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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: 2pkc | ||||||
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タイトル | CRYSTAL STRUCTURE OF CALCIUM-FREE PROTEINASE K AT 1.5 ANGSTROMS RESOLUTION | ||||||
![]() | PROTEINASE K | ||||||
![]() | HYDROLASE(SERINE PROTEINASE) | ||||||
機能・相同性 | ![]() peptidase K / serine-type endopeptidase activity / proteolysis / extracellular space / metal ion binding 類似検索 - 分子機能 | ||||||
生物種 | ![]() | ||||||
手法 | ![]() | ||||||
![]() | Mueller, A. / Hinrichs, W. / Wolf, W.M. / Saenger, W. | ||||||
![]() | ![]() タイトル: Crystal structure of calcium-free proteinase K at 1.5-A resolution. 著者: Muller, A. / Hinrichs, W. / Wolf, W.M. / Saenger, W. #1: ![]() タイトル: Long-Range Structural Changes in Proteinase K Triggered by Calcium Ion Removal 著者: Bajorath, J. / Raghunathan, S. / Hinrichs, W. / Saenger, W. #2: ![]() タイトル: Three-Dimensional Structure of Proteinase K at 0.15-Nm Resolution 著者: Betzel, C. / Pal, G.P. / Saenger, W. | ||||||
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 | ![]() | 62.6 KB | 表示 | ![]() |
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PDB形式 | ![]() | 49.6 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 | ![]() | 413 KB | 表示 | ![]() |
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文書・詳細版 | ![]() | 420.3 KB | 表示 | |
XML形式データ | ![]() | 14.7 KB | 表示 | |
CIF形式データ | ![]() | 21.1 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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単位格子 |
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Atom site foot note | 1: CIS PROLINE - PRO 171 2: RESIDUES SER 15, SER 219, AND SER 247, SHOWED TWOFOLD DISORDERED POSITIONS FOR ATOM OG, HENCE THEIR ALTERNATE INDICATORS ARE *A* AND *B*. THEY HAVE AN OCCUPANCY OF 0.5 EACH, AND WERE REFINED AS DESCRIBED ABOVE. 3: ONE WATER (HOH 322) WAS LOCATED PRECISELY ON AN ELEMENT OF SYMMETRY, THEREFORE, IT WAS GIVEN HALF THE OCCUPANCY IT WOULD HAVE HAD, IF NOT LOCATED ON THE AXIS (OCC.=0.35). 4: ALL ATOMS OF THE PEPTIDE SEQUENCE WERE LOCATED, EXCEPT FOR THE SIDE-CHAIN OF THE C-TERMINAL GLN (278), WHICH WAS ONLY FOUND UP TO CB. | ||||||||
Components on special symmetry positions |
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要素
#1: タンパク質 | 分子量: 28930.783 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 | ChemComp-NA / |
#3: 水 | ChemComp-HOH / |
構成要素の詳細 | THERE ARE THREE BENDS IN THIS STRUCTURE. S1: SER 79, GLY 83; S2: TRP 212, SER 216 (NESTED WITH T16); ...THERE ARE THREE BENDS IN THIS STRUCTURE. S1: SER 79, GLY 83; S2: TRP 212, SER 216 (NESTED WITH T16); S3: THR 244, ALA 248. |
配列の詳細 | THE PROTEIN SEQUENCE (279 AMINO ACIDS) IS THE SAME AS THAT OF THE NATIVE ENZYME PRESENTED IN ...THE PROTEIN SEQUENCE (279 AMINO ACIDS) IS THE SAME AS THAT OF THE NATIVE ENZYME PRESENTED IN PROTEIN DATA BANK ENTRY 2PRK. |
-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: 2.18 Å3/Da / 溶媒含有率: 43.47 % | ||||||||||||||||||||||||||||||||||||
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結晶化 | *PLUS pH: 7.5 / 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
反射 | *PLUS 最高解像度: 1.5 Å / 最低解像度: 10 Å / Num. obs: 33854 / % possible obs: 78 % / Observed criterion σ(I): 1 / Rmerge(I) obs: 0.147 |
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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: 0.201 / 最高解像度: 1.5 Å 詳細: THE OCCUPANCIES OF WATER OXYGENS COULD BE REFINED IN A LAST CYCLE OF REFINEMENT, BUT ONLY THOSE WITH OCCUPANCY GREATER THAN 0.5 WERE RETAINED. | ||||||||||||
精密化ステップ | サイクル: LAST / 最高解像度: 1.5 Å
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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: 1.5 Å / Rfactor obs: 0.201 | ||||||||||||
溶媒の処理 | *PLUS | ||||||||||||
原子変位パラメータ | *PLUS |