1SR5
 
 | | ANTITHROMBIN-ANHYDROTHROMBIN-HEPARIN TERNARY COMPLEX STRUCTURE | | 分子名称: | 2,3,4,6-tetra-O-sulfonato-alpha-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, 4-deoxy-2,3,6-tri-O-methyl-alpha-D-xylo-hexopyranose-(1-4)-2,3,6-tri-O-methyl-beta-D-glucopyranose-(1-4)-2,3-di-O-methyl-6-O-sulfo-alpha-D-glucopyranose-(1-4)-(2R,3R,4S,5S,6S)-6-(dihydroxymethyl)-3,4-dimethoxytetrahydro-2H-pyran-2,5-diol-(1-4)-2,3,6-tri-O-sulfo-alpha-D-glucopyranose-(1-4)-(2R,3R,4S,5S,6R)-6-(dihydroxymethyl)-3,4-dimethoxytetrahydro-2H-pyran-2,5-diol-(1-4)-1,5-anhydro-3-O-methyl-2,6-di-O-sulfo-D-glucitol, ... | | 著者 | Dementiev, A, Petitou, M, Gettins, P.G. | | 登録日 | 2004-03-22 | | 公開日 | 2004-08-17 | | 最終更新日 | 2023-08-23 | | 実験手法 | X-RAY DIFFRACTION (3.1 Å) | | 主引用文献 | The ternary complex of antithrombin-anhydrothrombin-heparin reveals the basis of inhibitor specificity.
Nat.Struct.Mol.Biol., 11, 2004
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1RNJ
 | | Crystal structure of inactive mutant dUTPase complexed with substrate analogue imido-dUTP | | 分子名称: | 2'-DEOXYURIDINE 5'-ALPHA,BETA-IMIDO-TRIPHOSPHATE, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, Deoxyuridine 5'-triphosphate nucleotidohydrolase, ... | | 著者 | Barabas, O, Pongracz, V, Kovari, J, Wilmanns, M, Vertessy, B.G. | | 登録日 | 2003-12-01 | | 公開日 | 2004-09-07 | | 最終更新日 | 2023-08-23 | | 実験手法 | X-RAY DIFFRACTION (1.7 Å) | | 主引用文献 | Structural Insights into the Catalytic Mechanism of Phosphate Ester Hydrolysis by dUTPase.
J.Biol.Chem., 279, 2004
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1RN8
 | | Crystal structure of dUTPase complexed with substrate analogue imido-dUTP | | 分子名称: | 2'-DEOXYURIDINE 5'-ALPHA,BETA-IMIDO-TRIPHOSPHATE, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ACETATE ION, ... | | 著者 | Barabas, O, Pongracz, V, Kovari, J, Wilmanns, M, Vertessy, B.G. | | 登録日 | 2003-12-01 | | 公開日 | 2004-09-07 | | 最終更新日 | 2023-09-20 | | 実験手法 | X-RAY DIFFRACTION (1.93 Å) | | 主引用文献 | Structural Insights into the Catalytic Mechanism of Phosphate Ester Hydrolysis by dUTPase.
J.Biol.Chem., 279, 2004
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1SEH
 | | Crystal structure of E. coli dUTPase complexed with the product dUMP | | 分子名称: | 2'-DEOXYURIDINE 5'-MONOPHOSPHATE, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, Deoxyuridine 5'-triphosphate nucleotidohydrolase | | 著者 | Barabas, O, Kovari, J, Pongracz, V, Wilmanns, M, Vertessy, B.G. | | 登録日 | 2004-02-17 | | 公開日 | 2004-09-07 | | 最終更新日 | 2023-10-25 | | 実験手法 | X-RAY DIFFRACTION (1.47 Å) | | 主引用文献 | Structural Insights into the Catalytic Mechanism of Phosphate Ester Hydrolysis by dUTPase
J.Biol.Chem., 279, 2004
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1SYL
 | | Crystal structure of inactive mutant dUTPase complexed with substrate dUTP | | 分子名称: | 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, DEOXYURIDINE-5'-TRIPHOSPHATE, Deoxyuridine 5'-triphosphate nucleotidohydrolase, ... | | 著者 | Barabas, O, Kovari, J, Pongracz, V, Wilmanns, M, Vertessy, B.G. | | 登録日 | 2004-04-01 | | 公開日 | 2004-09-07 | | 最終更新日 | 2023-10-25 | | 実験手法 | X-RAY DIFFRACTION (1.95 Å) | | 主引用文献 | Structural Insights into the Catalytic Mechanism of Phosphate Ester Hydrolysis by dUTPase
J.Biol.Chem., 279, 2004
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2HR6
 | | Crystal structure of dUTPase in complex with substrate analogue dUDP and manganese | | 分子名称: | 1,2-ETHANEDIOL, DEOXYURIDINE-5'-DIPHOSPHATE, Deoxyuridine 5'-triphosphate nucleotidohydrolase, ... | | 著者 | Barabas, O, Kovari, J, Tapai, R, Vertessy, B.G. | | 登録日 | 2006-07-19 | | 公開日 | 2007-07-31 | | 最終更新日 | 2023-08-30 | | 実験手法 | X-RAY DIFFRACTION (1.84 Å) | | 主引用文献 | Methylene substitution at the alpha-beta bridging position within the phosphate chain of dUDP profoundly perturbs ligand accommodation into the dUTPase active site.
Proteins, 71, 2008
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2HRM
 | | Crystal structure of dUTPase complexed with substrate analogue methylene-dUTP | | 分子名称: | 1,2-ETHANEDIOL, 2'-DEOXY-5'-O-[(S)-HYDROXY(PHOSPHONOMETHYL)PHOSPHORYL]URIDINE, Deoxyuridine 5'-triphosphate nucleotidohydrolase | | 著者 | Barabas, O, Kovari, J, Tapai, R, Vertessy, B.G. | | 登録日 | 2006-07-20 | | 公開日 | 2007-07-31 | | 最終更新日 | 2023-08-30 | | 実験手法 | X-RAY DIFFRACTION (1.7 Å) | | 主引用文献 | Methylene substitution at the alpha-beta bridging position within the phosphate chain of dUDP profoundly perturbs ligand accommodation into the dUTPase active site.
Proteins, 71, 2008
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