1CQE
PROSTAGLANDIN H2 SYNTHASE-1 COMPLEX WITH FLURBIPROFEN
1CQE の概要
| エントリーDOI | 10.2210/pdb1cqe/pdb |
| 分子名称 | PROTEIN (PROSTAGLANDIN H2 SYNTHASE-1), 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, octyl beta-D-glucopyranoside, ... (6 entities in total) |
| 機能のキーワード | oxidoreductase, dioxygenase, peroxidase |
| 由来する生物種 | Ovis aries (sheep) |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 138920.39 |
| 構造登録者 | Picot, D.,Loll, P.J.,Mulichak, A.M.,Garavito, R.M. (登録日: 1999-06-15, 公開日: 1999-06-30, 最終更新日: 2024-10-16) |
| 主引用文献 | Picot, D.,Loll, P.J.,Garavito, R.M. The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1. Nature, 367:243-249, 1994 Cited by PubMed Abstract: The three-dimensional structure of prostaglandin H2 synthase-1, an integral membrane protein, has been determined at 3.5 A resolution by X-ray crystallography. This bifunctional enzyme comprises three independent folding units: an epidermal growth factor domain, a membrane-binding motif and an enzymatic domain. Two adjacent but spatially distinct active sites were found for its haem-dependent peroxidase and cyclooxygenase activities. The cyclooxygenase active site is created by a long, hydrophobic channel that is the site of non-steroidal anti-inflammatory drug binding. The conformation of the membrane-binding motif strongly suggests that the enzyme integrates into only one leaflet of the lipid bilayer and is thus a monotopic membrane protein. PubMed: 8121489DOI: 10.1038/367243a0 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.1 Å) |
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