DHPS: Dihydropteroate Synthase (DHPS) is an essential enzyme for the synthesis of Dihydropteroate in bacteria, and DHPS is absent in the humans. The folp1 gene (ML0224) encodes DHPS in Mycobacterium leprae and mutations within folp1 gene are associated with resistance to dapsone, a bacteriostatic drug in the multi-drug therapy for leprosy. The mutations that are included in the HARP database are only the missense mutations represented by amino acid substitutions at each residue position in the DHPS structure. Structural impacts of all the 19 possible substitutions at each residue position are computed using various predictive algorithms. Please see the HELP page for more information. Submit either single mutations or just the residue positions in the fields below. Additionally, user can upload Ab1 chromatogram files and view results of the BlastX search.
Query Mutations:
Note: Query mutations and residue positions here. Please see the help page for more information.
Single Mutation:
Note: Submit single amino acid substitutions identified by translating the sequencing reads.
Systematic Mutations:
Note: Submit residue positions from the modelled region. Click help button for more information.
Upload AB1 File:
Note: Upload AB1 files from DNA sequencing.
3D Visualization of the Dapsone Binding Site in DHPS & Chemical structure of Dapsone
Note: Hold left mouse button and hover over the viewers to visualize the structures in 3D. Scroll to zoom.
Interactive 3D Viewer: Interactomic Interactions of dapsone with the surrounding residue environment in chain 'A' of wildtype DHPS. Hydrogen bonds (blue), weak hydrogen bond (light blue) and metal interactions (purple) can be noted.
Dapsone - 3D View
Note: Hold the left mouse click and move to see the structure of Dapsone in 3D. Scroll to Zoom
Click here to predict Pharmacokinetic Properties of Dapsone.
