8A6W

Crystal structure of CYP142 from Mycobacterium tuberculosis in complex with cholestenone

Functional Information from GO Data

Chain	GOid	namespace	contents
B	0004497	molecular_function	monooxygenase activity
B	0005506	molecular_function	iron ion binding
B	0006629	biological_process	lipid metabolic process
B	0006707	biological_process	cholesterol catabolic process
B	0008202	biological_process	steroid metabolic process
B	0008203	biological_process	cholesterol metabolic process
B	0008395	molecular_function	steroid hydroxylase activity
B	0009274	cellular_component	peptidoglycan-based cell wall
B	0016042	biological_process	lipid catabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B	0020037	molecular_function	heme binding
B	0031073	molecular_function	cholesterol 26-hydroxylase activity
B	0036199	molecular_function	cholest-4-en-3-one 26-monooxygenase activity
B	0046872	molecular_function	metal ion binding
E	0004497	molecular_function	monooxygenase activity
E	0005506	molecular_function	iron ion binding
E	0006629	biological_process	lipid metabolic process
E	0006707	biological_process	cholesterol catabolic process
E	0008202	biological_process	steroid metabolic process
E	0008203	biological_process	cholesterol metabolic process
E	0008395	molecular_function	steroid hydroxylase activity
E	0009274	cellular_component	peptidoglycan-based cell wall
E	0016042	biological_process	lipid catabolic process
E	0016491	molecular_function	oxidoreductase activity
E	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
E	0020037	molecular_function	heme binding
E	0031073	molecular_function	cholesterol 26-hydroxylase activity
E	0036199	molecular_function	cholest-4-en-3-one 26-monooxygenase activity
E	0046872	molecular_function	metal ion binding

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
B	PHE333-GLY342

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"20889498","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2XKR","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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