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EC Number	Crystallization (Commentary)
1.6.3.5	3D molecular models for mutants m5Ren1 and m6Ren1. Regions on the surface of the enzyme that are significantly changed include Q3R, C47R, R75S, S217D, and T329Q. Each of these mutations contributes to changes in polarity, charge, and hydrophilicity. Relative to wild-type, m6Ren1 exhibits a greater density of positively-charged residues around the active site
1.6.3.5	to 2.5 A resolution. Renalase adopts the p-hydroxybenzoate hydroxylase fold topology, comprising a Rossmann-fold-based flavin adenine dinucleotide-binding domain and a putative substrate-binding domain, the latter of which contains a five-stranded anti-parallel beta-sheet. A large cavity, facing the flavin ring, presumably represents the active site. The renalase active site is fully solvent exposed and lacks an aromatic cage for binding the substrate amino group

EC Number

Crystallization (Commentary)

1.6.3.5

3D molecular models for mutants m5Ren1 and m6Ren1. Regions on the surface of the enzyme that are significantly changed include Q3R, C47R, R75S, S217D, and T329Q. Each of these mutations contributes to changes in polarity, charge, and hydrophilicity. Relative to wild-type, m6Ren1 exhibits a greater density of positively-charged residues around the active site

1.6.3.5

to 2.5 A resolution. Renalase adopts the p-hydroxybenzoate hydroxylase fold topology, comprising a Rossmann-fold-based flavin adenine dinucleotide-binding domain and a putative substrate-binding domain, the latter of which contains a five-stranded anti-parallel beta-sheet. A large cavity, facing the flavin ring, presumably represents the active site. The renalase active site is fully solvent exposed and lacks an aromatic cage for binding the substrate amino group

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Release 2023.1 (January 2023)