3IBD

Crystal structure of a cytochrome P450 2B6 genetic variant in complex with the inhibitor 4-(4-chlorophenyl)imidazole

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004497	molecular_function	monooxygenase activity
A	0005506	molecular_function	iron ion binding
A	0005737	cellular_component	cytoplasm
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0006629	biological_process	lipid metabolic process
A	0006805	biological_process	xenobiotic metabolic process
A	0008202	biological_process	steroid metabolic process
A	0008390	molecular_function	testosterone 16-alpha-hydroxylase activity
A	0008392	molecular_function	arachidonate epoxygenase activity
A	0016491	molecular_function	oxidoreductase activity
A	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A	0016712	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
A	0019373	biological_process	epoxygenase P450 pathway
A	0020037	molecular_function	heme binding
A	0042178	biological_process	xenobiotic catabolic process
A	0042180	biological_process	ketone metabolic process
A	0046872	molecular_function	metal ion binding
A	0062184	molecular_function	testosterone 16-beta-hydroxylase activity
A	0062187	molecular_function	anandamide 8,9 epoxidase activity
A	0062188	molecular_function	anandamide 11,12 epoxidase activity
A	0062189	molecular_function	anandamide 14,15 epoxidase activity
A	0101021	molecular_function	estrogen 2-hydroxylase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	24
Details	BINDING SITE FOR RESIDUE HEM A 500

Chain	Residue
A	HOH14
A	THR303
A	THR306
A	GLN357
A	LEU363
A	VAL367
A	HIS369
A	LEU392
A	PRO428
A	PHE429
A	SER430
A	ARG98
A	ARG434
A	CYS436
A	LEU437
A	GLY438
A	CPZ501
A	VAL113
A	ILE114
A	TRP121
A	ARG125
A	ALA298
A	GLY299
A	THR302

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CPZ A 501

Chain	Residue
A	PHE297
A	ALA298
A	THR302
A	VAL367
A	HOH497
A	HEM500

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CM5 A 1001

Chain	Residue
A	PHE188
A	GLU194
A	MET198
A	PHE202
A	TYR244
A	PHE296

---

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CM5 A 1002

Chain	Residue
A	ASP47
A	LEU51

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SCN A 1003

Chain	Residue
A	LYS91
A	ALA92
A	GLU93
A	ALA94
A	SER461
A	PRO462

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SCN A 1004

Chain	Residue
A	ALA321
A	GLU322
A	MET459
A	ARG491
A	HOH607

---

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SCN A 1005

Chain	Residue
A	TYR317
A	PRO318
A	HIS319

---

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SCN A 1006

Chain	Residue
A	ARG57
A	PHE58
A	LYS61

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PHE429-GLY438

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Binding site: {"description":"axial binding residue"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by PKA","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---