4FIA

Crystal Structure of Human CYP46A1 P450 with bicalutamide Bound

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004497	molecular_function	monooxygenase activity
A	0005506	molecular_function	iron ion binding
A	0005783	cellular_component	endoplasmic reticulum
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0006629	biological_process	lipid metabolic process
A	0006699	biological_process	bile acid biosynthetic process
A	0006707	biological_process	cholesterol catabolic process
A	0006805	biological_process	xenobiotic metabolic process
A	0007399	biological_process	nervous system development
A	0008202	biological_process	steroid metabolic process
A	0008203	biological_process	cholesterol metabolic process
A	0008207	biological_process	C21-steroid hormone metabolic process
A	0008395	molecular_function	steroid hydroxylase activity
A	0016125	biological_process	sterol 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	0020037	molecular_function	heme binding
A	0030425	cellular_component	dendrite
A	0033781	molecular_function	cholesterol 24-hydroxylase activity
A	0042448	biological_process	progesterone metabolic process
A	0046872	molecular_function	metal ion binding
A	0050649	molecular_function	testosterone 6-beta-hydroxylase activity
A	0062184	molecular_function	testosterone 16-beta-hydroxylase activity
A	0098793	cellular_component	presynapse
A	0098794	cellular_component	postsynapse
A	1900271	biological_process	regulation of long-term synaptic potentiation
A	1903044	biological_process	protein localization to membrane raft

Functional Information from PDB Data

site_id	AC1
Number of Residues	28
Details	BINDING SITE FOR RESIDUE HEM A 600

Chain	Residue
A	LYS104
A	THR306
A	SER307
A	HIS310
A	ALA367
A	THR370
A	PRO429
A	PHE430
A	ARG435
A	SER436
A	CYS437
A	TYR109
A	ILE438
A	GLY439
A	PHE442
A	ALA443
A	0U9601
A	198602
A	HOH705
A	HOH724
A	HOH769
A	LEU125
A	VAL126
A	TRP134
A	ARG138
A	PHE299
A	ALA302
A	GLY303

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site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE 0U9 A 601

Chain	Residue
A	PHE80
A	LEU112
A	ILE222
A	ARG226
A	ALA302
A	THR306
A	TRP368
A	GLY369
A	PHE371
A	GLU472
A	ALA474
A	THR475
A	HEM600
A	HOH705

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site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 198 A 602

Chain	Residue
A	PHE80
A	ILE222
A	ARG226
A	ALA302
A	THR306
A	TRP368
A	GLY369
A	PHE371
A	GLU472
A	ALA474
A	THR475
A	HEM600
A	HOH705

---

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL A 603

Chain	Residue
A	THR100
A	LYS101

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PHE430-GLY439

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"18621681","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20667828","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23288837","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2Q9F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2Q9G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MDR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MDT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MDV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ENH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FIA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4J14","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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