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データを開く
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基本情報
登録情報 | データベース: PDB / ID: 3ins | ||||||
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タイトル | STRUCTURE OF INSULIN. RESULTS OF JOINT NEUTRON AND X-RAY REFINEMENT | ||||||
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![]() | HORMONE | ||||||
機能・相同性 | ![]() Insulin processing / IRS activation / Signal attenuation / Insulin receptor signalling cascade / Signaling by Insulin receptor / Synthesis, secretion, and deacylation of Ghrelin / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / Insulin receptor recycling / glycoprotein biosynthetic process / positive regulation of lipoprotein lipase activity ...Insulin processing / IRS activation / Signal attenuation / Insulin receptor signalling cascade / Signaling by Insulin receptor / Synthesis, secretion, and deacylation of Ghrelin / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / Insulin receptor recycling / glycoprotein biosynthetic process / positive regulation of lipoprotein lipase activity / response to L-arginine / lactate biosynthetic process / positive regulation of fatty acid biosynthetic process / positive regulation of glucose metabolic process / lipoprotein biosynthetic process / COPI-mediated anterograde transport / negative regulation of glycogen catabolic process / lipid biosynthetic process / positive regulation of nitric oxide mediated signal transduction / negative regulation of fatty acid metabolic process / negative regulation of feeding behavior / positive regulation of respiratory burst / negative regulation of acute inflammatory response / positive regulation of protein autophosphorylation / alpha-beta T cell activation / positive regulation of dendritic spine maintenance / negative regulation of respiratory burst involved in inflammatory response / negative regulation of protein secretion / positive regulation of glycogen biosynthetic process / negative regulation of gluconeogenesis / fatty acid homeostasis / positive regulation of insulin receptor signaling pathway / negative regulation of lipid catabolic process / regulation of protein localization to plasma membrane / nitric oxide-cGMP-mediated signaling / negative regulation of reactive oxygen species biosynthetic process / insulin-like growth factor receptor binding / neuron projection maintenance / positive regulation of mitotic nuclear division / positive regulation of glycolytic process / positive regulation of cytokine production / acute-phase response / positive regulation of DNA replication / positive regulation of D-glucose import / positive regulation of protein secretion / insulin receptor binding / wound healing / negative regulation of protein catabolic process / hormone activity / positive regulation of protein localization to nucleus / glucose metabolic process / vasodilation / insulin receptor signaling pathway / glucose homeostasis / protease binding / positive regulation of canonical NF-kappaB signal transduction / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / positive regulation of MAPK cascade / positive regulation of cell migration / G protein-coupled receptor signaling pathway / negative regulation of gene expression / positive regulation of cell population proliferation / extracellular space / identical protein binding 類似検索 - 分子機能 | ||||||
生物種 | ![]() ![]() | ||||||
手法 | ![]() | ||||||
![]() | Wlodawer, A. / Savage, H. | ||||||
![]() | ![]() タイトル: Structure of insulin: results of joint neutron and X-ray refinement. 著者: Wlodawer, A. / Savage, H. / Dodson, G. #1: ![]() タイトル: Experience with Fast Fourier Least Squares in the Refinement of the Crystal Structure of Rhombohedral 2-Zinc Insulin at 1.5 Angstroms Resolution 著者: Isaacs, N.W. / Agarwal, R.C. | ||||||
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構造の表示
構造ビューア | 分子: ![]() ![]() |
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ダウンロードとリンク
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ダウンロード
PDBx/mmCIF形式 | ![]() | 59.4 KB | 表示 | ![]() |
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PDB形式 | ![]() | 43 KB | 表示 | ![]() |
PDBx/mmJSON形式 | ![]() | ツリー表示 | ![]() | |
その他 | ![]() |
-検証レポート
文書・要旨 | ![]() | 414.7 KB | 表示 | ![]() |
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文書・詳細版 | ![]() | 424.4 KB | 表示 | |
XML形式データ | ![]() | 6.1 KB | 表示 | |
CIF形式データ | ![]() | 9.7 KB | 表示 | |
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-関連構造データ
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リンク
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集合体
登録構造単位 | ![]()
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単位格子 |
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Atom site foot note | 1: THE FOLLOWING RESIDUES ARE DISORDERED - VAL B 12, GLU B 21, ARG B 22, THR B 27, ARG D 22, LYS D 29. 2: DISORDER IN RESIDUE VAL B 12 PRECLUDES USE OF STANDARD NOMENCLATURE FOR HYDROGEN ATOMS IN THIS RESIDUE. THE HYDROGEN ATOMS, THEREFORE, ARE ARBITRARILY NAMED. ALSO SEE FTNOTE 1. | |||||||||||||||
Components on special symmetry positions |
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非結晶学的対称性 (NCS) | NCS oper: (Code: given Matrix: (-0.87862, -0.47696, 0.02305), 詳細 | THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT OF INSULIN CONSISTS OF TWO INSULIN MOLECULES EACH CONSISTING OF TWO CHAINS. THIS ENTRY PRESENTS COORDINATES FOR MOLECULES I (CHAIN INDICATORS A AND B) AND II (CHAIN INDICATORS C AND D). THE QUASI-TWO-FOLD AXIS THAT TRANSFORMS MOLECULE I INTO MOLECULE II IS GIVEN IN THE MTRIX RECORDS BELOW. APPLYING THE THREE-FOLD CRYSTALLOGRAPHIC AXIS YIELDS A HEXAMER AROUND THE AXIS. THERE ARE TWO ZINC IONS SITUATED ON THIS THREE-FOLD AXIS. COORDINATES FOR THE ZINC IONS AND WATER MOLECULES ARE INCLUDED BELOW WITH A BLANK CHAIN INDICATOR. | |
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要素
#1: タンパク質・ペプチド | 分子量: 2383.698 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() #2: タンパク質・ペプチド | 分子量: 3403.927 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() #3: 化合物 | #4: 化合物 | ChemComp-DOD / | Has protein modification | Y | |
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-実験情報
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試料調製
結晶 | マシュー密度: 1.92 Å3/Da / 溶媒含有率: 36.05 % | ||||||||||||||||||||||||||||||
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結晶化 | *PLUS pH: 6.5 / 手法: unknown | ||||||||||||||||||||||||||||||
溶液の組成 | *PLUS
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-データ収集
放射波長 | 相対比: 1 |
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反射 | *PLUS 最高解像度: 1.5 Å / 最低解像度: 10 Å / Observed criterion σ(F): 0 / Num. measured all: 13476 |
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解析
ソフトウェア | 名称: PROLSQ / 分類: 精密化 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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精密化 |
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精密化ステップ | サイクル: LAST / 最高解像度: 1.5 Å
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拘束条件 |
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精密化 | *PLUS Rfactor obs: 0.182 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
溶媒の処理 | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
原子変位パラメータ | *PLUS |