7XBN

Crystal Structure of YC-17-bound cytochrome P450 PikC with the unnatural amino acid p-Acetyl-L-Phenylalanine incorporated at position 238

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004497	molecular_function	monooxygenase activity
A	0005506	molecular_function	iron ion binding
A	0006707	biological_process	cholesterol catabolic process
A	0008395	molecular_function	steroid hydroxylase activity
A	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A	0017000	biological_process	antibiotic biosynthetic process
A	0020037	molecular_function	heme binding
A	0033068	biological_process	macrolide biosynthetic process
A	0036199	molecular_function	cholest-4-en-3-one 26-monooxygenase activity
A	0046872	molecular_function	metal ion binding
A	0055114	biological_process	obsolete oxidation-reduction process
B	0004497	molecular_function	monooxygenase activity
B	0005506	molecular_function	iron ion binding
B	0006707	biological_process	cholesterol catabolic process
B	0008395	molecular_function	steroid hydroxylase activity
B	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B	0017000	biological_process	antibiotic biosynthetic process
B	0020037	molecular_function	heme binding
B	0033068	biological_process	macrolide biosynthetic process
B	0036199	molecular_function	cholest-4-en-3-one 26-monooxygenase activity
B	0046872	molecular_function	metal ion binding
B	0055114	biological_process	obsolete oxidation-reduction process

Functional Information from PROSITE/UniProt

site_id	PS00086
Number of Residues	10
Details	CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGhGIHFCIG

Chain	Residue	Details
A	PHE347-GLY356

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:16825192, ECO:0000269\|PubMed:19124459

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: axial binding residue => ECO:0000269\|PubMed:16825192, ECO:0000269\|PubMed:19124459, ECO:0000269\|PubMed:19833867, ECO:0000269\|PubMed:24627965, ECO:0000312\|PDB:2C6H, ECO:0000312\|PDB:2C7X, ECO:0000312\|PDB:2CA0, ECO:0000312\|PDB:2CD8, ECO:0000312\|PDB:2VZ7, ECO:0000312\|PDB:2VZM, ECO:0000312\|PDB:2WHW, ECO:0000312\|PDB:2WI9, ECO:0000312\|PDB:3ZK5, ECO:0000312\|PDB:4B7D, ECO:0000312\|PDB:4B7S, ECO:0000312\|PDB:4BF4