- PDB-1fbg: CRYSTALLOGRAPHIC STUDIES OF THE CATALYTIC MECHANISM OF THE NEUTRA... -
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基本情報
登録情報
データベース: PDB / ID: 1fbg
タイトル
CRYSTALLOGRAPHIC STUDIES OF THE CATALYTIC MECHANISM OF THE NEUTRAL FORM OF FRUCTOSE-1,6-BISPHOSPHATASE
要素
FRUCTOSE 1,6-BISPHOSPHATASEフルクトース-1,6-ビスホスファターゼ
キーワード
HYDROLASE(PHOSPHORIC MONOESTER)
機能・相同性
機能・相同性情報
糖新生 / sucrose biosynthetic process / fructose-bisphosphatase / fructose 1,6-bisphosphate 1-phosphatase activity / cellular response to magnesium ion / negative regulation of Ras protein signal transduction / fructose 6-phosphate metabolic process / fructose metabolic process / fructose 1,6-bisphosphate metabolic process / monosaccharide binding ...糖新生 / sucrose biosynthetic process / fructose-bisphosphatase / fructose 1,6-bisphosphate 1-phosphatase activity / cellular response to magnesium ion / negative regulation of Ras protein signal transduction / fructose 6-phosphate metabolic process / fructose metabolic process / fructose 1,6-bisphosphate metabolic process / monosaccharide binding / negative regulation of glycolytic process / regulation of gluconeogenesis / AMP binding / 脱リン酸化 / 糖新生 / negative regulation of cell growth / cellular response to xenobiotic stimulus / identical protein binding / metal ion binding / 細胞質基質 / 細胞質 類似検索 - 分子機能
フルクトース-1,6-ビスホスファターゼ / Fructose-1,6-bisphosphatase, active site / Fructose-1-6-bisphosphatase class 1, C-terminal / Fructose-1-6-bisphosphatase active site. / Fructose-1,6-bisphosphatase class 1 / Fructose-1-6-bisphosphatase class I, N-terminal / Fructose-1-6-bisphosphatase, N-terminal domain / Fructose-1-6-bisphosphatase, C-terminal domain / D-Maltodextrin-Binding Protein; domain 2 - #80 / Fructose-1,6-Bisphosphatase, subunit A, domain 1 ...フルクトース-1,6-ビスホスファターゼ / Fructose-1,6-bisphosphatase, active site / Fructose-1-6-bisphosphatase class 1, C-terminal / Fructose-1-6-bisphosphatase active site. / Fructose-1,6-bisphosphatase class 1 / Fructose-1-6-bisphosphatase class I, N-terminal / Fructose-1-6-bisphosphatase, N-terminal domain / Fructose-1-6-bisphosphatase, C-terminal domain / D-Maltodextrin-Binding Protein; domain 2 - #80 / Fructose-1,6-Bisphosphatase, subunit A, domain 1 / Fructose-1,6-Bisphosphatase; Chain A, domain 1 / D-Maltodextrin-Binding Protein; domain 2 / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Alpha Beta 類似検索 - ドメイン・相同性
THE WHOLE MOLECULE IS A TETRAMER OF FOUR IDENTICAL CHAINS. THE OTHER HALF OF THE MOLECULE IS RELATED TO THE A + B DIMER BY A CRYSTALLOGRAPHIC TWO-FOLD OPERATION (Y, X, -Z). THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL YIELD APPROXIMATE COORDINATES FOR CHAIN A WHEN APPLIED TO CHAIN B.
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要素
#1: タンパク質
FRUCTOSE1,6-BISPHOSPHATASE / フルクトース-1,6-ビスホスファターゼ
分子量: 36503.004 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) Sus scrofa (ブタ) / 参照: UniProt: P00636, fructose-bisphosphatase
THE SUBSTRATE ANALOGUE 2,5-ANHYDROMANNITOL-1,6-BISPHOSPHATE OCCUPIES THE ACTIVE SITE OF THE A AND B ...THE SUBSTRATE ANALOGUE 2,5-ANHYDROMANNITOL-1,6-BISPHOSPHATE OCCUPIES THE ACTIVE SITE OF THE A AND B CHAINS. THERE IS ALSO ONE MANGANESE ION AT THE ACTIVE SITE OF EACH CHAIN.