Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3G93

Single ligand occupancy crystal structure of cytochrome P450 2B4 in complex with the inhibitor 1-biphenyl-4-methyl-1H-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	0006082	biological_process	organic acid metabolic process
A	0006805	biological_process	xenobiotic metabolic process
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	0046872	molecular_function	metal ion binding
B	0004497	molecular_function	monooxygenase activity
B	0005506	molecular_function	iron ion binding
B	0005737	cellular_component	cytoplasm
B	0005789	cellular_component	endoplasmic reticulum membrane
B	0006082	biological_process	organic acid metabolic process
B	0006805	biological_process	xenobiotic metabolic process
B	0008392	molecular_function	arachidonate epoxygenase activity
B	0016491	molecular_function	oxidoreductase activity
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	0046872	molecular_function	metal ion binding
C	0004497	molecular_function	monooxygenase activity
C	0005506	molecular_function	iron ion binding
C	0005737	cellular_component	cytoplasm
C	0005789	cellular_component	endoplasmic reticulum membrane
C	0006082	biological_process	organic acid metabolic process
C	0006805	biological_process	xenobiotic metabolic process
C	0008392	molecular_function	arachidonate epoxygenase activity
C	0016491	molecular_function	oxidoreductase activity
C	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
C	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
C	0019373	biological_process	epoxygenase P450 pathway
C	0020037	molecular_function	heme binding
C	0046872	molecular_function	metal ion binding
D	0004497	molecular_function	monooxygenase activity
D	0005506	molecular_function	iron ion binding
D	0005737	cellular_component	cytoplasm
D	0005789	cellular_component	endoplasmic reticulum membrane
D	0006082	biological_process	organic acid metabolic process
D	0006805	biological_process	xenobiotic metabolic process
D	0008392	molecular_function	arachidonate epoxygenase activity
D	0016491	molecular_function	oxidoreductase activity
D	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
D	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
D	0019373	biological_process	epoxygenase P450 pathway
D	0020037	molecular_function	heme binding
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE HEM A 500

Chain	Residue
A	ARG98
A	HIS369
A	PRO428
A	PHE429
A	SER430
A	ARG434
A	CYS436
A	LEU437
A	GLY438
A	PB2501
A	TRP121
A	ARG125
A	PHE296
A	GLY299
A	THR302
A	THR303
A	ILE363
A	VAL367

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PB2 A 501

Chain	Residue
A	ALA298
A	GLY299
A	THR302
A	HEM500
B	PHE217
B	PHE223

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PB2 A 496

Chain	Residue
A	PHE217
A	PHE223
A	LEU224
B	ALA298
B	GLY299
B	THR302
B	PRO368
B	HEM500

site_id	AC4
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HEM B 500

Chain	Residue
A	PHE217
A	PB2496
B	ARG98
B	TRP121
B	ARG125
B	PHE296
B	GLY299
B	THR302
B	THR303
B	GLN357
B	ILE363
B	VAL367
B	HIS369
B	PRO428
B	PHE429
B	SER430
B	ARG434
B	CYS436
B	GLY438

site_id	AC5
Number of Residues	18
Details	BINDING SITE FOR RESIDUE HEM C 500

Chain	Residue
C	ARG98
C	ARG125
C	PHE296
C	GLY299
C	THR300
C	THR302
C	THR303
C	ILE363
C	VAL367
C	HIS369
C	PRO428
C	PHE429
C	SER430
C	ARG434
C	CYS436
C	GLY438
C	ALA442
C	PB2501

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PB2 C 501

Chain	Residue
C	ALA298
C	GLY299
C	THR302
C	ILE363
C	HEM500
D	PHE217
D	PHE223
D	LEU224

site_id	AC7
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEM D 500

Chain	Residue
D	ARG98
D	TRP121
D	ARG125
D	PHE296
D	GLY299
D	THR300
D	THR302
D	THR303
D	THR306
D	GLN357
D	ILE363
D	VAL367
D	HIS369
D	LEU392
D	PRO428
D	PHE429
D	SER430
D	ARG434
D	CYS436
D	LEU437
D	GLY438
D	PB2501

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PB2 D 501

Chain	Residue
C	PHE217
C	PHE223
C	LEU224
D	ALA298
D	GLY299
D	THR302
D	ILE363
D	HEM500

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	4
Details	Binding site: {"description":"axial binding residue"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine; by PKA","evidences":[{"source":"UniProtKB","id":"P00176","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1akd

Chain	Residue	Details
A	THR302
A	GLU301

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1akd

Chain	Residue	Details
B	THR302
B	GLU301

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1akd

Chain	Residue	Details
C	THR302
C	GLU301

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1akd

Chain	Residue	Details
D	THR302
D	GLU301

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