Structure of PDB 5fsa Chain B Binding Site BS01

Receptor Information
>5fsa Chain B (length=483) Species: 5476 (Candida albicans) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KTPPLVFYWIPWFGSAASYGQQPYEFFESCRQKYGDVFSFMLLGKIMTVY
LGPKGHEFVFNAKLSDVSAEEAYKHLTTPVFGTGVIYDCPNSRLMEQKKF
AKFALTTDSFKRYVPKIREEILNYFVTDESFKLKEKTHGVANVMKTQPEI
TIFTASRSLFGDEMRRIFDRSFAQLYSDLDKGFTPINFVFPNLPLPHYWR
RDAAQKKISATYMKEIKLRRERGDIDPNRDLIDSLLIHSTYKDGVKMTDQ
EIANLLIGILMGGQHTSASTSAWFLLHLGEKPHLQDVIYQEVVELLKEKG
GDLNDLTYEDLQKLPSVNNTIKETLRMHMPLHSIFRKVTNPLRIPETNYI
VPKGHYVLVSPGYAHTSERYFDNPEDFDPTRWDTAAAKANSVSFNSSDEV
DYGFGKVSKGVSSPYLPFGGGRHRCIGEQFAYVQLGTILTTFVYNLRWTI
DGYKVPDPDYSSMVVLPTEPAEIIWEKRETCMF
Ligand information
Ligand IDHEM
InChIInChI=1S/C34H34N4O4.Fe/c1-7-21-17(3)25-13-26-19(5)23(9-11-33(39)40)31(37-26)16-32-24(10-12-34(41)42)20(6)28(38-32)15-30-22(8-2)18(4)27(36-30)14-29(21)35-25;/h7-8,13-16H,1-2,9-12H2,3-6H3,(H4,35,36,37,38,39,40,41,42);/q;+2/p-2/b25-13-,26-13-,27-14-,28-15-,29-14-,30-15-,31-16-,32-16-;
InChIKeyKABFMIBPWCXCRK-RGGAHWMASA-L
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6Cc1c2n3c(c1CCC(=O)O)C=C4C(=C(C5=[N]4[Fe]36[N]7=C(C=C8N6C(=C5)C(=C8C)C=C)C(=C(C7=C2)C)C=C)C)CCC(=O)O
CACTVS 3.385CC1=C(CCC(O)=O)C2=Cc3n4[Fe]5|6|N2=C1C=c7n5c(=CC8=N|6C(=Cc4c(C)c3CCC(O)=O)C(=C8C=C)C)c(C)c7C=C
ACDLabs 12.01C=1c3c(c(c4C=C5C(=C(C=6C=C7C(=C(C8=CC=2C(=C(C=1N=2[Fe](n34)(N5=6)N78)CCC(=O)O)C)\C=C)C)\C=C)C)C)CCC(=O)O
FormulaC34 H32 Fe N4 O4
NamePROTOPORPHYRIN IX CONTAINING FE;
HEME
ChEMBL
DrugBankDB18267
ZINC
PDB chain5fsa Chain B Residue 580 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
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.
Resolution2.86 Å
Binding residue
(original residue number in PDB)		Y132 K143 G308 T311 P375 I379 R381 P462 F463 H468 C470 I471 G472
Binding residue
(residue number reindexed from 1)		Y87 K98 G263 T266 P330 I334 R336 P417 F418 H423 C425 I426 G427
Annotation score1
Enzymatic activity
Enzyme Commision number 1.14.14.154: sterol 14alpha-demethylase.
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

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

[Back to BioLiP]