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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: 1rcb | ||||||
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| タイトル | CRYSTAL STRUCTURE OF HUMAN RECOMBINANT INTERLEUKIN-4 AT 2.25 ANGSTROMS RESOLUTION | ||||||
要素 | INTERLEUKIN-4 | ||||||
キーワード | CYTOKINE | ||||||
| 機能・相同性 | 機能・相同性情報interleukin-4 receptor binding / positive regulation of isotype switching to IgE isotypes / negative regulation of complement-dependent cytotoxicity / positive regulation of cellular respiration / Interleukin-18 signaling / regulation of isotype switching / negative regulation of neuroinflammatory response / negative regulation of epithelial cell migration / positive regulation of T-helper 2 cell cytokine production / dendritic cell differentiation ...interleukin-4 receptor binding / positive regulation of isotype switching to IgE isotypes / negative regulation of complement-dependent cytotoxicity / positive regulation of cellular respiration / Interleukin-18 signaling / regulation of isotype switching / negative regulation of neuroinflammatory response / negative regulation of epithelial cell migration / positive regulation of T-helper 2 cell cytokine production / dendritic cell differentiation / interleukin-4-mediated signaling pathway / neuroinflammatory response / positive regulation of isotype switching to IgG isotypes / positive regulation of interleukin-13 production / macrophage activation / positive regulation of amyloid-beta clearance / myeloid dendritic cell differentiation / positive regulation of MHC class II biosynthetic process / type 2 immune response / negative regulation of cellular response to transforming growth factor beta stimulus / positive regulation of T cell differentiation / negative regulation of osteoclast differentiation / positive regulation of ATP biosynthetic process / positive regulation of interleukin-10 production / positive regulation of macroautophagy / negative regulation of tumor necrosis factor production / cell surface receptor signaling pathway via JAK-STAT / regulation of immune response / negative regulation of endothelial cell apoptotic process / cholesterol metabolic process / positive regulation of B cell proliferation / positive regulation of T cell proliferation / T cell activation / B cell differentiation / cytokine activity / growth factor activity / positive regulation of receptor-mediated endocytosis / negative regulation of inflammatory response / positive regulation of cold-induced thermogenesis / Interleukin-4 and Interleukin-13 signaling / immune response / positive regulation of cell migration / negative regulation of DNA-templated transcription / positive regulation of cell population proliferation / positive regulation of gene expression / negative regulation of apoptotic process / positive regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / extracellular space / extracellular region 類似検索 - 分子機能 | ||||||
| 生物種 | Homo sapiens (ヒト) | ||||||
| 手法 | X線回折 / 解像度: 2.25 Å | ||||||
データ登録者 | Wlodawer, A. / Pavlovsky, A. / Gustchina, A. | ||||||
引用 | ジャーナル: FEBS Lett. / 年: 1992タイトル: Crystal structure of human recombinant interleukin-4 at 2.25 A resolution. 著者: Wlodawer, A. / Pavlovsky, A. / Gustchina, A. | ||||||
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構造の表示
| 構造ビューア | 分子: Molmil Jmol/JSmol |
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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 | 1rcb.cif.gz | 38.8 KB | 表示 | PDBx/mmCIF形式 |
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| PDB形式 | pdb1rcb.ent.gz | 26.8 KB | 表示 | PDB形式 |
| PDBx/mmJSON形式 | 1rcb.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
| 文書・要旨 | 1rcb_validation.pdf.gz | 363.6 KB | 表示 | wwPDB検証レポート |
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| 文書・詳細版 | 1rcb_full_validation.pdf.gz | 379.6 KB | 表示 | |
| XML形式データ | 1rcb_validation.xml.gz | 6.3 KB | 表示 | |
| CIF形式データ | 1rcb_validation.cif.gz | 8.4 KB | 表示 | |
| アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/rc/1rcb ftp://data.pdbj.org/pub/pdb/validation_reports/rc/1rcb | 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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| 1 | ![]()
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| 単位格子 |
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| Atom site foot note | 1: THE ELECTRON DENSITY FOR RESIDUES 38 - 40 IS POOR, AND THE TRACING IN THAT REGION IS UNCERTAIN. |
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要素
| #1: タンパク質 | 分子量: 14989.248 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: P05112 |
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| #2: 水 | ChemComp-HOH / |
| Has protein modification | Y |
-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: 3.26 Å3/Da / 溶媒含有率: 62.28 % | |||||||||||||||||||||||||
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| 結晶化 | *PLUS pH: 6 / 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: 2.23 Å / Num. obs: 8951 / % possible obs: 90.7 % / Observed criterion σ(F): 2 / Rmerge(I) obs: 0.06 |
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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 | 解像度: 2.25→10 Å 詳細: THE ELECTRON DENSITY FOR RESIDUES 38 - 40 IS POOR, AND THE TRACING IN THAT REGION IS UNCERTAIN.
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| 精密化ステップ | サイクル: LAST / 解像度: 2.25→10 Å
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| 拘束条件 |
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| 精密化 | *PLUS 最高解像度: 2.25 Å / 最低解像度: 10 Å / Num. reflection obs: 8085 / Rfactor obs: 0.218 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 溶媒の処理 | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 原子変位パラメータ | *PLUS |
ムービー
コントローラー
万見について




Homo sapiens (ヒト)
X線回折
引用







PDBj





