SUMO-specific endopeptidase activity / SUMO is proteolytically processed / SUMO is conjugated to E1 (UBA2:SAE1) / deSUMOylase activity / protein desumoylation / SUMO is transferred from E1 to E2 (UBE2I, UBC9) / Vitamin D (calciferol) metabolism / SUMOylation of SUMOylation proteins / RHOF GTPase cycle / SUMOylation of RNA binding proteins ...SUMO-specific endopeptidase activity / SUMO is proteolytically processed / SUMO is conjugated to E1 (UBA2:SAE1) / deSUMOylase activity / protein desumoylation / SUMO is transferred from E1 to E2 (UBE2I, UBC9) / Vitamin D (calciferol) metabolism / SUMOylation of SUMOylation proteins / RHOF GTPase cycle / SUMOylation of RNA binding proteins / ubiquitin-like protein ligase binding / SUMOylation of DNA replication proteins / SUMOylation of transcription factors / protein sumoylation / SUMOylation of DNA damage response and repair proteins / regulation of mRNA stability / SUMOylation of chromatin organization proteins / SUMOylation of transcription cofactors / apoptotic signaling pathway / SUMOylation of intracellular receptors / PML body / Formation of Incision Complex in GG-NER / protein tag activity / activation of cysteine-type endopeptidase activity involved in apoptotic process / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / Processing of DNA double-strand break ends / nuclear membrane / endopeptidase activity / 加水分解酵素; プロテアーゼ; ペプチド結合加水分解酵素; システインプロテアーゼ / focal adhesion / ubiquitin protein ligase binding / positive regulation of transcription by RNA polymerase II / proteolysis / RNA binding / nucleoplasm / nucleus / cytoplasm 類似検索 - 分子機能
THE EXTRA RESIDUE AT POSITION 593 IN CHAINS A AND B IS A KNOWN CONFLICT IN UNIPROT AND IS DESCRIBED ...THE EXTRA RESIDUE AT POSITION 593 IN CHAINS A AND B IS A KNOWN CONFLICT IN UNIPROT AND IS DESCRIBED IN PUBMED ID: 12477932.
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: 0.933 Å / 相対比: 1
反射
解像度: 3.2→120 Å / Num. obs: 13469 / % possible obs: 100 % / Observed criterion σ(I): 0 / 冗長度: 8 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 19
反射 シェル
解像度: 3.2→3.3 Å / 冗長度: 8 % / Rmerge(I) obs: 0.44 / Mean I/σ(I) obs: 3 / % possible all: 100
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解析
ソフトウェア
名称
バージョン
分類
REFMAC
5.2.0019
精密化
MOSFLM
データ削減
SCALA
データスケーリング
CCP4
位相決定
精密化
構造決定の手法: 分子置換 / 解像度: 3.2→46.98 Å / Cor.coef. Fo:Fc: 0.926 / Cor.coef. Fo:Fc free: 0.913 / SU B: 54.553 / SU ML: 0.378 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / ESU R: 0.581 / ESU R Free: 0.407 / 立体化学のターゲット値: MAXIMUM LIKELIHOOD 詳細: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. ONLY AN OVERALL B FACTOR REFINED THIS REPLACES PREVIOUS ENTRY WHICH HAD SEQUENCE CONFLICTS. THERE IS COVALENT LINK BETWEEN CYS A 603 (SENP1) ...詳細: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. ONLY AN OVERALL B FACTOR REFINED THIS REPLACES PREVIOUS ENTRY WHICH HAD SEQUENCE CONFLICTS. THERE IS COVALENT LINK BETWEEN CYS A 603 (SENP1) AND GLY B 92 (SUMO) THE DICTIONARY IS INCLUDED IN ENTRY
Rfactor
反射数
%反射
Selection details
Rfree
0.288
714
5 %
RANDOM
Rwork
0.272
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-
-
obs
0.273
13468
99 %
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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: BABINET MODEL WITH MASK