Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4RRT

Crystal structure of a human cytochrome P450 2B6 (Y226H/K262R) in complex with (+)-3-carene

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	0005783	cellular_component	endoplasmic reticulum
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	arachidonic acid epoxygenase activity
A	0016020	cellular_component	membrane
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	cellular ketone metabolic process
A	0043231	cellular_component	intracellular membrane-bounded organelle
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
B	0004497	molecular_function	monooxygenase activity
B	0005506	molecular_function	iron ion binding
B	0005737	cellular_component	cytoplasm
B	0005783	cellular_component	endoplasmic reticulum
B	0005789	cellular_component	endoplasmic reticulum membrane
B	0006629	biological_process	lipid metabolic process
B	0006805	biological_process	xenobiotic metabolic process
B	0008202	biological_process	steroid metabolic process
B	0008390	molecular_function	testosterone 16-alpha-hydroxylase activity
B	0008392	molecular_function	arachidonic acid epoxygenase activity
B	0016020	cellular_component	membrane
B	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B	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
B	0019373	biological_process	epoxygenase P450 pathway
B	0020037	molecular_function	heme binding
B	0042178	biological_process	xenobiotic catabolic process
B	0042180	biological_process	cellular ketone metabolic process
B	0043231	cellular_component	intracellular membrane-bounded organelle
B	0046872	molecular_function	metal ion binding
B	0062184	molecular_function	testosterone 16-beta-hydroxylase activity
B	0062187	molecular_function	anandamide 8,9 epoxidase activity
B	0062188	molecular_function	anandamide 11,12 epoxidase activity
B	0062189	molecular_function	anandamide 14,15 epoxidase activity
B	0101021	molecular_function	estrogen 2-hydroxylase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEM A 501

Chain	Residue
A	ARG98
A	LEU362
A	VAL367
A	HIS369
A	LEU392
A	PRO428
A	PHE429
A	SER430
A	ARG434
A	CYS436
A	LEU437
A	VAL113
A	GLY438
A	3V4502
A	HOH663
A	ILE114
A	TRP121
A	ARG125
A	ILE179
A	ALA298
A	THR302
A	THR306

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE 3V4 A 502

Chain	Residue
A	PHE297
A	ALA298
A	THR302
A	VAL367
A	HEM501

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CM5 A 503

Chain	Residue
A	PHE220
A	PHE223

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CM5 A 504

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

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CM5 A 505

Chain	Residue
A	LEU43
A	MET46
A	ARG48
A	GLY50
A	GLN215

site_id	AC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE GOL A 506

Chain	Residue
A	HOH790

site_id	AC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE GOL A 507

Chain	Residue
A	HOH789

site_id	AC8
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEM B 501

Chain	Residue
B	ARG98
B	VAL113
B	ILE114
B	TRP121
B	ARG125
B	ILE179
B	ALA298
B	THR302
B	THR306
B	GLN357
B	LEU362
B	HIS369
B	LEU392
B	PRO428
B	PHE429
B	SER430
B	ARG434
B	CYS436
B	LEU437
B	GLY438
B	3V4502
B	HOH612

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE 3V4 B 502

Chain	Residue
B	PHE297
B	ALA298
B	VAL367
B	HEM501

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CM5 B 503

Chain	Residue
B	PHE220
B	PHE223

site_id	BC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CM5 B 504

Chain	Residue
A	LYS384
A	HOH810
B	GLU194
B	MET198
B	PHE202
B	TYR244
B	HIS247
B	PHE296
B	HOH796

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CM5 B 505

Chain	Residue
B	LEU43
B	MET46
B	ASP47
B	ARG48

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	2
Details	BINDING: axial binding residue

Chain	Residue	Details
A	GLN455
B	GLN455

site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: Phosphoserine; by PKA => ECO:0000250

Chain	Residue	Details
A	GLN147
B	GLN147

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)