3kvk | pdb_00003kvk
From Proteopedia
Jump to navigationJump to search
Crystal structure of human dihydroorotate dehydrogenase (DHODH) with amino-benzoic acid inhibitor 641 at 2.05A resolution
| ||||||||||||
Structural highlights
DiseasePYRD_HUMAN Defects in DHODH are the cause of postaxial acrofacial dysostosis (POADS) [MIM:263750; also known as Miller syndrome. POADS is characterized by severe micrognathia, cleft lip and/or palate, hypoplasia or aplasia of the posterior elements of the limbs, coloboma of the eyelids and supernumerary nipples. POADS is a very rare disorder: only 2 multiplex families, each consisting of 2 affected siblings born to unaffected, nonconsanguineous parents, have been described among a total of around 30 reported cases.[1] FunctionPYRD_HUMAN Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAmino-benzoic acid derivatives 1-4 were found to be inhibitors for DHODH by virtual screening, biochemical, and X-ray crystallographic studies. X-ray structures showed that 1 and 2 bind to DHODH as predicted by virtual screening, but 3 and 4 were found to be structurally different from the corresponding compounds initially identified by virtual screening. Discovery of novel inhibitors for DHODH via virtual screening and X-ray crystallographic structures.,McLean LR, Zhang Y, Degnen W, Peppard J, Cabel D, Zou C, Tsay JT, Subramaniam A, Vaz RJ, Li Y Bioorg Med Chem Lett. 2010 Mar 15;20(6):1981-4. Epub 2010 Jan 25. PMID:20153645[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
| ||||||||||||||||||||
This page was last modified 08:25, 6 September 2023.