+データを開く
-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 | ||||||
要素 |
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キーワード | HORMONE (ホルモン) | ||||||
機能・相同性 | 機能・相同性情報 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 / response to L-arginine ...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 / response to L-arginine / positive regulation of lipoprotein lipase activity / lactate biosynthetic process / lipoprotein biosynthetic process / positive regulation of fatty acid biosynthetic process / positive regulation of glucose metabolic process / COPI-mediated anterograde transport / lipid biosynthetic process / negative regulation of glycogen catabolic process / regulation of cellular amino acid metabolic process / nitric oxide-cGMP-mediated signaling / negative regulation of fatty acid metabolic process / negative regulation of feeding behavior / positive regulation of respiratory burst / positive regulation of dendritic spine maintenance / alpha-beta T cell activation / negative regulation of acute inflammatory response / negative regulation of respiratory burst involved in inflammatory response / negative regulation of protein secretion / fatty acid homeostasis / positive regulation of glycogen biosynthetic process / negative regulation of gluconeogenesis / positive regulation of nitric oxide mediated signal transduction / regulation of protein localization to plasma membrane / negative regulation of lipid catabolic process / positive regulation of insulin receptor signaling pathway / negative regulation of reactive oxygen species biosynthetic process / positive regulation of protein autophosphorylation / insulin-like growth factor receptor binding / neuron projection maintenance / positive regulation of glycolytic process / positive regulation of mitotic nuclear division / positive regulation of DNA replication / positive regulation of cytokine production / acute-phase response / positive regulation of protein secretion / positive regulation of glucose import / negative regulation of proteolysis / wound healing / insulin receptor binding / negative regulation of protein catabolic process / hormone activity / vasodilation / positive regulation of protein localization to nucleus / glucose metabolic process / glucose homeostasis / insulin receptor signaling pathway / protease binding / positive regulation of MAPK cascade / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / 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 | Sus scrofa (ブタ) | ||||||
手法 | X線回折 / 中性子回折 / 解像度: 1.5 Å | ||||||
データ登録者 | Wlodawer, A. / Savage, H. | ||||||
引用 | ジャーナル: Acta Crystallogr.,Sect.B / 年: 1989 タイトル: Structure of insulin: results of joint neutron and X-ray refinement. 著者: Wlodawer, A. / Savage, H. / Dodson, G. #1: ジャーナル: Acta Crystallogr.,Sect.A / 年: 1978 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. | ||||||
履歴 |
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-構造の表示
構造ビューア | 分子: MolmilJmol/JSmol |
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-ダウンロードとリンク
-ダウンロード
PDBx/mmCIF形式 | 3ins.cif.gz | 56.1 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb3ins.ent.gz | 43.6 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 3ins.json.gz | ツリー表示 | PDBx/mmJSON形式 | |
その他 | その他のダウンロード |
-検証レポート
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/in/3ins ftp://data.pdbj.org/pub/pdb/validation_reports/in/3ins | HTTPS FTP |
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-関連構造データ
-リンク
-集合体
登録構造単位 |
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2 |
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3 |
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4 |
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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. | |
-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) Sus scrofa (ブタ) / 参照: UniProt: P01315 #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) Sus scrofa (ブタ) / 参照: UniProt: P01315 #3: 化合物 | #4: 化合物 | ChemComp-DOD / | |
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-実験情報
-実験
実験 |
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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 |
-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 |