5INH
Crystal structure of Autotaxin/ENPP2 with a covalent fragment
Summary for 5INH
| Entry DOI | 10.2210/pdb5inh/pdb |
| Descriptor | Ectonucleotide pyrophosphatase/phosphodiesterase family member 2, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total) |
| Functional Keywords | inhibitor, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Mus musculus (Mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 102907.16 |
| Authors | Klein, M.G.,Tjhen, R. (deposition date: 2016-03-07, release date: 2017-03-15, Last modification date: 2024-11-06) |
| Primary citation | Lanier, M.,Cole, D.C.,Istratiy, Y.,Klein, M.G.,Schwartz, P.A.,Tjhen, R.,Jennings, A.,Hixon, M.S. Repurposing Suzuki Coupling Reagents as a Directed Fragment Library Targeting Serine Hydrolases and Related Enzymes. J. Med. Chem., 60:5209-5215, 2017 Cited by PubMed Abstract: Serine hydrolases are susceptible to potent reversible inhibition by boronic acids. Large collections of chemically diverse boronic acid fragments are commercially available because of their utility in coupling chemistry. We repurposed the approximately 650 boronic acid reagents in our collection as a directed fragment library targeting serine hydrolases and related enzymes. Highly efficient hits (LE > 0.6) often result. The utility of the approach is illustrated with the results against autotaxin, a phospholipase implicated in cardiovascular disease. PubMed: 28564542DOI: 10.1021/acs.jmedchem.6b01224 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.84 Å) |
Structure validation
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