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Crystal structure of Trypanosoma cruzi CYP51 bound to the inhibitor (R)-N-(3-(1H-indol-3-yl)-1-oxo-1-(pyridin-4-ylamino)propan-2-yl)-3,3'- difluoro-(1,1'-biphenyl)-4-carboxamide

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 Residues23
DetailsBINDING SITE FOR RESIDUE HEM A 1450
ChainResidue
ATYR103
ASER296
ATHR299
ALEU356
AVAL359
AARG361
AGLY414
APHE415
AGLY416
AHIS420
ALYS421
ATYR116
ACYS422
AILE423
AGLY424
A5PS1460
ALEU127
ALEU130
ALEU134
AALA288
AALA291
AGLY292
ATHR295

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 5PS A 1460
ChainResidue
AMET106
ATYR116
AVAL213
AALA291
ALEU356
AMET358
AMET460
AVAL461
AHEM1450

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEM B 1450
ChainResidue
BTYR103
BTYR116
BALA288
BALA291
BGLY292
BTHR295
BTHR299
BVAL359
BARG361
BGLY414
BPHE415
BGLY416
BHIS420
BCYS422
BGLY424
B5PS1460

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 5PS B 1460
ChainResidue
BTYR103
BMET106
BTYR116
BPHE290
BALA291
BLEU356
BMET460
BHEM1450

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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