The crystal structure of T252E CYP199A4 bound to 4-(pyridin-2-yl)benzoic acid

Characterisation of the heme aqua-ligand coordination environment in an engineered peroxygenase cytochrome P450 variant.

MISNSSAESISAPPNDSTIPHLAIDPFSLDFFDDPYPDQQTLRDAGPVVYLDKWNVYGVARYAEVHAVLNDPTTFCSSRG
VGLSDFKKEKPWRPPSLILEADPPAHTRPRAVLSKVLSPATMKTIRDGFAAAADAKVDELLQRGCIDAIADLAEAYPLSV
FPDAMGLKQEGREHLLPYAGLVFNAFGPPNELRQTAIERSAPHQAYVNEQCQRPNLAPGGFGACIHAFTDTGEITPDEAP
LLVRSLLSAGLDETVNGIGAAVYCLARFPGELQRLRSDPTLARNAFEEAVRFESPVQTFFRTTTREVELGGAVIGEGEKV
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, peroxygenase mutant, inhibitor, OXIDOREDUCTASE

MISNSSAESISAPPNDSTIPHLAIDPFSLDFFDDPYPDQQTLRDAGPVVYLDKWNVYGVARYAEVHAVLNDPTTFCSSRG
VGLSDFKKEKPWRPPSLILEADPPAHTRPRAVLSKVLSPATMKTIRDGFAAAADAKVDELLQRGCIDAIADLAEAYPLSV
FPDAMGLKQEGREHLLPYAGLVFNAFGPPNELRQTAIERSAPHQAYVNEQCQRPNLAPGGFGACIHAFTDTGEITPDEAP
LLVRSLLSAGLDTTVNGIGAAVYCLARFPGELQRLRSDPTLARNAFEEAVRFESPVQTFFRTTTREVELGGAVIGEGEKV
LMFLGSANRDPRRWSDPDLYDITRKTSGHVGFGSGVHMCVGQLVARLEGEVMLSALARKVAAIDIDGPVKRRFNNTLRGL
ESLPVKLTPA