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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: 1mae | ||||||
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タイトル | The Active Site Structure of Methylamine Dehydrogenase: Hydrazines Identify C6 as the Reactive Site of the Tryptophan Derived Quinone Cofactor | ||||||
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![]() | OXIDOREDUCTASE(CHNH2(D)-DEAMINATING) | ||||||
機能・相同性 | ![]() methylamine dehydrogenase (amicyanin) / methylamine dehydrogenase (amicyanin) activity / methylamine metabolic process / aliphatic amine dehydrogenase activity / amine metabolic process / outer membrane-bounded periplasmic space / periplasmic space 類似検索 - 分子機能 | ||||||
生物種 | ![]() | ||||||
手法 | ![]() | ||||||
![]() | Huizinga, E.G. / Vellieux, F.M.D. / Hol, W.G.J. | ||||||
![]() | ![]() タイトル: Active site structure of methylamine dehydrogenase: hydrazines identify C6 as the reactive site of the tryptophan-derived quinone cofactor. 著者: Huizinga, E.G. / van Zanten, B.A. / Duine, J.A. / Jongejan, J.A. / Huitema, F. / Wilson, K.S. / Hol, W.G. #1: ![]() タイトル: Crystallographic Investigations of the Tryptophan-Derived Cofactor in the Quinoprotein Methylamine Dehydrogenase 著者: Chen, L. / Mathews, F.S. / Davidson, V.L. / Huizinga, E.G. / Vellieux, F.M.D. / Duine, J.A. / Hol, W.G.J. #2: ![]() タイトル: Structure of Quinoprotein Methylamine Dehydrogenase at 2.25 Angstroms Resolution 著者: Vellieux, F.M.D. / Huitema, F. / Groendijk, H. / Kalk, K.H. / Frank, J. / Jongejan, J.A. / Duine, J.A. / Petratos, K. / Drenth, J. / Hol, W.G.J. #3: ![]() タイトル: Purification, Crystallization and Preliminary X-Ray Investigation of Quinoprotein Methylamine Dehydrogenase from Thiobacillus Versutus 著者: Vellieux, F.M.D. / Frank, J. / Swarte, M.B.A. / Groendijk, H. / Duine, J.A. / Drenth, J. / Hol, W.G.J. | ||||||
履歴 |
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構造の表示
構造ビューア | 分子: ![]() ![]() |
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PDBx/mmCIF形式 | ![]() | 53.3 KB | 表示 | ![]() |
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PDB形式 | ![]() | 35.3 KB | 表示 | ![]() |
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その他 | ![]() |
-検証レポート
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
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-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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詳細 | THE MOLECULE IS NORMALLY A TETRAMER. THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT CONSISTS OF ONE-HALF OF THE TETRAMER, NAMELY ONE LIGHT CHAIN *L* AND ONE HEAVY CHAIN *H*. TO GENERATE THE FULL MOLECULE, THE FOLLOWING CRYSTALLOGRAPHIC TWO-FOLD OPERATION MUST BE APPLIED TO THE LIGHT AND HEAVY CHAINS PRESENTED IN THIS ENTRY -0.5 0.866025 0.0 0.0 0.866025 0.5 0.0 0.0 0.0 0.0 -1.0 208.368 |
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要素
#1: タンパク質 | 分子量: 13654.172 Da / 分子数: 1 / 由来タイプ: 組換発現 由来: (組換発現) ![]() 参照: UniProt: P22641, EC: 1.4.99.3 |
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#2: タンパク質 | 分子量: 38031.996 Da / 分子数: 1 / 由来タイプ: 組換発現 由来: (組換発現) ![]() 参照: UniProt: P23006, EC: 1.4.99.3 |
#3: 化合物 | ChemComp-HDZ / |
#4: 水 | ChemComp-HOH / |
構成要素の詳細 | THE L SUBUNIT CONTAINS THE SIDE CHAIN DERIVED COFACTOR TRYPTOPHYL TRYTOPHAN-QUINONE (MCINTYRE ET AL. ...THE L SUBUNIT CONTAINS THE SIDE CHAIN DERIVED COFACTOR TRYPTOPHYL |
配列の詳細 | FOR THE H-SUBUNIT THE SEQUENCE GIVEN IN THE SEQRES RECORDS IS AN *X-RAY SEQUENCE*, WHICH WAS ...FOR THE H-SUBUNIT THE SEQUENCE GIVEN IN THE SEQRES RECORDS IS AN *X-RAY SEQUENCE*, WHICH WAS ESTABLISHE |
-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: 4.91 Å3/Da / 溶媒含有率: 74.93 % | |||||||||||||||||||||||||
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結晶化 | *PLUS 温度: 4 ℃ / pH: 5 / 手法: 蒸気拡散法, ハンギングドロップ法詳細: taken from Ubbink, M. et al (1991). Eur. J. Biochem., 202, 1003-1012. | |||||||||||||||||||||||||
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: 2.8 Å / Num. obs: 25377 / % possible obs: 95.7 % / Num. measured all: 125106 / Rmerge(I) obs: 0.073 |
反射 シェル | *PLUS % possible obs: 92.4 % / Rmerge(I) obs: 0.157 |
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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: 0.183 / 最高解像度: 2.8 Å 詳細: ALTHOUGH CLEAR EXTRA DENSITY WAS OBSERVED IN THE ACTIVE SITE, SUFFICIENT DENSITY WAS NOT PRESENT TO ACCOMMODATE THE COMPLETE INHIBITOR (FOR DETAILS SEE ARTICLE SPECIFIED IN REFERENCE 1). TWO ...詳細: ALTHOUGH CLEAR EXTRA DENSITY WAS OBSERVED IN THE ACTIVE SITE, SUFFICIENT DENSITY WAS NOT PRESENT TO ACCOMMODATE THE COMPLETE INHIBITOR (FOR DETAILS SEE ARTICLE SPECIFIED IN REFERENCE 1). TWO ATOMS OF THE INHIBITOR (MHZ), TENTATIVELY IDENTIFIED AS NITROGENS HAVE BEEN INCLUDED IN THE MODEL AS HDZ. | ||||||||||||||||||||||||||||||
精密化ステップ | サイクル: LAST / 最高解像度: 2.8 Å
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拘束条件 |
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