1ZI9
 
 | | Crystal Structure Analysis of the dienelactone hydrolase (E36D, C123S) mutant- 1.5 A | | 分子名称: | Carboxymethylenebutenolidase, GLYCEROL, SULFATE ION | | 著者 | Kim, H.-K, Liu, J.-W, Carr, P.D, Ollis, D.L. | | 登録日 | 2005-04-27 | | 公開日 | 2005-07-05 | | 最終更新日 | 2023-10-25 | | 実験手法 | X-RAY DIFFRACTION (1.5 Å) | | 主引用文献 | Following directed evolution with crystallography: structural changes observed in changing the substrate specificity of dienelactone hydrolase.
Acta Crystallogr.,Sect.D, 61, 2005
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1ZJ4
 | | Crystal Structure Analysis of the dienelactone hydrolase mutant (E36D, C123S) bound with the PMS moiety of the protease inhibitor, Phenylmethylsulfonyl fluoride (PMSF)- 1.7 A | | 分子名称: | Carboxymethylenebutenolidase, GLYCEROL, SULFATE ION | | 著者 | Kim, H.-K, Liu, J.-W, Carr, P.D, Ollis, D.L. | | 登録日 | 2005-04-28 | | 公開日 | 2005-07-05 | | 最終更新日 | 2023-10-25 | | 実験手法 | X-RAY DIFFRACTION (1.7 Å) | | 主引用文献 | Following directed evolution with crystallography: structural changes observed in changing the substrate specificity of dienelactone hydrolase.
Acta Crystallogr.,Sect.D, 61, 2005
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1ZIY
 | | Crystal Structure Analysis of the dienelactone hydrolase mutant (C123S) bound with the PMS moiety of the protease inhibitor, Phenylmethylsulfonyl fluoride (PMSF)- 1.9 A | | 分子名称: | Carboxymethylenebutenolidase, GLYCEROL, SULFATE ION | | 著者 | Kim, H.-K, Liu, J.-W, Carr, P.D, Ollis, D.L. | | 登録日 | 2005-04-27 | | 公開日 | 2005-07-05 | | 最終更新日 | 2023-10-25 | | 実験手法 | X-RAY DIFFRACTION (1.9 Å) | | 主引用文献 | Following directed evolution with crystallography: structural changes observed in changing the substrate specificity of dienelactone hydrolase.
Acta Crystallogr.,Sect.D, 61, 2005
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1ZIX
 | | Crystal Structure Analysis of the dienelactone hydrolase mutant (E36D, R105H, C123S, G211D, K234N)- 1.8 A | | 分子名称: | Carboxymethylenebutenolidase, GLYCEROL | | 著者 | Kim, H.-K, Liu, J.-W, Carr, P.D, Ollis, D.L. | | 登録日 | 2005-04-27 | | 公開日 | 2005-07-05 | | 最終更新日 | 2023-10-25 | | 実験手法 | X-RAY DIFFRACTION (1.8 Å) | | 主引用文献 | Following directed evolution with crystallography: structural changes observed in changing the substrate specificity of dienelactone hydrolase.
Acta Crystallogr.,Sect.D, 61, 2005
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1ZJ5
 | | Crystal Structure Analysis of the dienelactone hydrolase mutant (E36D, C123S, A134S, S208G, A229V, K234R) bound with the PMS moiety of the protease inhibitor, Phenylmethylsulfonyl fluoride (PMSF)- 1.7 A | | 分子名称: | Carboxymethylenebutenolidase, GLYCEROL, SULFATE ION | | 著者 | Kim, H.-K, Liu, J.-W, Carr, P.D, Ollis, D.L. | | 登録日 | 2005-04-28 | | 公開日 | 2005-07-05 | | 最終更新日 | 2023-10-25 | | 実験手法 | X-RAY DIFFRACTION (1.7 Å) | | 主引用文献 | Following directed evolution with crystallography: structural changes observed in changing the substrate specificity of dienelactone hydrolase.
Acta Crystallogr.,Sect.D, 61, 2005
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1ZIC
 | | Crystal Structure Analysis of the dienelactone hydrolase (C123S, R206A) mutant- 1.7 A | | 分子名称: | Carboxymethylenebutenolidase, GLYCEROL, SULFATE ION | | 著者 | Kim, H.-K, Liu, J.-W, Carr, P.D, Ollis, D.L. | | 登録日 | 2005-04-27 | | 公開日 | 2005-07-05 | | 最終更新日 | 2023-10-25 | | 実験手法 | X-RAY DIFFRACTION (1.7 Å) | | 主引用文献 | Following directed evolution with crystallography: structural changes observed in changing the substrate specificity of dienelactone hydrolase.
