EC Number   |
|---|
    1.5.1.3 | - |
| 1.5.1.3 | 2.1 A resolution neutron structure of a pseudo-Michaelis complex determined at acidic pH, direct observation of the catalytic proton and its parent solvent molecule |
| 1.5.1.3 | analysis of higher energy conformational substrates by NMR relaxation dispersion. The maximum hydride transfer and steady-state turnover rates are governed by the dynamics of transitions between ground and excited states of the intermediates. Model of conformational changes during the catalytic cycle |
| 1.5.1.3 | binding mode analysis and docking approaches of inhibitors, and comparison between human and Mycobacterium tuberculosis enzyme. Presence of empty spaces around the 2,4-diamonodeazapteridine and N10-phenyl rings of inhibitors in the Mycobacterium tuberculosis enzyme active site that are not found in the human structures |
| 1.5.1.3 | binding to trimethoprim, structure analysis |
| 1.5.1.3 | co-crystallization of the purified enzyme with inhibitor 2-amino-4-oxo-4,7-dihydro-pyrrolo[2,3-d]pyrimidine-methyl-phenyl-L-glutamic acid and FdUMP in the TS site and NADPH and methotrexate in the DHFR site, X-ray diffraction structure determination and analysis at 3.45 A resolution, PDB ID 4Q0D |
| 1.5.1.3 | CoMFA and quantum chemical calculations studies on pyrimethamine derivatives active against quadruple mutant N5I/C59R/S108N/I164L. Residue N108 is the cause of pyrimethamine resistance with the highest repulsive interaction energy |
| 1.5.1.3 | comparison of temperature dependence of dynamics between Geobacillus stearothermophilus and Escherichia coli enzymes using elastic coherent scattering. The Geobacillus' enzyme has a significantly broader distribution and slightly larger amplitudes of the atomic mean-square displacements extracted from the dynamic structure factor |
| 1.5.1.3 | comparison of the backbone conformation in crystal structures, detection of mutational insertions |
| 1.5.1.3 | crystal structure of complex with methotrexate |
