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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: 2axi | ||||||
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タイトル | HDM2 in complex with a beta-hairpin | ||||||
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![]() | LIGASE/LIGASE INHIBITOR / P53 / DRUG DESIGN / PROTEIN-PROTEIN INTERACTIONS / LIGASE / LIGASE-LIGASE INHIBITOR complex | ||||||
機能・相同性 | ![]() : / cellular response to vitamin B1 / response to formaldehyde / response to water-immersion restraint stress / traversing start control point of mitotic cell cycle / negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator / response to ether / negative regulation of signal transduction by p53 class mediator / fibroblast activation / atrial septum development ...: / cellular response to vitamin B1 / response to formaldehyde / response to water-immersion restraint stress / traversing start control point of mitotic cell cycle / negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator / response to ether / negative regulation of signal transduction by p53 class mediator / fibroblast activation / atrial septum development / receptor serine/threonine kinase binding / Trafficking of AMPA receptors / positive regulation of vascular associated smooth muscle cell migration / peroxisome proliferator activated receptor binding / SUMO transferase activity / negative regulation of protein processing / response to iron ion / response to steroid hormone / NEDD8 ligase activity / AKT phosphorylates targets in the cytosol / atrioventricular valve morphogenesis / cellular response to peptide hormone stimulus / ventricular septum development / endocardial cushion morphogenesis / positive regulation of muscle cell differentiation / SUMOylation of ubiquitinylation proteins / cellular response to alkaloid / blood vessel development / regulation of protein catabolic process / cardiac septum morphogenesis / Constitutive Signaling by AKT1 E17K in Cancer / ligase activity / negative regulation of DNA damage response, signal transduction by p53 class mediator / response to magnesium ion / SUMOylation of transcription factors / protein sumoylation / protein localization to nucleus / cellular response to UV-C / blood vessel remodeling / cellular response to estrogen stimulus / protein autoubiquitination / cellular response to actinomycin D / ribonucleoprotein complex binding / positive regulation of vascular associated smooth muscle cell proliferation / DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest / NPAS4 regulates expression of target genes / transcription repressor complex / regulation of heart rate / positive regulation of mitotic cell cycle / positive regulation of protein export from nucleus / response to cocaine / proteolysis involved in protein catabolic process / ubiquitin binding / Stabilization of p53 / Regulation of RUNX3 expression and activity / protein destabilization / RING-type E3 ubiquitin transferase / establishment of protein localization / Oncogene Induced Senescence / Regulation of TP53 Activity through Methylation / response to toxic substance / cellular response to gamma radiation / cellular response to growth factor stimulus / cellular response to hydrogen peroxide / protein polyubiquitination / ubiquitin-protein transferase activity / endocytic vesicle membrane / ubiquitin protein ligase activity / disordered domain specific binding / Signaling by ALK fusions and activated point mutants / Regulation of TP53 Degradation / p53 binding / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / negative regulation of neuron projection development / cellular response to hypoxia / 5S rRNA binding / ubiquitin-dependent protein catabolic process / regulation of gene expression / protein-containing complex assembly / proteasome-mediated ubiquitin-dependent protein catabolic process / Oxidative Stress Induced Senescence / Regulation of TP53 Activity through Phosphorylation / amyloid fibril formation / Ub-specific processing proteases / regulation of cell cycle / protein ubiquitination / response to xenobiotic stimulus / protein domain specific binding / response to antibiotic / negative regulation of DNA-templated transcription / apoptotic process / ubiquitin protein ligase binding / positive regulation of cell population proliferation / positive regulation of gene expression / nucleolus / negative regulation of apoptotic process / enzyme binding / negative regulation of transcription by RNA polymerase II / protein-containing complex / zinc ion binding 類似検索 - 分子機能 | ||||||
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手法 | ![]() ![]() | ||||||
![]() | Mittl, P.R.E. / Fasan, R. / Robinson, J. / Gruetter, M.G. | ||||||
![]() | ![]() タイトル: Structure-Activity Studies in a Family of beta-Hairpin Protein Epitope Mimetic Inhibitors of the p53-HDM2 Protein-Protein Interaction. 著者: Fasan, R. / Dias, R.L. / Moehle, K. / Zerbe, O. / Obrecht, D. / Mittl, P.R. / Robinson, J.A. | ||||||
履歴 |
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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 | ![]() | 41.7 KB | 表示 | ![]() |
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PDB形式 | ![]() | 26.9 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 | ![]() | 446.1 KB | 表示 | ![]() |
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文書・詳細版 | ![]() | 449.4 KB | 表示 | |
XML形式データ | ![]() | 5.9 KB | 表示 | |
CIF形式データ | ![]() | 7.7 KB | 表示 | |
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-関連構造データ
関連構造データ | ![]() 1ycrS S: 精密化の開始モデル |
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類似構造データ |
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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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Components on special symmetry positions |
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要素
#1: タンパク質 | 分子量: 13364.231 Da / 分子数: 1 / 断片: HDM2 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() 参照: UniProt: Q9UMT8, UniProt: Q00987*PLUS, 合成酵素; C-N結合を形成; 酸-D-アミノ酸リガーゼ(ペプチド合成) | ||||
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#2: タンパク質・ペプチド | | ||||
#3: 化合物 | #4: 化合物 | ChemComp-MPO / | #5: 水 | ChemComp-HOH / | |
-実験情報
-実験
実験 | 手法: ![]() |
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試料調製
結晶 | マシュー密度: 1.82115 Å3/Da / 溶媒含有率: 32.460266 % / 解説: Data was collected in-house and at the synchrotron |
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結晶化 | 温度: 293 K / 手法: 蒸気拡散法, ハンギングドロップ法 / pH: 5.5 詳細: MES, ammonium sulfate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-データ収集
回折 | 平均測定温度: 100 K |
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放射光源 | 由来: ![]() |
検出器 | タイプ: MARRESEARCH / 検出器: IMAGE PLATE / 日付: 2003年10月1日 / 詳細: Osmic Mirrors |
放射 | プロトコル: SINGLE WAVELENGTH / 単色(M)・ラウエ(L): M / 散乱光タイプ: x-ray |
放射波長 | 波長: 1.54 Å / 相対比: 1 |
反射 | 解像度: 1.4→50 Å / Num. obs: 21288 / % possible obs: 98.4 % / Observed criterion σ(I): 0 / 冗長度: 4.18 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 15.19 |
反射 シェル | 解像度: 1.4→1.41 Å / 冗長度: 3.9 % / Rmerge(I) obs: 0.48 / Mean I/σ(I) obs: 2.91 / % possible all: 90.8 |
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解析
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精密化 | 構造決定の手法: ![]() 開始モデル: 1YCR 解像度: 1.4→10 Å / σ(F): 4 / 立体化学のターゲット値: ENGH & HUBER
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精密化ステップ | サイクル: LAST / 解像度: 1.4→10 Å
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