Literature summary extracted from

Dudev, T.; Lim, C.
Oxyanion selectivity in sulfate and molybdate transport proteins: An ab initio/CDM study (2004), J. Am. Chem. Soc., 126, 10296-10305.

Application

EC Number	Application	Comment	Organism
7.3.2.5	additional information	specifically binds MoO42-/WO42- but not SO42-, mainly because the desolvation penalty of MoO42-/WO42- is significantly less than that of SO42- and, to a lesser extent, because the large and rigid cavity in these proteins attenuates ligand interactions with SO42-, as compared to MoO42-, exclusion of positively charged Lys/Arg side chains in the anion-binding sites of ModA, because Lys/Arg do not contribute to the selectivity of the binding pocket and substantially stabilize the complex between the oxyanion and protein ligands, which in turn would prohibit the rapid release of the bound oxyanion at a certain stage during the transport process	Azotobacter vinelandii

Organism

EC Number	Organism	UniProt	Comment	Textmining
7.3.2.5	Azotobacter vinelandii	-	-	-

Synonyms

EC Number	Synonyms	Comment	Organism
7.3.2.5	ModA	-	Azotobacter vinelandii

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Release 2023.1 (January 2023)