Till now, three different human coronaviruses (CoVs) have been identified [1–3]. Severe acute respiratory syndrome (SARS-CoV), Middle East respiratory syndrome coronavirus (MERS-CoV), first reported in 2002 and 2012, were the first members of this pathogenic coronavirus family [1, 4, 5]. These pathogenic coronavirus family members were responsible for the outbreak in 2003 and 2012, respectively [1, 5, 6]. In December 2019, a new member of this family was identified, later named SARS-CoV-2, and soon became a ghost virus associated with the global pandemic . Since the emergence of SARS-CoV-2, the most highly pathogenic coronavirus reported so far, its rapid spread all over the globe has posed a severe threat to public health. The pandemic caused by this new coronavirus has emerged as a significant threat and has severely affected almost a considerable world population as a whole. First time reported from the Wuhan city, China, in December 2019, SARS-CoV-2 has quickly spread worldwide. Among all outbreaks of the 21st century, the SARS-CoV-2 causing COVID-19 pandemic has the highest infection and death rate, 61 million infections, and over 1.4 million deaths on December 1, 2020.. The studies have found that the SARS-CoV-2 mediates its viral entry by binding to the human ACE2 receptor via its spike protein. The RBD region of spike protein is well reported to be involved in binding with the host ACE2. The overall binding mode of ACE2- SARS-CoV-2 RBD is almost similar to other counterpart, SARS-CoV, which also uses the similar viral entry mechanism [8–11]. All the RNA coronaviruses family members, SARS-CoV-2, CoV, and MERS, present an extensive rate of mutations [11–13]. These high mutation rates may be a factor accountable for these coronaviruses' zoonotic nature and maybe a critical point leading the future risk of other members of this viral family to switch to humans from their traditional hosts. These mutations may develop resistance towards the antiviral drugs as well. The structural investigations identified that most of the SARS-CoV-2 RBD residues essential for its binding to ACE2 are highly conserved with those in the SARS-CoV RBD [14, 15]. A novel SARS-CoV-2 virus variant, referred to as SARS-CoV-2 VUI 202012/01 (Variant Under Investigation, year 2020, month 12, variant 01), has been recognized via viral genomic sequencing in the United Kingdom (UK). It is classified by means of numerous spike protein (protein responsible for the anchoring of the virus to the host cell) mutations (deletion 69–70, deletion 144, N501Y, A570D, D614G, P681H, T716I, S982A, D1118H). The variant belongs to Nextstrain clade 20B , GISAID clade GR [3, 4], lineage B.1.1.7. Out of these mutations, the N501Y mutation modifies the spike's essential part, known as the ‘receptor-binding domain’. This is where the spike makes initial contact with the body’s cell surface. Least changes in the structure make it uncomplicated for the virus to get within. N501Y was first sequenced in April 2020 in a virus in Brazil and is presently linked with a SARS-CoV-2 variant - an independent lineage from B.1.1.7, with an intensifying recurrence rate in South Africa . Mutation N501Y is one of the six major contact residues present inside the receptor-binding domain (RBD) and has been acknowledged to increase the binding affinity to human cell-surface protein angiotensin converting enzyme 2 (ACE2) [18–20]. Changes in the receptor-binding region of the spike protein may ultimately lead to the change in the virus's ACE2 binding specificity and alter antigenicity, i.e., recognition by immune antibodies the SARS-COV-2 virus becoming more contagious and spreading more effortlessly amid people. Here in this study, we have used Molecular dynamics and other computational approaches to explore the impact of this important point mutation on SARS-COV-2 RBD towards its binding against the receptor.