+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 1bal | ||||||
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タイトル | THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE E3-BINDING DOMAIN OF THE DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE CORE FROM THE 2-OXOGLUTARATE DEHYDROGENASE MULTIENZYME COMPLEX OF (ESCHERICHIA COLI) | ||||||
要素 | DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE | ||||||
キーワード | GLYCOLYSIS | ||||||
機能・相同性 | 機能・相同性情報 L-lysine catabolic process to acetyl-CoA via saccharopine / dihydrolipoyllysine-residue succinyltransferase / dihydrolipoyllysine-residue succinyltransferase activity / lipoic acid binding / oxoglutarate dehydrogenase complex / tricarboxylic acid cycle / cytoplasm / cytosol 類似検索 - 分子機能 | ||||||
生物種 | Escherichia coli (大腸菌) | ||||||
手法 | 溶液NMR | ||||||
データ登録者 | Clore, G.M. / Robien, M.A. / Gronenborn, A.M. | ||||||
引用 | ジャーナル: Biochemistry / 年: 1992 タイトル: Three-dimensional solution structure of the E3-binding domain of the dihydrolipoamide succinyltransferase core from the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli. 著者: Robien, M.A. / Clore, G.M. / Omichinski, J.G. / Perham, R.N. / Appella, E. / Sakaguchi, K. / Gronenborn, A.M. | ||||||
履歴 |
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-構造の表示
構造ビューア | 分子: MolmilJmol/JSmol |
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-ダウンロードとリンク
-ダウンロード
PDBx/mmCIF形式 | 1bal.cif.gz | 942.1 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb1bal.ent.gz | 802 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 1bal.json.gz | ツリー表示 | PDBx/mmJSON形式 | |
その他 | その他のダウンロード |
-検証レポート
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/ba/1bal ftp://data.pdbj.org/pub/pdb/validation_reports/ba/1bal | HTTPS FTP |
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-関連構造データ
-リンク
-集合体
登録構造単位 |
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1 |
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NMR アンサンブル |
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-要素
#1: タンパク質 | 分子量: 5509.133 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) Escherichia coli (大腸菌) 参照: UniProt: P07016, UniProt: P0AFG6*PLUS, dihydrolipoyllysine-residue succinyltransferase |
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-実験情報
-実験
実験 | 手法: 溶液NMR |
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-試料調製
結晶化 | *PLUS 手法: other / 詳細: NMR |
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-解析
精密化 | ソフトェア番号: 1 詳細: DETAILS OF THE STRUCTURE DETERMINATION AND ALL STRUCTURAL STATISTICS ARE GIVEN IN THE PAPER CITED ON *JRNL* RECORDS ABOVE. THE STRUCTURES ARE BASED ON 630 INTERPROTON DISTANCE RESTRAINTS ...詳細: DETAILS OF THE STRUCTURE DETERMINATION AND ALL STRUCTURAL STATISTICS ARE GIVEN IN THE PAPER CITED ON *JRNL* RECORDS ABOVE. THE STRUCTURES ARE BASED ON 630 INTERPROTON DISTANCE RESTRAINTS DERIVED FROM NOE MEASUREMENTS; AND 46 PHI AND 35 PSI BACKBONE TORSION ANGLE RESTRAINTS AND 20 CHI1 SIDE CHAIN TORSION ANGLE RESTRAINTS DERIVED FROM COUPLING CONSTANTS AND NOE DATA. THE LATTER ARE OBTAINED USING THE CONFORMATIONAL GRID SEARCH PROGRAM STEREOSEARCH (M.NILGES,G.M.CLORE,A.M.GRONENBORN (1990) BIOPOLYMERS 29, 813-822). THE METHOD USED TO DETERMINE THE STRUCTURES IS THE HYBRID METRIC MATRIX DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING METHOD (M.NILGES,G.M.CLORE, A.M.GRONENBORN, FEBS LETT. 229, 317-324 (1988)). THIS ENTRY CONTAINS THE COORDINATES OF 56 INDIVIDUAL SIMULATED ANNEALING STRUCTURES. THE COORDINATES OF THE (SA)R MINIMIZED AVERAGE STRUCTURE ARE PRESENTED IN PROTEIN DATA BANK ENTRY 1BBL. (SA)R RESTRAINED MINIMIZED MEAN STRUCTURE WAS DERIVED BY AVERAGING THE COORDINATES OF THE INDIVIDUAL SA STRUCTURES BEST FITTED TO RESIDUES 14 - 30 AND 39 - 47, AND SUBJECTING THE RESULTING COORDINATES TO RESTRAINED MINIMIZATION. RESIDUES 1 - 11 AND 48 - 51 ARE COMPLETELY DISORDERED AND ARE NOT INCLUDED IN THE COORDINATE SET. THE QUANTITY PRESENTED IN COLUMNS 61 - 66 OF ENTRY 1BBL HAS NO MEANING. THE QUANTITY PRESENTED IN COLUMNS 61 - 66 OF THIS ENTRY REPRESENTS THE ATOMIC RMS DEVIATIONS OF THE 56 INDIVIDUAL STRUCTURES ABOUT THE MEAN STRUCTURE. ALL THE INTERPROTON DISTANCE AND TORSION ANGLE RESTRAINTS ARE PRESENTED IN PROTEIN DATA BANK ENTRY R1BBLMR. |
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NMRアンサンブル | 登録したコンフォーマーの数: 56 |