Literature summary for 6.3.4.14 extracted from

Brylinski, M.; Waldrop, G.L.
Computational redesign of bacterial biotin carboxylase inhibitors using structure-based virtual screening of combinatorial libraries (2014), Molecules, 19, 4021-4045 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
in-silico docking studies of amino-oxazole inhibitors	Staphylococcus aureus
in-silico docking studies of amino-oxazole inhibitors	Haemophilus influenzae
in-silico docking studies of amino-oxazole inhibitors	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	docking studies of amino-oxazole inhibitors to biotin carboxylase from Escherichia coli, Haemophilus influenzae, Pseudomonas aeruginosa, Enterococcus faecalis, Staphylococcus aureus and others. Binding of the amino-oxazole anchor is stabilized by a network of hydrogen bonds to residues 201, 202 and 204. Halogenated aromatic moieties attached to the amino-oxazole scaffold enhance interactions with a hydrophobic pocket formed by residues 157, 169, 171 and 203. Larger substituents reach deeper into the binding pocket to form additional hydrogen bonds with the side chains of residues 209 and 233	Escherichia coli
additional information	docking studies of amino-oxazole inhibitors to biotin carboxylase from Escherichia coli, Haemophilus influenzae, Pseudomonas aeruginosa, Enterococcus faecalis, Staphylococcus aureus and others. Binding of the amino-oxazole anchor is stabilized by a network of hydrogen bonds to residues 201, 202 and 204. Halogenated aromatic moieties attached to the amino-oxazole scaffold enhance interactions with a hydrophobic pocket formed by residues 157, 169, 171 and 203. Larger substituents reach deeper into the binding pocket to form additional hydrogen bonds with the side chains of residues 209 and 233	Haemophilus influenzae
additional information	docking studies of amino-oxazole inhibitors to biotin carboxylase from Escherichia coli, Haemophilus influenzae, Pseudomonas aeruginosa, Enterococcus faecalis, Staphylococcus aureus and others. Binding of the amino-oxazole anchor is stabilized by a network of hydrogen bonds to residues 201, 202 and 204. Halogenated aromatic moieties attached to the amino-oxazole scaffold enhance interactions with a hydrophobic pocket formed by residues 157, 169, 171 and 203. Larger substituents reach deeper into the binding pocket to form additional hydrogen bonds with the side chains of residues 209 and 233	Staphylococcus aureus

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-
Haemophilus influenzae	-	-	-
Staphylococcus aureus	-	-	-

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Release 2023.1 (January 2023)