29TB
Crystal structure of carbonic anhydrase II with 3-(benzylthio)phenyl sulfamate
This is a non-PDB format compatible entry.
Summary for 29TB
| Entry DOI | 10.2210/pdb29tb/pdb |
| Descriptor | Carbonic anhydrase 2, ZINC ION, DIMETHYL SULFOXIDE, ... (7 entities in total) |
| Functional Keywords | drug design, carbonic anhydrase, sulfamate, lyase-inhibitor complex, lyase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 29992.28 |
| Authors | Paketuryte-Latve, V.,Smirnov, A.,Manakova, E.N.,Grazulis, S. (deposition date: 2026-04-07, release date: 2026-10-21, Last modification date: 2026-11-04) |
| Primary citation | Di Lorenzo, V.,Csorba, N.,Szabo, R.,Kollar, L.,Roske, Y.,Randelovic, I.,Balazs, K.,Szalai, T.V.,Efrem, N.L.,Mihalovits, L.,Imre, T.,Simon, J.,Tovari, J.,Nazare, M.,Daumke, O.,Abranyi-Balogh, P.,Keseru, G.M. Fragment-Based Covalent Targeting of Lysines at the Allosteric Latch Site of SHP2. J.Med.Chem., 69:21955-21971, 2026 Cited by PubMed Abstract: Covalent mechanism of action is a powerful way to modulate challenging drug targets. Here, we present a streamlined workflow that combines covalent fragment screening (electrophile first approach) and ligand-first strategy to identify covalent inhibitors targeting lysine residues in the allosteric latch site of SHP2 phosphatase. Supported by complementary computational and experimental analyses, this strategy enabled us to identify the first potent cell active allosteric covalent inhibitors acting at this site. Demonstrating the covalent tractability of the latch site opens further avenues for future optimization and therapeutic exploration of high-value allosteric SHP2 inhibitors. PubMed: 42917893DOI: 10.1021/acs.jmedchem.6c01030 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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