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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: 2c7n | ||||||
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タイトル | Human Rabex-5 residues 1-74 in complex with Ubiquitin | ||||||
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![]() | PROTEIN BINDING / PROTEIN-BINDING / UBIQUITIN BINDING DOMAIN / ENDOCYTOSIS / NUCLEAR PROTEIN / POLYPROTEIN / UBIQUITIN COMPLEX | ||||||
機能・相同性 | ![]() dendritic transport / negative regulation of Kit signaling pathway / : / mast cell migration / regulation of Fc receptor mediated stimulatory signaling pathway / Kit signaling pathway / negative regulation of mast cell degranulation / Translesion synthesis by REV1 / Recognition of DNA damage by PCNA-containing replication complex / Translesion Synthesis by POLH ...dendritic transport / negative regulation of Kit signaling pathway / : / mast cell migration / regulation of Fc receptor mediated stimulatory signaling pathway / Kit signaling pathway / negative regulation of mast cell degranulation / Translesion synthesis by REV1 / Recognition of DNA damage by PCNA-containing replication complex / Translesion Synthesis by POLH / Downregulation of ERBB4 signaling / Spry regulation of FGF signaling / Downregulation of ERBB2:ERBB3 signaling / NOD1/2 Signaling Pathway / APC/C:Cdc20 mediated degradation of Cyclin B / SCF-beta-TrCP mediated degradation of Emi1 / APC-Cdc20 mediated degradation of Nek2A / EGFR downregulation / TCF dependent signaling in response to WNT / NRIF signals cell death from the nucleus / p75NTR recruits signalling complexes / NF-kB is activated and signals survival / Activated NOTCH1 Transmits Signal to the Nucleus / Downregulation of TGF-beta receptor signaling / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / Downregulation of SMAD2/3:SMAD4 transcriptional activity / SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription / Senescence-Associated Secretory Phenotype (SASP) / Regulation of innate immune responses to cytosolic DNA / activated TAK1 mediates p38 MAPK activation / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / Regulation of FZD by ubiquitination / PINK1-PRKN Mediated Mitophagy / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Regulation of TNFR1 signaling / TNFR1-induced NF-kappa-B signaling pathway / Translesion synthesis by POLK / Translesion synthesis by POLI / Regulation of necroptotic cell death / MAP3K8 (TPL2)-dependent MAPK1/3 activation / HDR through Homologous Recombination (HRR) / Josephin domain DUBs / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / Processing of DNA double-strand break ends / Formation of Incision Complex in GG-NER / Gap-filling DNA repair synthesis and ligation in GG-NER / Dual Incision in GG-NER / Fanconi Anemia Pathway / Regulation of TP53 Activity through Phosphorylation / Regulation of TP53 Degradation / Regulation of TP53 Activity through Methylation / Negative regulation of MET activity / Cyclin D associated events in G1 / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Downregulation of ERBB2 signaling / E3 ubiquitin ligases ubiquitinate target proteins / Regulation of PTEN localization / ER Quality Control Compartment (ERQC) / Regulation of expression of SLITs and ROBOs / Interferon alpha/beta signaling / Endosomal Sorting Complex Required For Transport (ESCRT) / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / IKK complex recruitment mediated by RIP1 / IRAK2 mediated activation of TAK1 complex / TRAF6-mediated induction of TAK1 complex within TLR4 complex / Alpha-protein kinase 1 signaling pathway / RAS processing / Pexophagy / Inactivation of CSF3 (G-CSF) signaling / Negative regulation of FLT3 / Regulation of BACH1 activity / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / Regulation of NF-kappa B signaling / Termination of translesion DNA synthesis / Ovarian tumor domain proteases / Negative regulators of DDX58/IFIH1 signaling / Negative regulation of FGFR1 signaling / Negative regulation of FGFR2 signaling / Negative regulation of FGFR3 signaling / Negative regulation of FGFR4 signaling / Negative regulation of MAPK pathway / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / Iron uptake and transport / Deactivation of the beta-catenin transactivating complex / Metalloprotease DUBs / Formation of TC-NER Pre-Incision Complex / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / negative regulation of mast cell activation / DNA Damage Recognition in GG-NER / Activation of NF-kappaB in B cells / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / SCF(Skp2)-mediated degradation of p27/p21 / FCERI mediated NF-kB activation / Autodegradation of the E3 ubiquitin ligase COP1 / Asymmetric localization of PCP proteins / Degradation of AXIN 類似検索 - 分子機能 | ||||||
