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4LXJ

Saccharomyces cerevisiae lanosterol 14-alpha demethylase with lanosterol bound

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0006629biological_processlipid metabolic process
A0006694biological_processsteroid biosynthetic process
A0006696biological_processergosterol biosynthetic process
A0008202biological_processsteroid metabolic process
A0008398molecular_functionsterol 14-demethylase activity
A0016020cellular_componentmembrane
A0016126biological_processsterol biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEM A 601
ChainResidue
APHE113
ATHR322
ALEU374
APRO379
ALEU383
AARG385
APRO462
APHE463
AGLY464
AHIS468
ACYS470
ATYR126
AGLY472
AALA476
ALAN602
AOXY603
AHOH708
ATYR140
ALEU147
ALYS151
AVAL311
AGLY314
AGLY315
ATHR318

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE LAN A 602
ChainResidue
ATYR126
ALEU129
ATHR130
ATYR140
APHE236
APHE241
AGLY310
AGLY314
ALEU380
AHIS381
ASER382
ALEU383
APHE384
APHE506
ATHR507
ASER508
AMET509
AHEM601

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE OXY A 603
ChainResidue
AGLY314
AHEM601

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGgGRHRCIG
ChainResidueDetails
APHE463-GLY472

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"16847258","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24613931","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues488
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"16847258","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24613931","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24613931","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4LXJ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24613931","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5EQB","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"24613931","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4LXJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5EQB","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17330950","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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