Literature summary for 2.7.8.13 extracted from

Malek Zadeh, S.; Astani, E.K.; Wang, Z.C.; Adhikari, K.; Rattinam, R.; Li, T.L.
Theoretical study of intermolecular interactions between critical residues of membrane protein MraYAA and promising antibiotic muraymycin D2 (2020), ACS Omega, 5, 22739-22749 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
in the complex with inhibitor muraymycin D2, multiple hydrogen bonds are present in the active site with strength ranging from van der Waals to covalent limits. Lys70, Asp193, Gly194, Asp196, Gly264, Ala321, Gln305, and His325 are key active-site residues interacting with muraymycin D2. Conventional and unconventional hydrogen bonds in addition with charge-dipole and dipole-dipole interactions contribute significantly to stabilize the muraymycin D2 binding	Aquifex aeolicus

Crystallization (Comment)

Organism

in the complex with inhibitor muraymycin D2, multiple hydrogen bonds are present in the active site with strength ranging from van der Waals to covalent limits. Lys70, Asp193, Gly194, Asp196, Gly264, Ala321, Gln305, and His325 are key active-site residues interacting with muraymycin D2. Conventional and unconventional hydrogen bonds in addition with charge-dipole and dipole-dipole interactions contribute significantly to stabilize the muraymycin D2 binding

Aquifex aeolicus

Inhibitors

Inhibitors	Comment	Organism	Structure
muraymycin D2	-	Aquifex aeolicus

Organism

Organism	UniProt	Comment	Textmining
Aquifex aeolicus	O66465	-	-

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Release 2023.1 (January 2023)