Literature summary for 4.1.1.33 extracted from

Addo, J.; Skaff, D.; Miziorko, H.
Active site binding modes of inhibitors of Staphylococcus aureus mevalonate diphosphate decarboxylase from docking and molecular dynamics simulations (2016), J. Mol. Model., 22, 1-18 .

No PubMed abstract available

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Crystallization (Commentary)

Crystallization (Comment)	Organism
molecular docking of inhibitors 6-fluoromevalonate diphosphate and diphosphoglycolylproline	Staphylococcus aureus

Inhibitors

Inhibitors	Comment	Organism	Structure
6-fluoromevalonate diphosphate	forms stable hydrogen bonds with residues Arg144, Arg193, Lys21, Ser107, and Tyr18, as well as stable hydrophobic interactions with Tyr18, Trp19, and Met196	Staphylococcus aureus
diphosphoglycolylproline	-	Staphylococcus aureus

Organism

Organism	UniProt	Comment	Textmining
Staphylococcus aureus	-	-	-

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.00023	-	6-fluoromevalonate diphosphate	pH 7.0, 30°C	Staphylococcus aureus
0.034	-	diphosphoglycolylproline	pH 7.0, 30°C	Staphylococcus aureus

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Release 2023.1 (January 2023)