Literature summary extracted from

Hargis, J.; Vankayala, S.; White, J.; Woodcock, H.
Identification and characterization of noncovalent interactions that drive binding and specificity in DD-peptidases and beta-lactamases (2014), J. Chem. Theory Comput., 10, 855-864.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
3.4.16.4	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

EC Number	Organism	UniProt	Comment	Textmining
3.4.16.4	Streptomyces sp.	P15555	-	-

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Release 2023.1 (January 2023)