Acta Crystallogr.,Sect.D, 61, 2005
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1ZI8
 | | Crystal Structure Analysis of the dienelactone hydrolase mutant(E36D, C123S, A134S, S208G, A229V, K234R)- 1.4 A | | 分子名称: | Carboxymethylenebutenolidase, GLYCEROL, SULFATE ION | | 著者 | Kim, H.-K, Liu, J.-W, Carr, P.D, Ollis, D.L. | | 登録日 | 2005-04-27 | | 公開日 | 2005-07-05 | | 最終更新日 | 2023-10-25 | | 実験手法 | X-RAY DIFFRACTION (1.4 Å) | | 主引用文献 | Following directed evolution with crystallography: structural changes observed in changing the substrate specificity of dienelactone hydrolase.
Acta Crystallogr.,Sect.D, 61, 2005
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1ZI6
 | | Crystal Structure Analysis of the dienelactone hydrolase (C123S) mutant- 1.7 A | | 分子名称: | Carboxymethylenebutenolidase, GLYCEROL, SULFATE ION | | 著者 | Kim, H.-K, Liu, J.-W, Carr, P.D, Ollis, D.L. | | 登録日 | 2005-04-27 | | 公開日 | 2005-07-05 | | 最終更新日 | 2023-10-25 | | 実験手法 | X-RAY DIFFRACTION (1.7 Å) | | 主引用文献 | Following directed evolution with crystallography: structural changes observed in changing the substrate specificity of dienelactone hydrolase.
Acta Crystallogr.,Sect.D, 61, 2005
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3A3W
 | | Structure of OpdA mutant (G60A/A80V/S92A/R118Q/K185R/Q206P/D208G/I260T/G273S) with diethyl 4-methoxyphenyl phosphate bound in the active site | | 分子名称: | COBALT (II) ION, DIETHYL 4-METHOXYPHENYL PHOSPHATE, Phosphotriesterase | | 著者 | Ollis, D.L, Tawfik, D.S, Schenk, G, Jackson, C.J, Foo, J.L, Tokuriki, N, Afriat, L, Carr, P.D, Kim, H.K. | | 登録日 | 2009-06-23 | | 公開日 | 2010-01-12 | | 最終更新日 | 2023-11-15 | | 実験手法 | X-RAY DIFFRACTION (1.85 Å) | | 主引用文献 | Conformational sampling, catalysis, and evolution of the bacterial phosphotriesterase
Proc.Natl.Acad.Sci.USA, 2009
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3A3X
 | | Structure of OpdA mutant (G60A/A80V/R118Q/K185R/Q206P/D208G/I260T/G273S) | | 分子名称: | COBALT (II) ION, Phosphotriesterase | | 著者 | Ollis, D.L, Tawfik, D.S, Schenk, G, Jackson, C.J, Foo, J.L, Tokuriki, N, Afriat, L, Carr, P.D, Kim, H.K. | | 登録日 | 2009-06-23 | | 公開日 | 2010-01-12 | | 最終更新日 | 2023-11-15 | | 実験手法 | X-RAY DIFFRACTION (1.7 Å) | | 主引用文献 | Conformational sampling, catalysis, and evolution of the bacterial phosphotriesterase
Proc.Natl.Acad.Sci.USA, 2009
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3A4J
 | | arPTE (K185R/D208G/N265D/T274N) | | 分子名称: | 1,2-ETHANEDIOL, COBALT (II) ION, Phosphotriesterase | | 著者 | Foo, J.L, Jackson, C.J, Carr, P.D, Ollis, D.L. | | 登録日 | 2009-07-07 | | 公開日 | 2010-01-12 | | 最終更新日 | 2023-11-15 | | 実験手法 | X-RAY DIFFRACTION (1.25 Å) | | 主引用文献 | Conformational sampling, catalysis, and evolution of the bacterial phosphotriesterase
Proc.Natl.Acad.Sci.USA, 2009
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1KU0
 | | Structure of the Bacillus stearothermophilus L1 lipase | | 分子名称: | CALCIUM ION, L1 lipase, ZINC ION | | 著者 | Jeong, S.-T, Kim, H.-K, Kim, S.-J, Chi, S.-W, Pan, J.-G, Oh, T.-K, Ryu, S.-E. | | 登録日 | 2002-01-18 | | 公開日 | 2002-08-21 | | 最終更新日 | 2024-03-13 | | 実験手法 | X-RAY DIFFRACTION (2 Å) | | 主引用文献 | Novel zinc-binding center and a temperature switch in the Bacillus stearothermophilus L1 lipase.
J.Biol.Chem., 277, 2002
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