12UX
WT Human Aconitate Decarboxylase 1, apo
Summary for 12UX
| Entry DOI | 10.2210/pdb12ux/pdb |
| Descriptor | Cis-aconitate decarboxylase, SODIUM ION, TRIETHYLENE GLYCOL, ... (6 entities in total) |
| Functional Keywords | immune regulatory gene 1, oncoprotein, metabolism, immune system |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 101637.00 |
| Authors | Runge, B.,Monteiro, D.C.F. (deposition date: 2026-04-20, release date: 2026-08-19, Last modification date: 2026-09-02) |
| Primary citation | Runge, B.,Oktay, H.,Fucci, I.J.,Merten, E.M.,Tarasov, S.G.,Fan, L.,Monteiro, D.C.F. Robust structural, kinetic and biophysical characterization of wild-type human ACOD1, selected mutants and their interaction with citraconate. J Struct Biol X, 14:100157-100157, 2026 Cited by PubMed Abstract: Aconitate decarboxylase 1, an enzyme member of the MmgE-PrpD family of proteins, has gained significant attention in the last decade as a therapeutic target for cancer and inflammatory diseases. Its product, itaconate, is a multifunctional metabolite shown to drive several disease states. Though extensively studied and , this protein is biochemically and mechanistically under characterized and although a family of inhibitors has been described, no ligand-bound structures have yet been determined. In this work we present a thorough structural investigation that yielded the first ligand-bound structure of this protein family, which required the generation of artifact-free apo crystals. We also developed a novel, low-consumption, robust kinetic assay and investigated active site and allosteric mutants to further elucidate structural and dynamic activity relationships of this protein. PubMed: 42631184DOI: 10.1016/j.yjsbx.2026.100157 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.32 Å) |
Structure validation
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