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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: 1nvr | ||||||
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タイトル | The Complex Structure Of Checkpoint Kinase Chk1/Staurosporine | ||||||
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![]() | TRANSFERASE / Chk1-Staurosporine complex | ||||||
機能・相同性 | ![]() negative regulation of G0 to G1 transition / apoptotic process involved in development / histone H3T11 kinase activity / negative regulation of DNA biosynthetic process / mitotic G2/M transition checkpoint / negative regulation of mitotic nuclear division / regulation of mitotic centrosome separation / inner cell mass cell proliferation / regulation of double-strand break repair via homologous recombination / negative regulation of gene expression, epigenetic ...negative regulation of G0 to G1 transition / apoptotic process involved in development / histone H3T11 kinase activity / negative regulation of DNA biosynthetic process / mitotic G2/M transition checkpoint / negative regulation of mitotic nuclear division / regulation of mitotic centrosome separation / inner cell mass cell proliferation / regulation of double-strand break repair via homologous recombination / negative regulation of gene expression, epigenetic / nucleus organization / cellular response to caffeine / Transcriptional Regulation by E2F6 / mitotic G2 DNA damage checkpoint signaling / Presynaptic phase of homologous DNA pairing and strand exchange / replicative senescence / signal transduction in response to DNA damage / Activation of ATR in response to replication stress / Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex / positive regulation of cell cycle / condensed nuclear chromosome / regulation of signal transduction by p53 class mediator / DNA damage checkpoint signaling / replication fork / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / TP53 Regulates Transcription of DNA Repair Genes / peptidyl-threonine phosphorylation / Signaling by SCF-KIT / G2/M DNA damage checkpoint / cellular response to mechanical stimulus / G2/M transition of mitotic cell cycle / regulation of cell population proliferation / Processing of DNA double-strand break ends / DNA replication / Regulation of TP53 Activity through Phosphorylation / non-specific serine/threonine protein kinase / protein kinase activity / chromatin remodeling / protein domain specific binding / protein phosphorylation / intracellular membrane-bounded organelle / DNA repair / protein serine kinase activity / protein serine/threonine kinase activity / centrosome / DNA damage response / chromatin / apoptotic process / protein-containing complex / extracellular space / nucleoplasm / ATP binding / nucleus / cytosol / cytoplasm 類似検索 - 分子機能 | ||||||
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手法 | ![]() ![]() ![]() | ||||||
![]() | Zhao, B. / Bower, M.J. / McDevitt, P.J. / Zhao, H. / Davis, S.T. / Johanson, K.O. / Green, S.M. / Concha, N.O. / Zhou, B.B. | ||||||
![]() | ![]() タイトル: Structural Basis for Chk1 Inhibition by UCN-01 著者: Zhao, B. / Bower, M.J. / McDevitt, P.J. / Zhao, H. / Davis, S.T. / Johanson, K.O. / Green, S.M. / Concha, N.O. / Zhou, B.B. | ||||||
履歴 |
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Remark 999 | SEQUENCE A five-residue peptide 301-305 was found with the enzyme. Residues were named based on the ...SEQUENCE A five-residue peptide 301-305 was found with the enzyme. Residues were named based on the electron density. The peptide could be the part of C-terminal missing residues. |
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構造の表示
構造ビューア | 分子: ![]() ![]() |
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PDBx/mmCIF形式 | ![]() | 73.7 KB | 表示 | ![]() |
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PDB形式 | ![]() | 53.1 KB | 表示 | ![]() |
PDBx/mmJSON形式 | ![]() | ツリー表示 | ![]() | |
その他 | ![]() |
-検証レポート
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
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-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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要素
#1: タンパク質 | 分子量: 33042.988 Da / 分子数: 1 / 断片: CHK1KD (RESIDUES 1-289) / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() 参照: UniProt: O14757, 転移酵素; リンを含む基を移すもの; キナーゼ(アルコールにつなげるもの) |
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#2: タンパク質・ペプチド | 分子量: 433.457 Da / 分子数: 1 / 由来タイプ: 合成 |
#3: 化合物 | ChemComp-SO4 / |
#4: 化合物 | ChemComp-STU / |
#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: 2.54 Å3/Da / 溶媒含有率: 51.23 % | ||||||||||||||||||||
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結晶化 | 温度: 293 K / 手法: 蒸気拡散法, シッティングドロップ法 / pH: 7.5 詳細: PEG8000, ammonium sulfate, glycerol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K | ||||||||||||||||||||
結晶化 | *PLUS 手法: 蒸気拡散法 | ||||||||||||||||||||
溶液の組成 | *PLUS
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-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: CCD / 日付: 2000年12月2日 |
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 Å / 相対比: 1 |
反射 | 解像度: 1.8→50 Å / Num. all: 31548 / Num. obs: 31477 / % possible obs: 99.8 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 |
反射 | *PLUS 最高解像度: 1.8 Å / % possible obs: 100 % / 冗長度: 4.2 % / Num. measured all: 132242 / Rmerge(I) obs: 0.082 |
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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: PDB ENTRY 2PHK 解像度: 1.8→20 Å / σ(F): 1 / 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: 1.8→20 Å
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拘束条件 |
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精密化 | *PLUS 最低解像度: 20 Å / % reflection Rfree: 6 % / Rfactor Rfree: 0.237 / Rfactor Rwork: 0.213 | |||||||||||||||||||||||||
溶媒の処理 | *PLUS | |||||||||||||||||||||||||
原子変位パラメータ | *PLUS | |||||||||||||||||||||||||
拘束条件 | *PLUS
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