The crystal structure of CYP199A4 bound to 4-(furan-2-yl)benzoic acid

The Oxidation of Oxygen and Sulfur-Containing Heterocycles by Cytochrome P450 Enzymes.

Double-crystal Si(111) liquid nitrogen cooled (DC) or channel-cut Si(111) liquid nitrogen cooled (CC)

MISNSSAESISAPPNDSTIPHLAIDPFSLDFFDDPYPDQQTLRDAGPVVYLDKWNVYGVARYAEVHAVLNDPTTFCSSRG
VGLSDFKKEKPWRPPSLILEADPPAHTRPRAVLSKVLSPATMKTIRDGFAAAADAKVDELLQRGCIDAIADLAEAYPLSV
FPDAMGLKQEGREHLLPYAGLVFNAFGPPNELRQTAIERSAPHQAYVNEQCQRPNLAPGGFGACIHAFTDTGEITPDEAP
LLVRSLLSAGLDTTVNGIGAAVYCLARFPGELQRLRSDPTLARNAFEEAVRFESPVQTFFRTTTREVELGGAVIGEGEKV
LMFLGSANRDPRRWSDPDLYDITRKTSGHVGFGSGVHMCVGQLVARLEGEVMLSALARKVAAIDIDGPVKRRFNNTLRGL
ESLPVKLTPA

The crystallisation buffer was 100 mM Bis-Tris buffer (adjusted to pH 5.0-5.75 with acetic acid), 0.2 M magnesium acetate and 20-32% PEG 3350

Cytochrome P450, heterocycle, furan, OXIDOREDUCTASE