhina, G.,Rossjohn, J.,Federici, G.,Ricci, G.,Parker, M.W.,Lo Bello, M.; Engineering a new C-terminal tail in the H-site of human glutathione transferase P1-1: structural and functional consequences.; J.Mol.Biol., 325:111-122, 2003; PubMed: 12473455; DOI: 10.1016/S0022-2836(02)01178-6

実験手法

X-RAY DIFFRACTION (1.86 Å)