3TSG
 
 | | Crystal structure of GES-14 | | 分子名称: | Extended-spectrum beta-lactamase GES-14, GLYCEROL, IODIDE ION | | 著者 | Delbruck, H, Hoffmann, K.M.V, Bebrone, C. | | 登録日 | 2011-09-13 | | 公開日 | 2012-09-26 | | 最終更新日 | 2023-09-13 | | 実験手法 | X-RAY DIFFRACTION (1.9 Å) | | 主引用文献 | Kinetic and crystallographic studies of extended-spectrum GES-11, GES-12, and GES-14 beta-lactamases.
Antimicrob.Agents Chemother., 56, 2012
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3SW3
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3FAI
 | | The Di Zinc Carbapenemase CphA N220G mutant | | 分子名称: | Beta-lactamase, CHLORIDE ION, GLYCEROL, ... | | 著者 | Delbruck, H, Hoffmann, K.M.V. | | 登録日 | 2008-11-17 | | 公開日 | 2009-09-01 | | 最終更新日 | 2023-11-01 | | 実験手法 | X-RAY DIFFRACTION (1.7 Å) | | 主引用文献 | The structure of the dizinc subclass B2 metallo-beta-lactamase CphA reveals that the second inhibitory zinc ion binds in the histidine site
Antimicrob.Agents Chemother., 53, 2009
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2HPB
 | | Crystal structure of the OXA-10 W154A mutant at pH 9.0 | | 分子名称: | Beta-lactamase PSE-2, SULFATE ION | | 著者 | Kerff, F, Falzone, C, Herman, R, Sauvage, E, Charlier, P. | | 登録日 | 2006-07-17 | | 公開日 | 2007-07-03 | | 最終更新日 | 2023-08-30 | | 実験手法 | X-RAY DIFFRACTION (2.05 Å) | | 主引用文献 | Critical role of tryptophan 154 for the activity and stability of class D beta-lactamases.
Biochemistry, 48, 2009
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2HP5
 | | Crystal Structure of the OXA-10 W154G mutant at pH 7.0 | | 分子名称: | Beta-lactamase PSE-2, COBALT (II) ION, SULFATE ION | | 著者 | Kerff, F, Falzone, C, Herman, R, Sauvage, E, Charlier, P. | | 登録日 | 2006-07-17 | | 公開日 | 2007-07-03 | | 最終更新日 | 2023-08-30 | | 実験手法 | X-RAY DIFFRACTION (2.7 Å) | | 主引用文献 | Critical role of tryptophan 154 for the activity and stability of class D beta-lactamases.
Biochemistry, 48, 2009
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2HP6
 | | Crystal structure of the OXA-10 W154A mutant at pH 7.5 | | 分子名称: | Beta-lactamase PSE-2, SULFATE ION | | 著者 | Kerff, F, Falzone, C, Herman, R, Sauvage, E, Charlier, P. | | 登録日 | 2006-07-17 | | 公開日 | 2007-07-03 | | 最終更新日 | 2023-08-30 | | 実験手法 | X-RAY DIFFRACTION (2.2 Å) | | 主引用文献 | Critical role of tryptophan 154 for the activity and stability of class D beta-lactamases.
Biochemistry, 48, 2009
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2HP9
 | | Crystal Structure of the OXA-10 W154A mutant at pH 6.0 | | 分子名称: | Beta-lactamase PSE-2, SULFATE ION | | 著者 | Kerff, F, Falzone, C, Herman, R, Sauvage, E, Charlier, P. | | 登録日 | 2006-07-17 | | 公開日 | 2007-07-03 | | 最終更新日 | 2023-08-30 | | 実験手法 | X-RAY DIFFRACTION (2.5 Å) | | 主引用文献 | Critical role of tryptophan 154 for the activity and stability of class D beta-lactamases.
Biochemistry, 48, 2009
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3ZNT
 | | Crystal structure of OXA-24 class D beta-lactamase with tazobactam | | 分子名称: | BETA-LACTAMASE, SULFATE ION, TAZOBACTAM INTERMEDIATE | | 著者 | Power, P, Sauvage, E, Herman, R, Kerff, F, Charlier, P. | | 登録日 | 2013-02-18 | | 公開日 | 2014-01-08 | | 最終更新日 | 2023-12-20 | | 実験手法 | X-RAY DIFFRACTION (1.95 Å) | | 主引用文献 | Crystal Structure of Oxa-24 Beta-Lactamase Inhibited by Tazobactam
To be Published
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3V3R
 | | Crystal Structure of GES-11 | | 分子名称: | Extended spectrum class A beta-lactamase GES-11, IODIDE ION, SODIUM ION | | 著者 | Delbruck, H, Hoffmann, K.M.V, Bebrone, C. | | 登録日 | 2011-12-14 | | 公開日 | 2012-09-26 | | 最終更新日 | 2023-09-13 | | 実験手法 | X-RAY DIFFRACTION (1.898 Å) | | 主引用文献 | Kinetic and crystallographic studies of extended-spectrum GES-11, GES-12, and GES-14 beta-lactamases.
Antimicrob.Agents Chemother., 56, 2012
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4A5R
 | | Crystal structure of class A beta-lactamase from Bacillus licheniformis BS3 with tazobactam | | 分子名称: | BETA-LACTAMASE, CARBON DIOXIDE, CITRIC ACID, ... | | 著者 | Power, P, Sauvage, E, Herman, R, Kerff, F, Charlier, P. | | 登録日 | 2011-10-28 | | 公開日 | 2012-10-10 | | 最終更新日 | 2023-12-20 | | 実験手法 | X-RAY DIFFRACTION (2.1 Å) | | 主引用文献 | Crystal Structure of Class a Beta-Lactamase from Bacillus Licheniformis Inhibited by Tazobactam
To be Published
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1AMK
 | | LEISHMANIA MEXICANA TRIOSE PHOSPHATE ISOMERASE | | 分子名称: | 2-PHOSPHOGLYCOLIC ACID, TRIOSE PHOSPHATE ISOMERASE | | 著者 | Williams, J.C, Wierenga, R. | | 登録日 | 1997-06-17 | | 公開日 | 1997-12-17 | | 最終更新日 | 2024-05-22 | | 実験手法 | X-RAY DIFFRACTION (1.83 Å) | | 主引用文献 | Structural and mutagenesis studies of leishmania triosephosphate isomerase: a point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power.
Protein Eng., 12, 1999
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1M2X
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