1D3H

HUMAN DIHYDROOROTATE DEHYDROGENASE COMPLEXED WITH ANTIPROLIFERATIVE AGENT A771726

Summary for 1D3H

Entry DOI	10.2210/pdb1d3h/pdb
Related	1D3G
Descriptor	DIHYDROOROTATE DEHYDROGENASE, SULFATE ION, ACETATE ION, ... (7 entities in total)
Functional Keywords	alpha-beta barrel, membrane binding motif, oxidoreductase
Biological source	Homo sapiens (human)
Cellular location	Mitochondrion inner membrane; Single-pass membrane protein: Q02127
Total number of polymer chains	1
Total formula weight	40894.29
Authors	Liu, S.,Neidhardt, E.A.,Grossman, T.H.,Ocain, T.,Clardy, J. (deposition date: 1999-09-29, release date: 2000-08-13, Last modification date: 2024-02-07)
Primary citation	Liu, S.,Neidhardt, E.A.,Grossman, T.H.,Ocain, T.,Clardy, J. Structures of human dihydroorotate dehydrogenase in complex with antiproliferative agents. Structure Fold.Des., 8:25-33, 2000 Cited by PubMed Abstract: Dihydroorotate dehydrogenase (DHODH) catalyzes the fourth committed step in the de novo biosynthesis of pyrimidines. As rapidly proliferating human T cells have an exceptional requirement for de novo pyrimidine biosynthesis, small molecule DHODH inhibitors constitute an attractive therapeutic approach to autoimmune diseases, immunosuppression, and cancer. Neither the structure of human DHODH nor any member of its family was known. PubMed: 10673429 DOI: 10.1016/S0969-2126(00)00077-0 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.8 Å)

Structure validation