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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: 1sda | ||||||
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タイトル | CRYSTAL STRUCTURE OF PEROXYNITRITE-MODIFIED BOVINE CU,ZN SUPEROXIDE DISMUTASE | ||||||
![]() | COPPER,ZINC SUPEROXIDE DISMUTASE | ||||||
![]() | OXIDOREDUCTASE(COPPER) | ||||||
機能・相同性 | ![]() Platelet degranulation / Detoxification of Reactive Oxygen Species / neurofilament cytoskeleton organization / protein phosphatase 2B binding / relaxation of vascular associated smooth muscle / response to superoxide / peripheral nervous system myelin maintenance / retina homeostasis / negative regulation of cholesterol biosynthetic process / hydrogen peroxide biosynthetic process ...Platelet degranulation / Detoxification of Reactive Oxygen Species / neurofilament cytoskeleton organization / protein phosphatase 2B binding / relaxation of vascular associated smooth muscle / response to superoxide / peripheral nervous system myelin maintenance / retina homeostasis / negative regulation of cholesterol biosynthetic process / hydrogen peroxide biosynthetic process / auditory receptor cell stereocilium organization / regulation of protein kinase activity / myeloid cell homeostasis / muscle cell cellular homeostasis / superoxide metabolic process / heart contraction / superoxide dismutase / positive regulation of catalytic activity / transmission of nerve impulse / superoxide dismutase activity / regulation of multicellular organism growth / response to axon injury / ovarian follicle development / embryo implantation / dendrite cytoplasm / removal of superoxide radicals / reactive oxygen species metabolic process / glutathione metabolic process / : / regulation of mitochondrial membrane potential / positive regulation of cytokine production / locomotory behavior / sensory perception of sound / response to hydrogen peroxide / regulation of blood pressure / protein polyubiquitination / ubiquitin-protein transferase activity / peroxisome / protein-folding chaperone binding / response to heat / cytoplasmic vesicle / spermatogenesis / proteasome-mediated ubiquitin-dependent protein catabolic process / response to ethanol / intracellular iron ion homeostasis / negative regulation of neuron apoptotic process / positive regulation of MAPK cascade / copper ion binding / neuronal cell body / protein homodimerization activity / protein-containing complex / mitochondrion / zinc ion binding / nucleus / cytoplasm / cytosol 類似検索 - 分子機能 | ||||||
生物種 | ![]() ![]() | ||||||
手法 | ![]() | ||||||
![]() | Smith, C.D. / Carson, M. / Van Der Woerd, M. / Chen, J. / Ischiropoulos, H. / Beckman, J.S. | ||||||
![]() | ![]() タイトル: Crystal structure of peroxynitrite-modified bovine Cu,Zn superoxide dismutase. 著者: Smith, C.D. / Carson, M. / van der Woerd, M. / Chen, J. / Ischiropoulos, H. / Beckman, J.S. #1: ![]() タイトル: Peroxynitrite-Mediated Tyrosine Nitration Catalyzed by Superoxide Dismutase 著者: Ischiropoulos, H. / Zhu, L. / Chen, J. / Tsai, M. / Martin, J.C. / Smith, C.D. / Beckman, J.S. #2: ![]() タイトル: Determination and Analysis of the 2 Angstroms Structure of Copper, Zinc Superoxide Dismutase 著者: Tainer, J.A. / Getzoff, E.D. / Beem, K.M. / Richardson, J.S. / Richardson, D.C. | ||||||
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 | ![]() | 114 KB | 表示 | ![]() |
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PDB形式 | ![]() | 95.4 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 | ![]() | 390.6 KB | 表示 | ![]() |
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文書・詳細版 | ![]() | 401.9 KB | 表示 | |
XML形式データ | ![]() | 13.5 KB | 表示 | |
CIF形式データ | ![]() | 21 KB | 表示 | |
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-関連構造データ
類似構造データ |
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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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2 | ![]()
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単位格子 |
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非結晶学的対称性 (NCS) | NCS oper:
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詳細 | THE TRANSFORMATION WHICH WILL PLACE THE YELLOW MONOMER INTO BEST ALIGNMENT WITH THE ORANGE MONOMER IS GIVEN BY MTRIX 1 BELOW. THE TRANSFORMATION WHICH WILL PLACE THE BLUE MONOMER INTO BEST ALIGNMENT WITH THE ORANGE MONOMER IS GIVEN BY MTRIX 2 BELOW. THE TRANSFORMATION WHICH WILL PLACE THE GREEN MONOMER INTO BEST ALIGNMENT WITH THE ORANGE MONOMER IS GIVEN BY MTRIX 3 BELOW. |
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要素
#1: タンパク質 | 分子量: 15644.371 Da / 分子数: 4 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() #2: 化合物 | ChemComp-CU / #3: 化合物 | ChemComp-ZN / #4: 水 | ChemComp-HOH / | 構成要素の詳細 | EACH MONOMER CONTAINS AN ACETYL GROUP BLOCKING THE N-TERMINUS, 151 RESIDUES, ZN ION, CU ION AND A ...EACH MONOMER CONTAINS AN ACETYL GROUP BLOCKING THE N-TERMINUS, 151 RESIDUES, ZN ION, CU ION AND A WATER MOLECULE. THE DOMINANT STRUCTURAL | |
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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: 2.42 Å3/Da / 溶媒含有率: 49.13 % | ||||||||||||||||||||||||||||||
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結晶化 | *PLUS 温度: 5 ℃ / pH: 7.4 / 手法: 蒸気拡散法 | ||||||||||||||||||||||||||||||
溶液の組成 | *PLUS
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-データ収集
反射 | *PLUS 最高解像度: 2.5 Å / Rmerge(I) obs: 0.323 |
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解析
ソフトウェア |
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精密化 | Rfactor Rwork: 0.187 / Rfactor obs: 0.187 / 最高解像度: 2.5 Å 詳細: COORDINATES IN THE A*BC ORTHOGONAL FRAME ARE PRESENTED BELOW FOR FOUR MONOMERS. ONE ENZYMATICALLY ACTIVE SOD DIMER COMPRISES MONOMERS ORANGE (CHAIN INDICATOR O) AND YELLOW (Y). ANOTHER DIMER ...詳細: COORDINATES IN THE A*BC ORTHOGONAL FRAME ARE PRESENTED BELOW FOR FOUR MONOMERS. ONE ENZYMATICALLY ACTIVE SOD DIMER COMPRISES MONOMERS ORANGE (CHAIN INDICATOR O) AND YELLOW (Y). ANOTHER DIMER COMPRISES MONOMERS BLUE (B) AND GREEN (G). FOR THE ACTIVE SITE HISTIDINES, THE PLACEMENT OF HYDROGENS WAS AS FOLLOWS FOR X-PLOR REFINEMENT: HIS 46, 118 HAVE A HYDROGEN ON THE DELTA NITROGEN; HIS 44, 69, 78 HAVE A HYDROGEN ON THE EPSILON NITROGEN; AND HIS 61 IS NEGATIVELY CHARGED WITH NEITHER HYDROGEN. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
精密化ステップ | サイクル: LAST / 最高解像度: 2.5 Å
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拘束条件 |
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ソフトウェア | *PLUS 名称: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
精密化 | *PLUS 最低解像度: 6 Å / Rfactor obs: 0.187 / Rfactor Rwork: 0.187 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
溶媒の処理 | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
原子変位パラメータ | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
拘束条件 | *PLUS タイプ: x_angle_d / Dev ideal: 1.23 |