Literature summary for 2.3.2.B14 extracted from

Ntombela, T.; Fakhar, Z.; Ibeji, C.U.; Govender, T.; Maguire, G.E.M.; Lamichhane, G.; Kruger, H.G.; Honarparvar, B.
Molecular insight on the non-covalent interactions between carbapenems and L,D-transpeptidase 2 from Mycobacterium tuberculosis ONIOM study (2018), J. Comput. Aided Mol. Des., 32, 687-701 .

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Inhibitors

Inhibitors	Comment	Organism	Structure
biapenem	investigation of the binding interactions using a two-layered ONIOM model	Mycobacterium tuberculosis
Imipenem	investigation of the binding interactions using a two-layered ONIOM model	Mycobacterium tuberculosis
meropenem	investigation of the binding interactions using a two-layered ONIOM model	Mycobacterium tuberculosis
additional information	investigation of the binding interactions carbapenems (biapenem, imipenem, meropenem, and tebipenem) using a two-layered ONIOM model. The carbapenems exhibit reasonable binding interactions towards LdtB. Increasing the number of amino acid residues that form hydrogen bond interactions in the QM layer shows significant impact in binding interaction energy differences and the stabilities of the carbapenems inside the active pocket. The hydrogen bond interactions and charge transfer from the bonding to anti-bonding orbitals between catalytic residues of the enzyme and selected ligands enhances the binding and stability of carbapenem-LdtB complexes	Mycobacterium tuberculosis
tebipenem	investigation of the binding interactions using a two-layered ONIOM model	Mycobacterium tuberculosis

Organism

Organism	UniProt	Comment	Textmining
Mycobacterium tuberculosis	O53223	-	-
Mycobacterium tuberculosis CDC 1551	O53223	-	-

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Release 2023.1 (January 2023)