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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: 1dr5 | ||||||
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タイトル | CRYSTAL STRUCTURES OF ORGANOMERCURIAL-ACTIVATED CHICKEN LIVER DIHYDROFOLATE REDUCTASE COMPLEXES | ||||||
![]() | DIHYDROFOLATE REDUCTASE | ||||||
![]() | OXIDOREDUCTASE | ||||||
機能・相同性 | ![]() tetrahydrofolate metabolic process / response to methotrexate / dihydrofolate metabolic process / dihydrofolate reductase / dihydrofolate reductase activity / folic acid metabolic process / tetrahydrofolate biosynthetic process / one-carbon metabolic process / NADP binding / mRNA binding / mitochondrion 類似検索 - 分子機能 | ||||||
生物種 | ![]() ![]() | ||||||
手法 | ![]() | ||||||
![]() | Mctigue, M.A. / Davies /II, J.F. / Kaufman, B.T. / Xuong, N.-H. / Kraut, J. | ||||||
![]() | ![]() タイトル: Crystal Structures of Organomercurial-Activated Chicken Liver Dihydrofolate Reductase Complexes 著者: Mctigue, M.A. / Davies II, J.F. / Kaufman, B.T. / Xuong, N.-H. / Kraut, J. #1: ![]() タイトル: Crystal Structures of Recombinant Human Dihydrofolate Reductase Complexed with Folate and 5-Deazafolate 著者: Davies II, J.F. / Delcamp, T.J. / Prendergast, N.J. / Ashford, V.A. / Freisheim, J.H. / Kraut, J. #2: ![]() タイトル: Refined Crystal Structure of Escherichia Coli and Chicken Liver Dihydrofolate Reductase Containing Bound Trimethoprim 著者: Matthews, D.A. / Bolin, J.T. / Burridge, J.M. / Filman, D.J. / Volz, K.W. / Kaufman, B.T. / Beddell, C.R. / Champness, J.N. / Stammers, D.K. / Kraut, J. #3: ![]() タイトル: Dihydrofolate Reductase, the Stereochemistry of Inhibitor Selectivity 著者: Matthews, D.A. / Bolin, J.T. / Burridge, J.M. / Filman, D.J. / Volz, K.W. / Kraut, J. #4: ![]() タイトル: Crystal Structure of Avian Dihydrofolate Reductase Containing Phenyltriazine and Nadph 著者: Volz, K.W. / Matthews, D.A. / Alden, R.A. / Freer, S.T. / Hansch, C. / Kaufman, B.T. / Kraut, J. #5: ![]() タイトル: Primary Structure of Chicken Liver Dihydrofolate Reductase 著者: Kumar, A.A. / Blankenship, D.T. / Kaufman, B.T. / Freisheim, J.H. | ||||||
履歴 |
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Remark 650 | HELIX RESIDUES 21-26 FORM A LEFT-HANDED POLYPROLINE HELIX. RESIDUES LYS 108 AND VAL 109 PARTICIPATE ...HELIX RESIDUES 21-26 FORM A LEFT-HANDED POLYPROLINE HELIX. RESIDUES LYS 108 AND VAL 109 PARTICIPATE IN BOTH HELIX EP AND BETA STRAND E. | ||||||
Remark 700 | SHEET RESIDUES ASP 110 AND MET 111 FORM A BETA-BULGE IN STRAND E. RESIDUES VAL 115 AND GLY 116 FORM ...SHEET RESIDUES ASP 110 AND MET 111 FORM A BETA-BULGE IN STRAND E. RESIDUES VAL 115 AND GLY 116 FORM A BETA-BULGE IN STRAND E. TIGHT TURN 7 (RESIDUES 162-165) DISRUPT LAST STRAND OF SHEET INTO 2 STRANDS 8 AND 9. THIS STRAND IS CONTINUOUS IN (E. COLI). A BETA BULGE IS PRESENT HERE IN (L. CASEI). RESIDUES GLU 172 AND ILE 175 PARTICIPATE IN BOTH TIGHT-TURN 8 AND BETA STRANDS 7 AND 9. |
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構造の表示
構造ビューア | 分子: ![]() ![]() |
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PDB形式 | ![]() | 38.7 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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Atom site foot note | 1: SEE REMARK 6. 2: RESIDUES 21-26 FORM A LEFT-HANDED POLYPROLINE HELIX. 1DR5 3: RESIDUE 66 IS A CIS PROLINE. 4: RESIDUES LYS 108 AND VAL 109 PARTICIPATE IN BOTH HELIX EP AND BETA STRAND E. 5: RESIDUES ASP 110 AND MET 111 FORM A BETA-BULGE IN STRAND E. 6: RESIDUES VAL 115 AND GLY 116 FORM A BETA-BULGE IN STRAND E. 7: PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION GLY 116 - GLY 117 4.019 8: TIGHT TURN 7 (RESIDUES 162-165) DISRUPT LAST STRAND OF SHEET INTO 2 STRANDS 8 AND 9. THIS STRAND IS CONTINUOUS IN (E. COLI). A BETA BULGE IS PRESENT HERE IN (L. CASEI). 9: RESIDUES GLU 172 AND ILE 175 PARTICIPATE IN BOTH TIGHT-TURN 8 AND BETA STRANDS 7 AND 9. 10: RESIDUE 200 (CALCIUM ION) LIES ON THE CRYSTALLOGRAPHIC TWO-FOLD AT ONE-HALF OCCUPANCY. | ||||||||
Components on special symmetry positions |
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要素
#1: タンパク質 | 分子量: 21679.932 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-HG / |
#3: 化合物 | ChemComp-CA / |
#4: 化合物 | ChemComp-NAP / |
#5: 水 | ChemComp-HOH / |
構成要素の詳細 | CYSTEINE 11 HAS A MERCURY ATOM COVALENTLY BOUND TO SG IN TWO CONFORMATIONS. THE METHYL GROUP BOUND ...CYSTEINE 11 HAS A MERCURY ATOM COVALENTLY |
-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: 2.61 Å3/Da / 溶媒含有率: 52.94 % |
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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 |
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解析
ソフトウェア | 名称: PROLSQ / 分類: 精密化 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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精密化 | Rfactor obs: 0.16 / 最高解像度: 2.4 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
精密化ステップ | サイクル: LAST / 最高解像度: 2.4 Å
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拘束条件 |
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