| Description | This entry represents a domain located in the middle of human Molybdenum cofactor sulfurase (MOCOS) and it homologues from all cellular organisms. MOCOS sulfurates the molybdenum cofactor [ ]. Mutations in this protein lead to a disorder characterised by excretion of very large amounts of xanthine in the urine and a tendency to form xanthine stones [].It is also found at the N-terminal end of Mitochondrial amidoxime-reducing component 1 (mARC1), which catalyses the reduction of N-oxygenated molecules, acting as a counterpart of cytochrome P450 and flavin-containing monooxygenases in metabolic cycles [ , ], This protein comprises two structural domains which consist of nonsuccessive secondary-structure element, with mainly β-strands forming three- and four-stranded antiparallel β-sheets and several α-helices of different lengths [].This domain, also known as the MOSC_N domain, is often found to the N terminus of MOSC domain ( ). | Name | Molybdenum cofactor sulfurase, middle domain |
| Short Name | MOCOS_middle | Type | Domain |
Powered by
Have you tried our InterMine mobile apps?
and interoperation is funded by 
