Literature summary for 4.3.1.17 extracted from

Yan, Y.; Grant, G.A.; Gross, M.L.
Hydrogen-deuterium exchange mass spectrometry reveals unique conformational and chemical transformations occurring upon [4Fe-4S] cluster binding in the type 2 L-serine dehydratase from Legionella pneumophila (2015), Biochemistry, 54, 5322-5328 .

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
4Fe-4S-center	the enzyme contains a [4Fe-4S]2+ cluster that acts as a Lewis acid to extract the hydroxyl group of L-serine during the dehydration reaction. Fe-S cluster binding induces protein conformational changes in L-serine dehydratase. All four iron atoms of the [4Fe-4S] cluster are coordinated with protein cysteine residues (C396, C485, C343, C385). formation of disulfide bonds between C396 and C485 and possibly between C343 and C385	Legionella pneumophila

Organism

Organism	UniProt	Comment	Textmining
Legionella pneumophila	Q5ZXE1	-	-

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Release 2023.1 (January 2023)