GYR: DNA Gyrase (GYR) is an essential enzyme in mycobacteria that catalyses ATP-dependent transient cleavage and negative supercoiling of closed circular DNA. The heterotetrameric protein (GyrA2, GyrB2) is comprised of four chains (A, B, C, D)
which are encoded by gyrA (ML0006) and gyrB (ML0005) in Mycobacterium leprae. Mutations within the GyrA subunit are associated with resistance to ofloxacin, a second-line bactericidal drug in the treatment of leprosy. The mutations that are included in the HARP database are only missense mutations
represented by amino acid substitutions at each residue position in all the chains of the GYR structure. All the 19 possible substitutions at each residue position are analysed using various computational tools. Submit either single mutations or just the residue positions in the fields below. Additionally, user can upload Ab1 chromatogram files and view the Blastx results.
Note: The GYR model of Mycobacterium leprae is built using PDB ID:5BS8. Chain A has an intein region from residue positions 131-550 which was removed during modelling. The residue numbering is consistent with the template alignment.
Note: Query mutations and residue positions here. Please see the help page for more information.
3D Visualization of the Ofloxacin Binding Site in GYR & Chemical structure of Ofloxacin
Note: Hold left mouse button and hover over the viewers to visualize the structures in 3D. Scroll to zoom.