Rat dihydroorotate dehydrogenase (DHOD)in complex with atovaquone

Beta-Octylglucoside; octyl beta-D-glucoside; octyl D-glucoside; octyl glucoside

Inhibitor Binding in a Class 2 Dihydroorotate Dehydrogenase Causes Variations in the Membrane-Associated N-Terminal Domain

AFI A 400 HAS WRONG CHIRALITY AT ATOM C16

AFI B 400 HAS WRONG CHIRALITY AT ATOM C16

MITOCHONDRIAL PRECURSOR, DIHYDROOROTATE OXIDASE, DHODEHASE

HHHHHHATGDDHFYAEYLMPGLQRLLDPESAHRLAVRVTSLGLLPRATFQDSDMLEVKVLGHKFRNPVGIAAGFDKNGEA
VDGLYKLGFGFVEVGSVTPQPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSVVEHRLRARQQKQAQLTADGLPLGINLGK
NKTSEDAAADYAEGVRTLGPLADYLVVNVSSPNTAGLRSLQGKTELRHLLSKVLQERDALKGTRKPAVLVKIAPDLTAQD
KEDIASVARELGIDGLIVTNTTVSRPVGLQGALRSETGGLSGKPLRDLSTQTIREMYALTQGRIPIIGVGGVSSGQDALE
KIQAGASLVQLYTALIFLGPPVVVRVKRELEALLKERGFTTVTDAIGADHRR

VAPOUR DIFFUSION HANGING DROP WITH MOTHER LIQUOR, 5% PEG400, 1.9 M AMMONIUM SULPHATE, 0.1 M TRIS-HCL PH 8.6, PROTEIN SOLUTION: 15 MG/ML PROTEIN, 2 MM OROTATE, 0.1 % BETA-OCTYLGLUCOSIDE, 0.1 MM ATOVAQUONE

RAT DIHYDROOROTATE DEHYDROGENASE (DHOD)IN COMPLEX WITH BREQUINAR

SHEET
DETERMINATION METHOD: DSSP
THE SHEETS PRESENTED AS "AB" IN EACH CHAIN ON SHEET RECORDS
BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
ARE IDENTICAL.

THE SHEETS PRESENTED AS "BB" IN EACH CHAIN ON SHEET RECORDS
BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
ARE IDENTICAL.

CATALYTIC ACTIVITY: (S)-DIHYDROOROTATE + O2 = OROTATE + H2O2
29 FIRST RESIDUES IN N-TERMINAL DELETED AND HIS-TAQ ADDED

OXIDOREDUCTASE, DIHYDROOROTATE DEHYDROGENASE, BREQUINAR, ATOVAQUONE, NUCLEOTIDE METABOLISM, PYRIMIDINE BIOSYNTHESIS, FAD, FLAVOPROTEIN, TRANSIT PEPTIDE