4UYL

Crystal structure of sterol 14-alpha demethylase (CYP51B) from a pathogenic filamentous fungus Aspergillus fumigatus in complex with VNI

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	0006696	biological_process	ergosterol biosynthetic process
A	0008168	molecular_function	methyltransferase activity
A	0008398	molecular_function	sterol 14-demethylase activity
A	0009058	biological_process	biosynthetic process
A	0016020	cellular_component	membrane
A	0016126	biological_process	sterol biosynthetic 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	0032259	biological_process	methylation
A	0046872	molecular_function	metal ion binding
B	0004497	molecular_function	monooxygenase activity
B	0005506	molecular_function	iron ion binding
B	0005783	cellular_component	endoplasmic reticulum
B	0005789	cellular_component	endoplasmic reticulum membrane
B	0006696	biological_process	ergosterol biosynthetic process
B	0008168	molecular_function	methyltransferase activity
B	0008398	molecular_function	sterol 14-demethylase activity
B	0009058	biological_process	biosynthetic process
B	0016020	cellular_component	membrane
B	0016126	biological_process	sterol biosynthetic process
B	0016491	molecular_function	oxidoreductase activity
B	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B	0020037	molecular_function	heme binding
B	0032259	biological_process	methylation
B	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEM A 580

Chain	Residue
A	TYR136
A	PHE456
A	GLY457
A	HIS461
A	CYS463
A	GLY465
A	VNI590
A	LEU143
A	LYS147
A	SER311
A	LEU367
A	ILE373
A	ILE376
A	ARG378
A	PRO455

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site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE VNI A 590

Chain	Residue
A	VAL121
A	TYR122
A	LEU125
A	PHE130
A	PHE234
A	ALA303
A	MET306
A	ALA307
A	LEU503
A	HEM580

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site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE HEM B 580

Chain	Residue
B	TYR136
B	LYS147
B	SER311
B	ARG378
B	PRO455
B	PHE456
B	HIS461
B	CYS463
B	VNI590

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site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE VNI B 590

Chain	Residue
B	VAL121
B	TYR122
B	ALA303
B	MET306
B	ALA307
B	ILE377
B	HEM580

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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. FGaGRHRCIG

Chain	Residue	Details
A	PHE456-GLY465

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: axial binding residue => ECO:0007744|PDB:4UYL, ECO:0007744|PDB:4UYM, ECO:0007744|PDB:5FRB

Chain	Residue	Details
A	CYS463
B	CYS463

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