1PGP
CRYSTALLOGRAPHIC STUDY OF COENZYME, COENZYME ANALOGUE AND SUBSTRATE BINDING IN 6-PHOSPHOGLUCONATE DEHYDROGENASE: IMPLICATIONS FOR NADP SPECIFICITY AND THE ENZYME MECHANISM
1PGP の概要
エントリーDOI | 10.2210/pdb1pgp/pdb |
関連するPDBエントリー | 1PGN 1PGO 1PGQ 2PGD |
分子名称 | 6-PHOSPHOGLUCONATE DEHYDROGENASE, 6-PHOSPHOGLUCONIC ACID, SULFATE ION, ... (4 entities in total) |
機能のキーワード | oxidoreductase (choh(d)-nadp+(a)) |
由来する生物種 | Ovis aries (sheep) |
細胞内の位置 | Cytoplasm : P00349 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 53277.85 |
構造登録者 | Adams, M.J.,Phillips, C.,Gover, S.,Naylor, C.E. (登録日: 1994-07-18, 公開日: 1995-02-27, 最終更新日: 2024-02-14) |
主引用文献 | Adams, M.J.,Ellis, G.H.,Gover, S.,Naylor, C.E.,Phillips, C. Crystallographic study of coenzyme, coenzyme analogue and substrate binding in 6-phosphogluconate dehydrogenase: implications for NADP specificity and the enzyme mechanism. Structure, 2:651-668, 1994 Cited by PubMed Abstract: The nicotinamide adenine dinucleotide phosphate (NADP)-dependent oxidative decarboxylase, 6-phosphogluconate dehydrogenase, is a major source of reduced coenzyme for synthesis. Enzymes later in the pentose phosphate pathway convert the reaction product, ribulose 5-phosphate, to ribose 5-phosphate. Crystallographic study of complexes with coenzyme and substrate explain the NADP dependence which determines the enzyme's metabolic role and support the proposed general base-general acid mechanism. PubMed: 7922042DOI: 10.1016/S0969-2126(00)00066-6 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.5 Å) |
構造検証レポート
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