3ZBY

Ligand-free structure of CYP142 from Mycobacterium smegmatis

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	0008203	biological_process	cholesterol metabolic process
A	0008395	molecular_function	steroid hydroxylase activity
A	0016042	biological_process	lipid catabolic process
A	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A	0020037	molecular_function	heme binding
A	0036199	molecular_function	cholest-4-en-3-one 26-monooxygenase activity
A	0046872	molecular_function	metal ion binding
B	0004497	molecular_function	monooxygenase activity
B	0005506	molecular_function	iron ion binding
B	0006707	biological_process	cholesterol catabolic process
B	0008203	biological_process	cholesterol metabolic process
B	0008395	molecular_function	steroid hydroxylase activity
B	0016042	biological_process	lipid catabolic process
B	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B	0020037	molecular_function	heme binding
B	0036199	molecular_function	cholest-4-en-3-one 26-monooxygenase activity
B	0046872	molecular_function	metal ion binding
C	0004497	molecular_function	monooxygenase activity
C	0005506	molecular_function	iron ion binding
C	0006707	biological_process	cholesterol catabolic process
C	0008203	biological_process	cholesterol metabolic process
C	0008395	molecular_function	steroid hydroxylase activity
C	0016042	biological_process	lipid catabolic process
C	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
C	0020037	molecular_function	heme binding
C	0036199	molecular_function	cholest-4-en-3-one 26-monooxygenase activity
C	0046872	molecular_function	metal ion binding
D	0004497	molecular_function	monooxygenase activity
D	0005506	molecular_function	iron ion binding
D	0006707	biological_process	cholesterol catabolic process
D	0008203	biological_process	cholesterol metabolic process
D	0008395	molecular_function	steroid hydroxylase activity
D	0016042	biological_process	lipid catabolic process
D	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
D	0020037	molecular_function	heme binding
D	0036199	molecular_function	cholest-4-en-3-one 26-monooxygenase activity
D	0046872	molecular_function	metal ion binding
E	0004497	molecular_function	monooxygenase activity
E	0005506	molecular_function	iron ion binding
E	0006707	biological_process	cholesterol catabolic process
E	0008203	biological_process	cholesterol metabolic process
E	0008395	molecular_function	steroid hydroxylase activity
E	0016042	biological_process	lipid catabolic process
E	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
E	0020037	molecular_function	heme binding
E	0036199	molecular_function	cholest-4-en-3-one 26-monooxygenase activity
E	0046872	molecular_function	metal ion binding
F	0004497	molecular_function	monooxygenase activity
F	0005506	molecular_function	iron ion binding
F	0006707	biological_process	cholesterol catabolic process
F	0008203	biological_process	cholesterol metabolic process
F	0008395	molecular_function	steroid hydroxylase activity
F	0016042	biological_process	lipid catabolic process
F	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
F	0020037	molecular_function	heme binding
F	0036199	molecular_function	cholest-4-en-3-one 26-monooxygenase activity
F	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
A	PHE336-GLY345

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: axial binding residue => ECO:0000269|PubMed:23489718, ECO:0000269|PubMed:25210044, ECO:0007744|PDB:2YOO, ECO:0007744|PDB:3ZBY, ECO:0007744|PDB:4TRI, ECO:0007744|PDB:4UAX

Chain	Residue	Details
A	CYS343
B	CYS343
C	CYS343
D	CYS343
E	CYS343
F	CYS343

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