3G3D

Crystal Structure of Human Orotidine 5'-monophosphate Decarboxylase Covalently Modified by 5-fluoro-6-azido-UMP

Summary for 3G3D

Entry DOI	10.2210/pdb3g3d/pdb
Related	3G3M
Descriptor	Uridine 5'-monophosphate synthase, 5-FLUORO-URIDINE-5'-MONOPHOSPHATE, GLYCEROL, ... (5 entities in total)
Functional Keywords	ump synthase, c-terminal domain, orotidine 5'-monophosphate decarboxylase, human, 5-fluoro-6-azido-ump, decarboxylase, disease mutation, glycosyltransferase, lyase, multifunctional enzyme, phosphoprotein, pyrimidine biosynthesis, transferase
Biological source	Homo sapiens (Human)
Total number of polymer chains	2
Total formula weight	69165.00
Authors	Liu, Y.,Tang, H.L.,Bello, A.,Poduch, E.,Kotra, L.,Pai, E. (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: 19260677 DOI: 10.1021/jm801224t PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.7 Å)

Structure validation