3KOO
Crystal Structure of soluble epoxide Hydrolase
Summary for 3KOO
| Entry DOI | 10.2210/pdb3koo/pdb |
| Descriptor | Epoxide hydrolase 2, N-(2,4-dichlorobenzyl)-4-(pyrimidin-2-yloxy)piperidine-1-carboxamide (3 entities in total) |
| Functional Keywords | hydrolase |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: P34913 |
| Total number of polymer chains | 1 |
| Total formula weight | 63066.87 |
| Authors | Farrow, N.A. (deposition date: 2009-11-13, release date: 2010-04-28, Last modification date: 2024-02-21) |
| Primary citation | Eldrup, A.B.,Soleymanzadeh, F.,Farrow, N.A.,Kukulka, A.,De Lombaert, S. Optimization of piperidyl-ureas as inhibitors of soluble epoxide hydrolase. Bioorg.Med.Chem.Lett., 20:571-575, 2010 Cited by PubMed Abstract: Inhibition of sEH is hypothesized to lead to an increase in epoxyeicosatrienoic acids resulting in the potentiation of their anti-inflammatory and vasodilatory effects. In an effort to explore sEH inhibition as an avenue for the development of vasodilatory and cardio- or renal-protective agents, a lead identified through high-throughput screening was optimized, guided by the determination of a solid state co-structure with sEH. Replacement of potential toxicophores was followed by optimization of cell-based potency and ADME properties to provide a new class of functionally potent sEH inhibitors with attractive in vitro metabolic profiles and high and sustained plasma exposures after oral administration in the rat. PubMed: 19969453DOI: 10.1016/j.bmcl.2009.11.091 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.791 Å) |
Structure validation
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