The ability of an enzyme to select and act upon a specific class of compounds with unerring precision and efficiency is an essential feature of life. Simultaneously, these enzymes often catalyze the reaction of a range of similar substrates of the same class, and also have promiscuous activities on unrelated substrates. Previously, we have established a methodology to quantify promiscuous activities in a wide range of proteins. In the current work, we quantitatively characterize the active site for the ability to catalyze distinct, yet related, substrates (BRASS). A protein with known structure and active site residues provides the framework for computing ‘duplicate’ residues, each of which results in slightly modified replicas of the active site scaffold. Such spatial congruence is supplemented by Finite difference Poisson Boltzmann analysis which filters out electrostatically unfavorable configurations. The congruent configurations are used to compute an index (BrassIndex), which reflects the broad substrate profile of the active site.  Citations are important for a journal to get impact factor. Impact factor is a measure reflecting the average number of citations to recent articles published in the journal. The impact of the journal is influenced by impact factor, the journals with high impact factor are considered more important than those with lower ones. To increase the visibility and ease of use of open access scientific and scholarly journals PrimeOA Publications top online publishing journals are indexed in different indexing and archiving services.