Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5VCC

Crystal structure of human CYP3A4 bound to glycerol

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002933	biological_process	lipid hydroxylation
A	0004497	molecular_function	monooxygenase activity
A	0005496	molecular_function	steroid binding
A	0005506	molecular_function	iron ion binding
A	0005515	molecular_function	protein 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	0006631	biological_process	fatty acid metabolic process
A	0006694	biological_process	steroid biosynthetic process
A	0006706	biological_process	steroid catabolic process
A	0006805	biological_process	xenobiotic metabolic process
A	0008202	biological_process	steroid metabolic process
A	0008203	biological_process	cholesterol metabolic process
A	0008209	biological_process	androgen metabolic process
A	0008210	biological_process	estrogen metabolic process
A	0008395	molecular_function	steroid hydroxylase activity
A	0008401	molecular_function	retinoic acid 4-hydroxylase activity
A	0009822	biological_process	alkaloid catabolic process
A	0016020	cellular_component	membrane
A	0016098	biological_process	monoterpenoid metabolic process
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	0019825	molecular_function	oxygen binding
A	0019899	molecular_function	enzyme binding
A	0020037	molecular_function	heme binding
A	0030343	molecular_function	vitamin D3 25-hydroxylase activity
A	0034875	molecular_function	caffeine oxidase activity
A	0036378	biological_process	calcitriol biosynthetic process from calciol
A	0042178	biological_process	xenobiotic catabolic process
A	0042359	biological_process	vitamin D metabolic process
A	0042369	biological_process	vitamin D catabolic process
A	0042572	biological_process	retinol metabolic process
A	0042573	biological_process	retinoic acid metabolic process
A	0042759	biological_process	long-chain fatty acid biosynthetic process
A	0043231	cellular_component	intracellular membrane-bounded organelle
A	0046222	biological_process	aflatoxin metabolic process
A	0046872	molecular_function	metal ion binding
A	0050591	molecular_function	quinine 3-monooxygenase activity
A	0050649	molecular_function	testosterone 6-beta-hydroxylase activity
A	0062181	molecular_function	1-alpha,25-dihydroxyvitamin D3 23-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	0070330	molecular_function	aromatase activity
A	0070576	molecular_function	vitamin D 24-hydroxylase activity
A	0070989	biological_process	oxidative demethylation
A	0101020	molecular_function	estrogen 16-alpha-hydroxylase activity
A	0101021	molecular_function	estrogen 2-hydroxylase activity
A	0102320	molecular_function	1,8-cineole 2-exo-monooxygenase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	24
Details	binding site for residue HEM A 601

Chain	Residue
A	ARG105
A	ALA370
A	ARG375
A	PRO434
A	PHE435
A	GLY436
A	SER437
A	ARG440
A	ASN441
A	CYS442
A	ILE443
A	ILE118
A	MET452
A	GOL602
A	EDO611
A	HOH788
A	HOH798
A	SER119
A	TRP126
A	ARG130
A	PHE137
A	PHE302
A	ALA305
A	GLY306

site_id	AC2
Number of Residues	8
Details	binding site for residue GOL A 602

Chain	Residue
A	SER119
A	ARG212
A	PHE304
A	ALA305
A	HEM601
A	EDO612
A	HOH798
A	HOH813

site_id	AC3
Number of Residues	6
Details	binding site for residue GOL A 603

Chain	Residue
A	PRO41
A	SER52
A	PHE60
A	GLU63
A	LYS67
A	TYR68

site_id	AC4
Number of Residues	8
Details	binding site for residue GOL A 604

Chain	Residue
A	THR42
A	LEU44
A	ASN49
A	LEU51
A	SER52
A	EDO613
A	HOH747
A	HOH760

site_id	AC5
Number of Residues	11
Details	binding site for residue GOL A 605

Chain	Residue
A	GLY56
A	PHE57
A	CYS58
A	MET371
A	SER478
A	GLY480
A	GLY481
A	LEU482
A	LEU483
A	GLN484
A	HOH706

site_id	AC6
Number of Residues	8
Details	binding site for residue GOL A 606

Chain	Residue
A	ILE50
A	LEU51
A	TYR53
A	HIS54
A	LEU216
A	LEU221
A	HOH714
A	HOH830

site_id	AC7
Number of Residues	6
Details	binding site for residue GOL A 607

Chain	Residue
A	LYS330
A	GLU354
A	MET358
A	GLU417
A	HOH705
A	HOH834

site_id	AC8
Number of Residues	4
Details	binding site for residue GOL A 608

Chain	Residue
A	ASP380
A	GLU382
A	PHE387
A	HOH738

site_id	AC9
Number of Residues	8
Details	binding site for residue GOL A 609

Chain	Residue
A	PRO39
A	PRO325
A	GLN328
A	GLN329
A	GLN332
A	SER464
A	HOH741
A	HOH870

site_id	AD1
Number of Residues	4
Details	binding site for residue EDO A 610

Chain	Residue
A	GLY40
A	GLN329
A	HOH725
A	HOH757

site_id	AD2
Number of Residues	3
Details	binding site for residue EDO A 611

Chain	Residue
A	ARG212
A	HEM601
A	HOH798

site_id	AD3
Number of Residues	3
Details	binding site for residue EDO A 612

Chain	Residue
A	PHE108
A	SER119
A	GOL602

site_id	AD4
Number of Residues	2
Details	binding site for residue EDO A 613

Chain	Residue
A	LEU51
A	GOL604

site_id	AD5
Number of Residues	4
Details	binding site for residue EDO A 614

Chain	Residue
A	TRP408
A	THR409
A	ARG418
A	EDO618

site_id	AD6
Number of Residues	3
Details	binding site for residue EDO A 615

Chain	Residue
A	LYS173
A	GLY177
A	SER311

site_id	AD7
Number of Residues	1
Details	binding site for residue EDO A 616

Chain	Residue
A	GLN279

site_id	AD8
Number of Residues	3
Details	binding site for residue EDO A 617

Chain	Residue
A	LEU351
A	ASP357
A	LYS453

site_id	AD9
Number of Residues	4
Details	binding site for residue EDO A 618

Chain	Residue
A	TYR407
A	TRP408
A	ASP428
A	EDO614

site_id	AE1
Number of Residues	6
Details	binding site for residue EDO A 619

Chain	Residue
A	ILE184
A	THR187
A	SER188
A	PHE271
A	PHE302
A	HOH799

site_id	AE2
Number of Residues	7
Details	binding site for residue EDO A 620

Chain	Residue
A	ASP76
A	GLY77
A	GLN78
A	GLN79
A	THR224
A	PRO227
A	HOH740

site_id	AE3
Number of Residues	2
Details	binding site for residue EDO A 621

Chain	Residue
A	PHE367
A	ARG403

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PHE435-GLY444

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: axial binding residue => ECO:0007744\|PDB:1TQN, ECO:0007744\|PDB:1W0G

Chain	Residue	Details
A	CYS442

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