3G3M
Crystal Structure of Human Orotidine 5'-monophosphate Decarboxylase Covalently Modified by 5-fluoro-6-iodo-UMP
Summary for 3G3M
Entry DOI | 10.2210/pdb3g3m/pdb |
Related | 3G3D |
Descriptor | Uridine 5'-monophosphate synthase, 5-FLUORO-URIDINE-5'-MONOPHOSPHATE (3 entities in total) |
Functional Keywords | human, orotidine 5'-monophosphate decarboxylase, c-terminal domain, 5-fluoro-6-iodo-ump, alternative splicing, decarboxylase, disease mutation, glycosyltransferase, lyase, multifunctional enzyme, phosphoprotein, polymorphism, pyrimidine biosynthesis, transferase |
Biological source | Homo sapiens (Human) |
Total number of polymer chains | 1 |
Total formula weight | 30830.33 |
Authors | Liu, Y.,Tang, H.L.,Bello, A.M.,Poduch, E.,Kotra, L.P.,Pai, E.F. (deposition date: 2009-02-02, release date: 2009-03-03, Last modification date: 2023-09-06) |
Primary citation | Bello, A.M.,Konforte, D.,Poduch, E.,Furlonger, C.,Wei, L.,Liu, Y.,Lewis, M.,Pai, E.F.,Paige, C.J.,Kotra, L.P. Structure-activity relationships of orotidine-5'-monophosphate decarboxylase inhibitors as anticancer agents. J.Med.Chem., 52:1648-1658, 2009 Cited by PubMed: 19260677DOI: 10.1021/jm801224t PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
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