1KVM
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![BU of 1kvm by Molmil](/molmil-images/mine/1kvm) | X-ray Crystal Structure of AmpC WT beta-Lactamase in Complex with Covalently Bound Cephalothin | 分子名称: | 5-METHYLENE-2-[2-OXO-1-(2-THIOPHEN-2-YL-ACETYLAMINO)-ETHYL]-5,6-DIHYDRO-2H-[1,3]THIAZINE-4-CARBOXYLIC ACID, PHOSPHATE ION, beta-lactamase | 著者 | Beadle, B.M, Trehan, I, Focia, P.J, Shoichet, B.K. | 登録日 | 2002-01-27 | 公開日 | 2002-03-13 | 最終更新日 | 2023-08-16 | 実験手法 | X-RAY DIFFRACTION (2.06 Å) | 主引用文献 | Structural milestones in the reaction pathway of an amide hydrolase: substrate, acyl, and product complexes of cephalothin with AmpC beta-lactamase. Structure, 10, 2002
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1L0D
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1L0G
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1LL5
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1L0F
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![BU of 1l0f by Molmil](/molmil-images/mine/1l0f) | |
1L0E
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![BU of 1l0e by Molmil](/molmil-images/mine/1l0e) | |
1KVL
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![BU of 1kvl by Molmil](/molmil-images/mine/1kvl) | X-ray Crystal Structure of AmpC S64G Mutant beta-Lactamase in Complex with Substrate and Product Forms of Cephalothin | 分子名称: | 2-[CARBOXY-(2-THIOPHEN-2-YL-ACETYLAMINO)-METHYL]-5-METHYL-3,6-DIHYDRO-2H-[1,3]THIAZINE-4-CARBOXYLIC ACID, 2-[CARBOXY-(2-THIOPHEN-2-YL-ACETYLAMINO)-METHYL]-5-METHYLENE-5,6-DIHYDRO-2H-[1,3]THIAZINE-4-CARBOXYLIC ACID, Beta-lactamase, ... | 著者 | Beadle, B.M, Trehan, I, Focia, P.J, Shoichet, B.K. | 登録日 | 2002-01-27 | 公開日 | 2002-03-13 | 最終更新日 | 2023-08-16 | 実験手法 | X-RAY DIFFRACTION (1.53 Å) | 主引用文献 | Structural milestones in the reaction pathway of an amide hydrolase: substrate, acyl, and product complexes of cephalothin with AmpC beta-lactamase. Structure, 10, 2002
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1I5Q
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![BU of 1i5q by Molmil](/molmil-images/mine/1i5q) | CRYSTAL STRUCTURE OF THE E. COLI AMPC BETA-LACTAMASE MUTANT N152A COVALENTLY ACYLATED WITH THE INHIBITORY BETA-LACTAM, MOXALACTAM | 分子名称: | (2R)-2-[(1R)-1-{[(2S)-2-carboxy-2-(4-hydroxyphenyl)acetyl]amino}-1-methoxy-2-oxoethyl]-5-methylidene-5,6-dihydro-2H-1,3-oxazine-4-carboxylic acid, BETA-LACTAMASE | 著者 | Trehan, I, Beadle, B.M, Shoichet, B.K. | 登録日 | 2001-02-28 | 公開日 | 2001-06-20 | 最終更新日 | 2023-08-09 | 実験手法 | X-RAY DIFFRACTION (1.83 Å) | 主引用文献 | Inhibition of AmpC beta-lactamase through a destabilizing interaction in the active site. Biochemistry, 40, 2001
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