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4CK8

STEROL 14-ALPHA DEMETHYLASE (CYP51)FROM TRYPANOSOMA CRUZI IN COMPLEX WITH (R)-1-(2,4-dichlorophenyl)-2-(1H-imidazol-1-yl)ethyl 4-(4-(3,4- dichlorophenyl)piperazin-1-yl)phenylcarbamate (LFD)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0008398molecular_functionsterol 14-demethylase activity
A0016020cellular_componentmembrane
A0016126biological_processsterol biosynthetic process
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0008398molecular_functionsterol 14-demethylase activity
B0016020cellular_componentmembrane
B0016126biological_processsterol biosynthetic process
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEM A 1480
ChainResidue
ATYR103
AGLY414
APHE415
AGLY416
AHIS420
ALYS421
ACYS422
AGLY424
ALFD1490
AALA288
AALA291
AGLY292
ATHR295
ATHR299
ALEU356
AVAL359
AARG361

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE LFD A 1490
ChainResidue
AILE45
APHE48
APHE110
ATYR116
APRO210
AVAL213
APHE290
AALA291
ATHR295
AMET460
AHEM1480

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEM B 1480
ChainResidue
BTYR103
BARG124
BLEU127
BALA288
BALA291
BGLY292
BTHR295
BTHR299
BLEU356
BVAL359
BARG361
BGLY414
BPHE415
BGLY416
BHIS420
BCYS422
BILE423
BGLY424
BLFD1490

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE LFD B 1490
ChainResidue
BILE45
BGLY49
BTYR103
BPHE110
BTYR116
BPRO210
BPHE290
BALA291
BTHR295
BLEU356
BMET460
BHEM1480

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGaGVHKCIG
ChainResidueDetails
APHE415-GLY424

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000250|UniProtKB:P0A512
ChainResidueDetails
ACYS422
BCYS422

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PDB entries from 2024-07-10

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