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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: 2n9e | ||||||
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タイトル | Structure of SUMO-2 bound to phosphorylated RAP80 SIM | ||||||
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![]() | PROTEIN BINDING / SUMO-2-phosphoRAP80 / SUMO-2-phosphoSIM | ||||||
機能・相同性 | ![]() BRCA1-A complex / SUMO is proteolytically processed / SUMO is conjugated to E1 (UBA2:SAE1) / SUMO is transferred from E1 to E2 (UBE2I, UBC9) / ubiquitin-modified histone reader activity / Vitamin D (calciferol) metabolism / SUMOylation of SUMOylation proteins / mitotic G2/M transition checkpoint / SUMOylation of RNA binding proteins / SUMO transferase activity ...BRCA1-A complex / SUMO is proteolytically processed / SUMO is conjugated to E1 (UBA2:SAE1) / SUMO is transferred from E1 to E2 (UBE2I, UBC9) / ubiquitin-modified histone reader activity / Vitamin D (calciferol) metabolism / SUMOylation of SUMOylation proteins / mitotic G2/M transition checkpoint / SUMOylation of RNA binding proteins / SUMO transferase activity / K63-linked polyubiquitin modification-dependent protein binding / response to ionizing radiation / DNA repair-dependent chromatin remodeling / mitotic G2 DNA damage checkpoint signaling / ubiquitin-like protein ligase binding / SUMOylation of transcription factors / SUMOylation of DNA replication proteins / protein sumoylation / postsynaptic cytosol / SUMOylation of DNA damage response and repair proteins / regulation of DNA repair / presynaptic cytosol / SUMOylation of transcription cofactors / positive regulation of DNA repair / SUMOylation of chromatin organization proteins / hippocampal mossy fiber to CA3 synapse / Regulation of endogenous retroelements by KRAB-ZFP proteins / SUMOylation of intracellular receptors / Nonhomologous End-Joining (NHEJ) / Formation of Incision Complex in GG-NER / protein tag activity / G2/M DNA damage checkpoint / Metalloprotease DUBs / PML body / GABA-ergic synapse / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / site of double-strand break / double-strand break repair / Processing of DNA double-strand break ends / histone binding / nuclear body / negative regulation of DNA-templated transcription / ubiquitin protein ligase binding / glutamatergic synapse / positive regulation of transcription by RNA polymerase II / DNA binding / RNA binding / zinc ion binding / nucleoplasm / nucleus 類似検索 - 分子機能 | ||||||
生物種 | ![]() | ||||||
手法 | 溶液NMR / molecular dynamics, torsion angle dynamics | ||||||
![]() | Anamika, A. / Spyracopoulos, L. | ||||||
![]() | ![]() タイトル: Molecular Basis for Phosphorylation-dependent SUMO Recognition by the DNA Repair Protein RAP80. 著者: Anamika / Spyracopoulos, L. | ||||||
履歴 |
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構造の表示
構造ビューア | 分子: ![]() ![]() |
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-検証レポート
文書・要旨 | ![]() | 428.4 KB | 表示 | ![]() |
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文書・詳細版 | ![]() | 643.5 KB | 表示 | |
XML形式データ | ![]() | 44.3 KB | 表示 | |
CIF形式データ | ![]() | 69.1 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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その他のデータベース |
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集合体
登録構造単位 | ![]()
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NMR アンサンブル |
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要素
#1: タンパク質・ペプチド | 分子量: 1580.415 Da / 分子数: 1 / 断片: SUMO interacting motif (UNP residues 37-49) / 由来タイプ: 合成 / 由来: (合成) ![]() |
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#2: タンパク質 | 分子量: 10886.217 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() |
Has protein modification | Y |
-実験情報
-実験
実験 | 手法: 溶液NMR | ||||||||||||||||||||||||||||||||||||
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NMR実験 |
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試料調製
詳細 | 内容: 1.2 mM peptide, 0.4 mM [U-100% 13C; U-100% 15N] protein, 90% H2O/10% D2O 溶媒系: 90% H2O/10% D2O | ||||||||||||
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試料 |
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試料状態 | イオン強度: 25 / pH: 7.3 / 圧: ambient / 温度: 298 K |
-NMR測定
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解析
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精密化 | 手法: molecular dynamics, torsion angle dynamics / ソフトェア番号: 1 | ||||||||||||||||||||||||
NMR constraints | NOE constraints total: 45 / NOE intraresidue total count: 3 / NOE long range total count: 0 / NOE medium range total count: 6 / NOE sequential total count: 21 / Protein chi angle constraints total count: 30 / Protein other angle constraints total count: 0 / Protein phi angle constraints total count: 68 / Protein psi angle constraints total count: 68 | ||||||||||||||||||||||||
代表構造 | 選択基準: closest to the average | ||||||||||||||||||||||||
NMRアンサンブル | コンフォーマー選択の基準: structures with the lowest energy 計算したコンフォーマーの数: 20 / 登録したコンフォーマーの数: 20 / Maximum lower distance constraint violation: 0 Å / Maximum upper distance constraint violation: 0 Å | ||||||||||||||||||||||||
NMR ensemble rms | Distance rms dev: 0 Å / Distance rms dev error: 2 Å |