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9IUL

The structure of Candida albicans Cdr1 in fluconazole-bound state

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005524molecular_functionATP binding
A0005886cellular_componentplasma membrane
A0009986cellular_componentcell surface
A0015244molecular_functionfluconazole transmembrane transporter activity
A0015247molecular_functionaminophospholipid flippase activity
A0015903biological_processfluconazole transport
A0016020cellular_componentmembrane
A0016887molecular_functionATP hydrolysis activity
A0017111molecular_functionribonucleoside triphosphate phosphatase activity
A0042626molecular_functionATPase-coupled transmembrane transporter activity
A0042910molecular_functionxenobiotic transmembrane transporter activity
A0045117biological_processazole transmembrane transport
A0045332biological_processphospholipid translocation
A0046677biological_processresponse to antibiotic
A0046898biological_processresponse to cycloheximide
A0055085biological_processtransmembrane transport
A0090554molecular_functionphosphatidylcholine floppase activity
A0090556molecular_functionphosphatidylserine floppase activity
A0140331biological_processaminophospholipid translocation
A0140341molecular_functionphosphatidylethanolamine floppase activity
A0140359molecular_functionABC-type transporter activity
A1901474molecular_functionazole transmembrane transporter activity
A1903561cellular_componentextracellular vesicle
A1903875molecular_functioncorticosterone binding
A1903924molecular_functionestradiol binding
A1990961biological_processxenobiotic detoxification by transmembrane export across the plasma membrane
Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. VSGGERKRVSIAEAS
ChainResidueDetails
AVAL303-SER317

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1019
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
AMET1-SER513
AGLU570-GLU597
AARG644-SER654
AASN786-GLY1195
AVAL1251-GLU1280
ACYS1336-THR1355
AALA1488-LYS1501

site_idSWS_FT_FI2
Number of Residues20
DetailsTRANSMEM: Helical; Name=1 => ECO:0000255
ChainResidueDetails
AILE514-TYR534

site_idSWS_FT_FI3
Number of Residues217
DetailsTOPO_DOM: Extracellular => ECO:0000305
ChainResidueDetails
AASN535-ALA548
AARG619-PRO622
APRO676-ASN764
ALYS1217-MET1229
ATYR1302-ARG1314
AMET1377-ASN1466

site_idSWS_FT_FI4
Number of Residues20
DetailsTRANSMEM: Helical; Name=2 => ECO:0000255
ChainResidueDetails
AALA549-PHE569

site_idSWS_FT_FI5
Number of Residues20
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255
ChainResidueDetails
ALEU598-PHE618

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255
ChainResidueDetails
AGLY623-PHE643

site_idSWS_FT_FI7
Number of Residues20
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255
ChainResidueDetails
AGLY655-ILE675

site_idSWS_FT_FI8
Number of Residues20
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255
ChainResidueDetails
ALEU765-PHE785

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255
ChainResidueDetails
ATYR1196-PHE1216

site_idSWS_FT_FI10
Number of Residues20
DetailsTRANSMEM: Helical; Name=8 => ECO:0000255
ChainResidueDetails
APHE1230-PHE1250

site_idSWS_FT_FI11
Number of Residues20
DetailsTRANSMEM: Helical; Name=9 => ECO:0000255
ChainResidueDetails
AILE1281-LEU1301

site_idSWS_FT_FI12
Number of Residues20
DetailsTRANSMEM: Helical; Name=10 => ECO:0000255
ChainResidueDetails
AGLY1315-LEU1335

site_idSWS_FT_FI13
Number of Residues20
DetailsTRANSMEM: Helical; Name=11 => ECO:0000255
ChainResidueDetails
AMET1356-PHE1376

site_idSWS_FT_FI14
Number of Residues20
DetailsTRANSMEM: Helical; Name=12 => ECO:0000255
ChainResidueDetails
APHE1467-LEU1487

site_idSWS_FT_FI15
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00434
ChainResidueDetails
AGLY895

236620

PDB entries from 2025-05-28

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