+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 1cll | ||||||
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タイトル | CALMODULIN STRUCTURE REFINED AT 1.7 ANGSTROMS RESOLUTION | ||||||
要素 | CALMODULINカルモジュリン | ||||||
キーワード | CALCIUM-BINDING PROTEIN (カルシウム結合タンパク質) | ||||||
機能・相同性 | 機能・相同性情報 : / establishment of protein localization to mitochondrial membrane / type 3 metabotropic glutamate receptor binding / CAM型光合成 / Cam-PDE 1 activation / Sodium/Calcium exchangers / Calmodulin induced events / Reduction of cytosolic Ca++ levels / Activation of Ca-permeable Kainate Receptor / CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde ...: / establishment of protein localization to mitochondrial membrane / type 3 metabotropic glutamate receptor binding / CAM型光合成 / Cam-PDE 1 activation / Sodium/Calcium exchangers / Calmodulin induced events / Reduction of cytosolic Ca++ levels / Activation of Ca-permeable Kainate Receptor / CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde / regulation of synaptic vesicle endocytosis / Loss of phosphorylation of MECP2 at T308 / CREB1 phosphorylation through the activation of Adenylate Cyclase / PKA activation / negative regulation of high voltage-gated calcium channel activity / regulation of synaptic vesicle exocytosis / CaMK IV-mediated phosphorylation of CREB / Glycogen breakdown (glycogenolysis) / negative regulation of calcium ion export across plasma membrane / organelle localization by membrane tethering / Activation of RAC1 downstream of NMDARs / regulation of cardiac muscle cell action potential / mitochondrion-endoplasmic reticulum membrane tethering / CLEC7A (Dectin-1) induces NFAT activation / autophagosome membrane docking / response to corticosterone / positive regulation of ryanodine-sensitive calcium-release channel activity / Negative regulation of NMDA receptor-mediated neuronal transmission / nitric-oxide synthase binding / regulation of cell communication by electrical coupling involved in cardiac conduction / Unblocking of NMDA receptors, glutamate binding and activation / negative regulation of peptidyl-threonine phosphorylation / Synthesis of IP3 and IP4 in the cytosol / Phase 0 - rapid depolarisation / protein phosphatase activator activity / RHO GTPases activate PAKs / positive regulation of cyclic-nucleotide phosphodiesterase activity / positive regulation of phosphoprotein phosphatase activity / 長期増強 / Ion transport by P-type ATPases / Uptake and function of anthrax toxins / adenylate cyclase binding / Calcineurin activates NFAT / Regulation of MECP2 expression and activity / catalytic complex / DARPP-32 events / detection of calcium ion / negative regulation of ryanodine-sensitive calcium-release channel activity / Smooth Muscle Contraction / RHO GTPases activate IQGAPs / regulation of cardiac muscle contraction / calcium channel inhibitor activity / cellular response to interferon-beta / positive regulation of DNA binding / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / Protein methylation / enzyme regulator activity / voltage-gated potassium channel complex / phosphatidylinositol 3-kinase binding / Activation of AMPK downstream of NMDARs / eNOS activation / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / regulation of calcium-mediated signaling / positive regulation of protein dephosphorylation / titin binding / regulation of ryanodine-sensitive calcium-release channel activity / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / Ion homeostasis / positive regulation of protein autophosphorylation / sperm midpiece / response to amphetamine / calcium channel complex / activation of adenylate cyclase activity / substantia nigra development / adenylate cyclase activator activity / Ras activation upon Ca2+ influx through NMDA receptor / regulation of heart rate / nitric-oxide synthase regulator activity / protein serine/threonine kinase activator activity / sarcomere / FCERI mediated Ca+2 mobilization / FCGR3A-mediated IL10 synthesis / VEGFR2 mediated vascular permeability / positive regulation of peptidyl-threonine phosphorylation / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / VEGFR2 mediated cell proliferation / regulation of cytokinesis / positive regulation of nitric-oxide synthase activity / Translocation of SLC2A4 (GLUT4) to the plasma membrane / spindle microtubule / ミトコンドリア / RAF activation / positive regulation of receptor signaling pathway via JAK-STAT / positive regulation of protein serine/threonine kinase activity / Transcriptional activation of mitochondrial biogenesis / Stimuli-sensing channels / synaptic vesicle membrane / 紡錘体 / cellular response to type II interferon / response to calcium ion 類似検索 - 分子機能 | ||||||
