Crystal structure of human CYP7A1 in complex with cholest-4-en-3-one

CYP7A1, CYPVII, Cholesterol 7-alpha-hydroxylase, Cytochrome P450 7A1

MAKKTSSRRRQTGEPPLENGLIPYLGCALQFGANPLEFLRANQRKHGHVFTCKLMGKYVHFITNPLSYHKVLCHGKYFDW
KKFHFALSAKAFGHRSIDPMDGNTTENINDTFIKTLQGHALNSLTESMMENLQRIMRPPVSSNSKTAAWVTEGMYSFCYR
VMFEAGYLTIFGRDLTRRDTQKAHILNNLDNFKQFDKVFPALVAGLPIHMFRTAHNAREKLAESLRHENLQKRESISELI
SLRMFLNDTLSTFDDLEKAKTHLVVLWASQANTIPATFWSLFQMIRNPEAMKAATEEVKRTLENAGQKVSLEGNPICLSQ
AELNDLPVLDSIIKESLRLSSASLNIRTAKEDFTLHLEDGSYNIRKDDIIALYPQLMHLDPEIYPDPLTFKYDRYLDENG
KTKTTFYCNGLKLKYYYMPFGSGATICPGRLFAIHEIKQFLILMLSYFELELIEGQAKCPPLDQSRAGLGILPPLNDIEF
KYKFKHHHHHH

18% PEG550 MME, 0.1 M MES, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K

Cholestenone restraints are based on PDB entry 2X5W and were optimized on the prodrg server. Solvent atoms were added based on peaks in the Fo-Fc map. Non-crystallographic symmetry in the peak positions was considered in the rejection and addition of some sites. Solvent atoms were not included in refinement and structure factor calculation. Some of the assigned water positions likely represent other molecule/atom/ion types. REFMAC, Phenix, coot, and the molprobity server were also used.

cytochrome P450, cholesterol 7-alpha hydroxylase, CYP7A1, cholest-4-en-3-one, bile acid biosynthesis, Structural Genomics, Structural Genomics Consortium, SGC, OXIDOREDUCTASE

RRRQTGEPPLENGLIPYLGCALQFGANPLEFLRANQRKHGHVFTCKLMGKYVHFITNPLSYHKVLCHGKYFDWKKFHFAT
SAKAFGHRSIDPMDGNTTENINDTFIKTLQGHALNSLTESMMENLQRIMRPPVSSNSKTAAWVTEGMYSFCYRVMFEAGY
LTIFGRDLTRRDTQKAHILNNLDNFKQFDKVFPALVAGLPIHMFRTAHNAREKLAESLRHENLQKRESISELISLRMFLN
DTLSTFDDLEKAKTHLVVLWASQANTIPATFWSLFQMIRNPEAMKAATEEVKRTLENAGQKVSLEGNPICLSQAELNDLP
VLDSIIKESLRLSSASLNIRTAKEDFTLHLEDGSYNIRKDDIIALYPQLMHLDPEIYPDPLTFKYDRYLDENGKTKTTFY
CNGLKLKYYYMPFGSGATICPGRLFAIHEIKQFLILMLSYFELELIEGQAKCPPLDQSRAGLGILPPLNDIEFKYKFKH