Crystallization (Comment) | Organism |
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characterization of the noncovalent interactions based on cocrystallized structures of benzylpenicillin and perfect penicillin covalently bound to DD-peptidase by computational methods. Benzylpenicillins phenyl group forms an extended pi?pi network with Phe120 and Trp233 that contributes significantly to its efficacy in DD-peptidase. This aromatic stabilization is conserved in beta-lactamases. Interactions between the protein and the peptidomimetic tail region, particularly carboxylate 2 and the terminal N4H3+ unit, form unique hydrogen bonding and strong electrostatic interactions. Between Asp217 and the N4H3+ there is a water mediated salt bridge | Streptomyces sp. |
Organism | UniProt | Comment | Textmining |
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Streptomyces sp. | P15555 | - |
- |