生物種 | ![]() ![]() ![]() | ||||||
手法 | ![]() ![]() ![]() | ||||||
![]() | Penengo, L. / Mapelli, M. / Murachelli, A.G. / Confalioneri, S. / Magri, L. / Musacchio, A. / Di Fiore, P.P. / Polo, S. / Schneider, T.R. | ||||||
![]() | ![]() タイトル: Crystal Structure of the Ubiquitin Binding Domains of Rabex-5 Reveals Two Modes of Interaction with Ubiquitin. 著者: Penengo, L. / Mapelli, M. / Murachelli, A.G. / Confalonieri, S. / Magri, L. / Musacchio, A. / Di Fiore, P.P. / Polo, S. / Schneider, T.R. | ||||||
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 | ![]() | 169.8 KB | 表示 | ![]() |
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PDB形式 | ![]() | 136.8 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 | ![]() | 509.1 KB | 表示 | ![]() |
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文書・詳細版 | ![]() | 527.1 KB | 表示 | |
XML形式データ | ![]() | 32.8 KB | 表示 | |
CIF形式データ | ![]() | 45.7 KB | 表示 | |
アーカイブディレクトリ | ![]() ![]() | 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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単位格子 |
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詳細 | THE QUATERNARY STRUCTURE FOR THIS ENTRY IS NOT RELEVANTSINCE THE COMPLEX IS ONLY MADE UP OF FRAGMENTS OF RABEX-5IN COMPLEX WITH UBIQUITIN. HOWEVER, THESE REMARKSONLY INDICATE THE COMPLEX AS SEEN IN THE PDB FILE, ANDDO NOT HAVE RELEVANCE TO THE BIOLOGICAL STATE OF THEMOLECULE. |
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要素
#1: タンパク質 | 分子量: 8784.761 Da / 分子数: 6 / 断片: TWO UBIQUTIN BINDING DOMAINS, RESIDUES 1-74 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() #2: タンパク質 | 分子量: 8576.831 Da / 分子数: 6 / 由来タイプ: 合成 / 詳細: BOSTON BIOCHEM / 由来: (合成) ![]() ![]() #3: 化合物 | ChemComp-ZN / #4: 水 | ChemComp-HOH / | 構成要素の詳細 | INVOLVED IN THE ATP-DEPENDENT SELECTIVE DEGRADATION OF CELLULAR PROTEINS, THE MAINTENANCE OF ...INVOLVED IN THE ATP-DEPENDENT SELECTIVE DEGRADATIO | 配列の詳細 | THE CONSTRUCT USED IN THE STRUCTURE DETERMINAT | |
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-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: 3.08 Å3/Da / 溶媒含有率: 59.77 % | |||||||||||||||||||||||||
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結晶化 | 手法: 蒸気拡散法, シッティングドロップ法 / pH: 6.5 詳細: SITTING DROP 300NL PLUS 300NL 0.2M AMMONIUM ACETATE 0.1M NACITRATE PH 6.5 25% PEG400 | |||||||||||||||||||||||||
結晶化 | *PLUS 温度: 20 ℃ / 手法: 蒸気拡散法, シッティングドロップ法 | |||||||||||||||||||||||||
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: 2005年9月16日 |
放射 | プロトコル: MAD / 単色(M)・ラウエ(L): M / 散乱光タイプ: x-ray |
放射波長 | 波長: 0.9762 Å / 相対比: 1 |
反射 | 解像度: 2.1→20 Å / Num. obs: 57954 / % possible obs: 92.3 % / Observed criterion σ(I): -4 / 冗長度: 2.7 % / Rmerge(I) obs: 0.03 / Net I/σ(I): 12.7 |
反射 シェル | 解像度: 2.1→2.2 Å / 冗長度: 2 % / Rmerge(I) obs: 0.17 / Mean I/σ(I) obs: 3.5 / % possible all: 66.4 |
反射 | *PLUS Rmerge(I) obs: 0.033 |
反射 シェル | *PLUS % possible obs: 66.4 % / Rmerge(I) obs: 0.169 |
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解析
ソフトウェア |
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精密化 | 構造決定の手法: ![]() 詳細: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUES 1-17 ARE DISORDERED IN ALL COPIES OF RABEX-5 1-74. THE C-TERMINUS OF RABEX-5 1-74 IS ORDERED TO A VARIABLE DEGREE. RESIDUES 74-76 ...詳細: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUES 1-17 ARE DISORDERED IN ALL COPIES OF RABEX-5 1-74. THE C-TERMINUS OF RABEX-5 1-74 IS ORDERED TO A VARIABLE DEGREE. RESIDUES 74-76 OF UBIQUTIN ARE DISORDERED IN ALL COPIES
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溶媒の処理 | イオンプローブ半径: 0.8 Å / 減衰半径: 0.8 Å / VDWプローブ半径: 1.2 Å / 溶媒モデル: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
原子変位パラメータ | Biso mean: 44.95 Å2
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精密化ステップ | サイクル: LAST / 解像度: 2.1→20 Å
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拘束条件 |
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