Literature summary for 3.4.16.4 extracted from

Hargis, J.C.; Vankayala, S.L.; White, J.K.; Woodcock, H.L.
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)

Crystallization (Comment)	Organism
molecular dynamics simulations of noncovalent interactions in binding and specificity of benzylpenicillin and beta-lactam peptidomimetic perfect penicillin. Benzylpenicillin's phenyl group forms an extended pi-pi network with Phe120 and Trp233 that contributes significantly to its efficacy in DD-peptidase. 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, particularly the water-mediated salt bridge between Asp217 and the N4H3+	Streptomyces sp. R61

Crystallization (Comment)

Organism

molecular dynamics simulations of noncovalent interactions in binding and specificity of benzylpenicillin and beta-lactam peptidomimetic perfect penicillin. Benzylpenicillin's phenyl group forms an extended pi-pi network with Phe120 and Trp233 that contributes significantly to its efficacy in DD-peptidase. 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, particularly the water-mediated salt bridge between Asp217 and the N4H3+

Streptomyces sp. R61

Organism

Organism	UniProt	Comment	Textmining
Streptomyces sp. R61	P15555	-	-

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Release 2023.1 (January 2023)