Structure of PDB 5fsa Chain B

Receptor sequence
>5fsaB (length=483) Species: 5476 (Candida albicans) [Search protein sequence]
KTPPLVFYWIPWFGSAASYGQQPYEFFESCRQKYGDVFSFMLLGKIMTVY
LGPKGHEFVFNAKLSDVSAEEAYKHLTTPVFGTGVIYDCPNSRLMEQKKF
AKFALTTDSFKRYVPKIREEILNYFVTDESFKLKEKTHGVANVMKTQPEI
TIFTASRSLFGDEMRRIFDRSFAQLYSDLDKGFTPINFVFPNLPLPHYWR
RDAAQKKISATYMKEIKLRRERGDIDPNRDLIDSLLIHSTYKDGVKMTDQ
EIANLLIGILMGGQHTSASTSAWFLLHLGEKPHLQDVIYQEVVELLKEKG
GDLNDLTYEDLQKLPSVNNTIKETLRMHMPLHSIFRKVTNPLRIPETNYI
VPKGHYVLVSPGYAHTSERYFDNPEDFDPTRWDTAAAKANSVSFNSSDEV
DYGFGKVSKGVSSPYLPFGGGRHRCIGEQFAYVQLGTILTTFVYNLRWTI
DGYKVPDPDYSSMVVLPTEPAEIIWEKRETCMF
3D structure
PDB5fsa Structural analyses of Candida albicans sterol 14 alpha-demethylase complexed with azole drugs address the molecular basis of azole-mediated inhibition of fungal sterol biosynthesis.
ChainB
Resolution2.86 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.14.14.154: sterol 14alpha-demethylase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 HEM B Y132 K143 G308 T311 P375 I379 R381 P462 F463 H468 C470 I471 G472 Y87 K98 G263 T266 P330 I334 R336 P417 F418 H423 C425 I426 G427
BS02 X2N B G65 Q66 Y118 F126 P230 G307 L376 H377 F380 S506 S507 M508 G20 Q21 Y73 F81 P185 G262 L331 H332 F335 S461 S462 M463 BindingDB: Kd=81nM
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0008398 sterol 14-demethylase activity
GO:0016491 oxidoreductase activity
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0020037 heme binding
GO:0046872 metal ion binding
Biological Process
GO:0001766 membrane raft polarization
GO:0006696 ergosterol biosynthetic process
GO:0007032 endosome organization
GO:0016126 sterol biosynthetic process
GO:0036187 cell growth mode switching, budding to filamentous
Cellular Component
GO:0005783 endoplasmic reticulum
GO:0005789 endoplasmic reticulum membrane
GO:0005886 plasma membrane
GO:0016020 membrane
GO:0032541 cortical endoplasmic reticulum
GO:0097038 perinuclear endoplasmic reticulum

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5fsa, PDBe:5fsa, PDBj:5fsa
PDBsum5fsa
PubMed28258218
UniProtP10613|CP51_CANAL Lanosterol 14-alpha demethylase (Gene Name=ERG11)

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