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The main aim of current study was to perform  in silico  functional analysis of all reported RPIA mutations.  In silico  analysis was done using different tools i.e. trRosetta tool, Autodock Vina, PatchDock and iMODS. Among all the reported mutations, lowest percentage identity of 4.69% with wild-type protein was shown by splice site mutation, while highest percentage identity of 78.78%, was shown by p.Ser61Val mutation. In protein-substrate docking, wild-type protein was docking with substrate with 11 different bonds. However in case of mutant protein highest interaction with substrate molecule was shown by mutant p.Ile257Thr proteins via 13 different bonds, while lowest interaction was noted in mutant p.Asn255Ilefs17Term protein via 5 bonds. From the results, it was concluded that the binding of RPIA with ribose 5-phosphate is altered by the type of amino acid substitution, as well as the nature and number of bonds, which are capable to influence its biological activity.

Computational analyses of RPIA gene mutation causing Ribose-5-phosphate isomerase deficiency: a rarest known metabolic disorder in humans