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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: 1can | ||||||
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タイトル | CRYSTALLOGRAPHIC STUDIES OF THE BINDING OF PROTONATED AND UNPROTONATED INHIBITORS TO CARBONIC ANHYDRASE USING HYDROGEN SULPHIDE AND NITRATE ANIONS | ||||||
![]() | CARBONIC ANHYDRASE II | ||||||
![]() | LYASE(OXO-ACID) | ||||||
機能・相同性 | ![]() positive regulation of cellular pH reduction / positive regulation of dipeptide transmembrane transport / regulation of monoatomic anion transport / secretion / cyanamide hydratase / cyanamide hydratase activity / arylesterase activity / regulation of chloride transport / Reversible hydration of carbon dioxide / morphogenesis of an epithelium ...positive regulation of cellular pH reduction / positive regulation of dipeptide transmembrane transport / regulation of monoatomic anion transport / secretion / cyanamide hydratase / cyanamide hydratase activity / arylesterase activity / regulation of chloride transport / Reversible hydration of carbon dioxide / morphogenesis of an epithelium / angiotensin-activated signaling pathway / regulation of intracellular pH / positive regulation of synaptic transmission, GABAergic / carbonic anhydrase / carbonate dehydratase activity / carbon dioxide transport / Erythrocytes take up oxygen and release carbon dioxide / Erythrocytes take up carbon dioxide and release oxygen / neuron cellular homeostasis / apical part of cell / myelin sheath / extracellular exosome / zinc ion binding / plasma membrane / cytosol / cytoplasm 類似検索 - 分子機能 | ||||||
生物種 | ![]() | ||||||
手法 | ![]() | ||||||
![]() | Mangani, S. / Hakansson, K. | ||||||
![]() | ![]() タイトル: Crystallographic studies of the binding of protonated and unprotonated inhibitors to carbonic anhydrase using hydrogen sulphide and nitrate anions. 著者: Mangani, S. / Hakansson, K. | ||||||
履歴 |
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Remark 700 | SHEET SHEET B1 OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET ...SHEET SHEET B1 OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS *B1A* AND *B1B* ARE DEFINED. STRANDS 5, 6, 7, 8, 9, AND 10 OF B1A ARE IDENTICAL TO STRANDS 2, 3, 4, 5, 6, AND 7 OF B1B, RESPECTIVELY. |
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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 | ![]() | 72.7 KB | 表示 | ![]() |
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PDB形式 | ![]() | 52.2 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 | ![]() | 428.5 KB | 表示 | ![]() |
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文書・詳細版 | ![]() | 436.1 KB | 表示 | |
XML形式データ | ![]() | 17.4 KB | 表示 | |
CIF形式データ | ![]() | 24.3 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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Atom site foot note | 1: RESIDUES PRO 30 AND PRO 202 ARE CIS PROLINES. / 2: RESIDUES 2 AND 3 HAVE PARTIAL OCCUPANCY. 3: SOME MERCURY++ FROM THE CRYSTALLIZATION REMAINS. (HG, MTL RESIDUE 510) |
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要素
#1: タンパク質 | 分子量: 29183.902 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() | ||||||||
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#2: 化合物 | #3: 化合物 | ChemComp-NO3 / | #4: 水 | ChemComp-HOH / | Has protein modification | Y | 配列の詳細 | RESIDUES 125 AND 127 ARE ADJACENT IN THE SEQUENCE. | |
-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: 2.15 Å3/Da / 溶媒含有率: 42.89 % | ||||||||||||||||||||
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結晶化 | 温度: 277 K 詳細: THIS IS THE HIGH-ACTIVITY ERYTHROCYTIC FORM OF HUMAN CARBONIC ANHYDRASE, CARBONIC ANHYDRASE II, OR CAII. CRYSTALLIZED IN 50 MM TRIS-HCL 2.4 M AMMONIUM SULFATE PH 8.5 AND 1 MM HGCL2 AT 4 DEG C ...詳細: THIS IS THE HIGH-ACTIVITY ERYTHROCYTIC FORM OF HUMAN CARBONIC ANHYDRASE, CARBONIC ANHYDRASE II, OR CAII. CRYSTALLIZED IN 50 MM TRIS-HCL 2.4 M AMMONIUM SULFATE PH 8.5 AND 1 MM HGCL2 AT 4 DEG C (TILANDER, B., STRANDBERG, B. AND FRIDBORG, K. (1965). CRYSTAL STRUCTURE ON HUMAN ERYTHROCYTIC CARBONIC ANHYDRASE C. J. MOL. BIOL. 12, 740-760.) THE MERCURY IS SUBSEQUENTLY REMOVED BY MERCAPTOETHANOL. THE CRYSTAL IS SOAKED IN 0.6M KNO3 80 MM CITRATE 3M AMMONIUM SULFATE PH 6.0., temperature 277K | ||||||||||||||||||||
結晶化 | *PLUS 温度: 0-5 ℃ / pH: 8.5 / 手法: microdialysis詳細: referred to 'Tilander,B.', (1965) J.Mol.Biol., 12, 740. | ||||||||||||||||||||
溶液の組成 | *PLUS
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-データ収集
放射 | 散乱光タイプ: x-ray |
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放射波長 | 相対比: 1 |
反射 | *PLUS 最高解像度: 1.9 Å / Num. obs: 19792 / % possible obs: 90.3 % / Num. measured all: 55815 / Rmerge(I) obs: 0.058 |
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解析
ソフトウェア | 名称: TNT / 分類: 精密化 | ||||||||||||||||||||||||||||||
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精密化 | Rfactor obs: 0.141 / 最高解像度: 1.9 Å | ||||||||||||||||||||||||||||||
精密化ステップ | サイクル: LAST / 最高解像度: 1.9 Å
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拘束条件 |
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ソフトウェア | *PLUS 名称: TNT / 分類: refinement | ||||||||||||||||||||||||||||||
精密化 | *PLUS 最高解像度: 1.9 Å / Num. reflection obs: 18704 / σ(I): 2 / Rfactor obs: 0.141 | ||||||||||||||||||||||||||||||
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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