8UK6
Candida albicans glutaminyl tRNA synthetase (GLN4) in complex with N-pyrimidinyl-beta-thiophenylacrylamide
Summary for 8UK6
Entry DOI | 10.2210/pdb8uk6/pdb |
Descriptor | glutamine--tRNA ligase, ZINC ION, (2E)-N-(pyrimidin-2-yl)-3-(thiophen-2-yl)prop-2-enamide, ... (4 entities in total) |
Functional Keywords | inhibitor, complex, allosteric, ligase, ligase-ligase inhibitor complex, ligase/ligase inhibitor |
Biological source | Candida albicans |
Total number of polymer chains | 1 |
Total formula weight | 93783.95 |
Authors | Sychantha, D.,Wright, G.D. (deposition date: 2023-10-12, release date: 2024-03-06, Last modification date: 2024-05-01) |
Primary citation | Puumala, E.,Sychantha, D.,Lach, E.,Reeves, S.,Nabeela, S.,Fogal, M.,Nigam, A.,Johnson, J.W.,Aspuru-Guzik, A.,Shapiro, R.S.,Uppuluri, P.,Kalyaanamoorthy, S.,Magolan, J.,Whitesell, L.,Robbins, N.,Wright, G.D.,Cowen, L.E. Allosteric inhibition of tRNA synthetase Gln4 by N-pyrimidinyl-beta-thiophenylacrylamides exerts highly selective antifungal activity. Cell Chem Biol, 31:760-, 2024 Cited by PubMed: 38402621DOI: 10.1016/j.chembiol.2024.01.010 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.73 Å) |
Structure validation
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