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5JLC

Structure of CYP51 from the pathogen Candida glabrata

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0005783cellular_componentendoplasmic reticulum
A0006696biological_processergosterol biosynthetic process
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
A0032541cellular_componentcortical endoplasmic reticulum
A0046872molecular_functionmetal ion binding
A0097038cellular_componentperinuclear endoplasmic reticulum
Functional Information from PDB Data
site_idAC1
Number of Residues23
Detailsbinding site for residue HEM A 601
ChainResidue
APHE114
APRO380
ALEU384
AARG386
APRO464
APHE465
AGLY466
AHIS470
ACYS472
AILE473
AGLY474
ATYR127
APHE477
AALA478
A1YN602
AHOH732
ATYR141
ALEU148
ALYS152
AVAL312
AGLY315
AGLY316
ATHR319

site_idAC2
Number of Residues17
Detailsbinding site for residue 1YN A 602
ChainResidue
AALA70
ATYR73
ATYR127
AILE140
APHE237
AGLY311
AVAL312
AGLY315
ATHR319
AHIS382
ASER383
APHE385
APHE509
ATHR510
ASER511
AMET512
AHEM601

site_idAC3
Number of Residues5
Detailsbinding site for residue PGE A 603
ChainResidue
APRO422
AGLU426
AASN428
AHIS430
AARG431

site_idAC4
Number of Residues5
Detailsbinding site for residue 1PE A 604
ChainResidue
AGLU217
ALYS221
ATHR265
ASER268
AGLU272

site_idAC5
Number of Residues2
Detailsbinding site for residue CL A 605
ChainResidue
AARG180
AASN188

site_idAC6
Number of Residues1
Detailsbinding site for residue CL A 606
ChainResidue
ALYS156

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGgGRHRCIG
ChainResidueDetails
APHE465-GLY474

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: axial binding residue => ECO:0000250
ChainResidueDetails
ACYS472

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PDB entries from 2024-07-24

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