生物種 | Homo sapiens (ヒト) | ||||||
手法 | X線回折 / 解像度: 1.7 Å | ||||||
データ登録者 | Chattopadhyaya, R. / Quiocho, F.A. | ||||||
引用 | ジャーナル: J.Mol.Biol. / 年: 1992 タイトル: Calmodulin structure refined at 1.7 A resolution. 著者: Chattopadhyaya, R. / Meador, W.E. / Means, A.R. / Quiocho, F.A. #1: ジャーナル: Science / 年: 1992 タイトル: Target Enzyme Recognition by Calmodulin: 2.4 Angstroms Structure of a Calmodulin-Peptide Complex 著者: Meador, W.E. / Means, A.R. / Quiocho, F.A. #2: ジャーナル: J.Mol.Biol. / 年: 1988 タイトル: Structure of Calmodulin Refined at 2.2 Angstroms Resolution 著者: Babu, Y.S. / Bugg, C.E. / Cook, W.J. | ||||||
履歴 |
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Remark 700 | SHEET THE ANTI-PARALLEL BETA SHEETS ARE EXTREMELY SHORT IN THIS STRUCTURE. THERE IS ADDITIONAL ...SHEET THE ANTI-PARALLEL BETA SHEETS ARE EXTREMELY SHORT IN THIS STRUCTURE. THERE IS ADDITIONAL CONNECTIVITY VIA WATERS BETWEEN THE TWO STRANDS OF EACH SHEET. |
-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 | 1cll.cif.gz | 45.5 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb1cll.ent.gz | 31.7 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 1cll.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/cl/1cll ftp://data.pdbj.org/pub/pdb/validation_reports/cl/1cll | 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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単位格子 |
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-要素
#1: タンパク質 | 分子量: 16721.350 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 参照: UniProt: P62158, UniProt: P0DP23*PLUS | ||||
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#2: 化合物 | ChemComp-CA / #3: 化合物 | ChemComp-EOH / | #4: 水 | ChemComp-HOH / | |
-実験情報
-実験
実験 | 手法: X線回折 |
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-試料調製
結晶 | マシュー密度: 2.41 Å3/Da / 溶媒含有率: 48.89 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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結晶化 | *PLUS pH: 5 / 手法: 蒸気拡散法, ハンギングドロップ法 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
溶液の組成 | *PLUS
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-データ収集
放射 | 散乱光タイプ: x-ray |
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放射波長 | 相対比: 1 |
反射 | *PLUS 最高解像度: 1.7 Å / Num. all: 46091 / Num. obs: 15417 / Rmerge(I) obs: 0.329 / Biso Wilson estimate: 25 Å2 |
-解析
ソフトウェア |
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精密化 | 解像度: 1.7→10 Å / σ(F): 0.5 詳細: CRYSTAL PACKING IS EXTENSIVELY STUDIED IN THE CHATTOPADHYAYA ET AL. PAPER ON CALMODULIN, AND FACILE CRYSTAL GROWTH ALONG THE Z-DIRECTION EXPLAINED. THE AUTHORS ALSO HAVE REPORTED IN DETAIL ...詳細: CRYSTAL PACKING IS EXTENSIVELY STUDIED IN THE CHATTOPADHYAYA ET AL. PAPER ON CALMODULIN, AND FACILE CRYSTAL GROWTH ALONG THE Z-DIRECTION EXPLAINED. THE AUTHORS ALSO HAVE REPORTED IN DETAIL ABOUT THE HYDROGEN BONDING WITHIN VARIOUS STRUCTURAL ELEMENTS IN THAT PUBLICATION. HYDRATION IS ALSO DESCRIBED. THESE ARE AREAS WHICH WERE NOT DEALT WITH IN THE BABU ET AL. (1988) PUBLICATION.
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精密化ステップ | サイクル: LAST / 解像度: 1.7→10 Å
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拘束条件 |
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ソフトウェア | *PLUS 名称: PROLSQ / 分類: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
精密化 | *PLUS 最高解像度: 1.7 Å / 最低解像度: 10 Å / Num. reflection obs: 14469 / σ(F): 0.5 / Rfactor obs: 0.225 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
溶媒の処理 | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
原子変位パラメータ | *PLUS |