Title : Structural and computational investigations of VIM-7: insights into the substrate specificity of vim metallo-β-lactamases.

Pub. Date : 2011 Aug 5

PMID : 21645522






3 Functional Relationships(s)
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1 Comparison with VIM-2 and VIM-4 structures suggests an explanation for the reduced catalytic efficiency of VIM-7 against cephalosporins with a positively charged cyclic substituent at the C3 position (e.g., ceftazidime). Ceftazidime vimentin Homo sapiens
2 Comparison with VIM-2 and VIM-4 structures suggests an explanation for the reduced catalytic efficiency of VIM-7 against cephalosporins with a positively charged cyclic substituent at the C3 position (e.g., ceftazidime). Ceftazidime vimentin Homo sapiens
3 Docking of the cephalosporins ceftazidime and cefotaxime into the VIM-2 and VIM-7 structures reveals that amino acid substitutions may cause the mode of substrate binding to differ between the two enzymes. Ceftazidime vimentin Homo sapiens