Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

8EIO

The complex of phosphorylated human delta F508 cystic fibrosis transmembrane conductance regulator (CFTR) with elexacaftor (VX-445), lumacaftor (VX-809) and ATP/Mg

Functional Information from GO Data
ChainGOidnamespacecontents
A0005254molecular_functionchloride channel activity
A0005260molecular_functionintracellularly ATP-gated chloride channel activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005765cellular_componentlysosomal membrane
A0005768cellular_componentendosome
A0005769cellular_componentearly endosome
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006695biological_processcholesterol biosynthetic process
A0006811biological_processmonoatomic ion transport
A0006821biological_processchloride transport
A0006904biological_processvesicle docking involved in exocytosis
A0009986cellular_componentcell surface
A0010008cellular_componentendosome membrane
A0015106molecular_functionbicarbonate transmembrane transporter activity
A0015108molecular_functionchloride transmembrane transporter activity
A0015701biological_processbicarbonate transport
A0016020cellular_componentmembrane
A0016324cellular_componentapical plasma membrane
A0016853molecular_functionisomerase activity
A0016887molecular_functionATP hydrolysis activity
A0017081molecular_functionchloride channel regulator activity
A0019869molecular_functionchloride channel inhibitor activity
A0019899molecular_functionenzyme binding
A0030165molecular_functionPDZ domain binding
A0030301biological_processcholesterol transport
A0030660cellular_componentGolgi-associated vesicle membrane
A0030669cellular_componentclathrin-coated endocytic vesicle membrane
A0031901cellular_componentearly endosome membrane
A0032991cellular_componentprotein-containing complex
A0034220biological_processmonoatomic ion transmembrane transport
A0034707cellular_componentchloride channel complex
A0034976biological_processresponse to endoplasmic reticulum stress
A0035377biological_processtransepithelial water transport
A0035774biological_processpositive regulation of insulin secretion involved in cellular response to glucose stimulus
A0042626molecular_functionATPase-coupled transmembrane transporter activity
A0043225molecular_functionATPase-coupled inorganic anion transmembrane transporter activity
A0045921biological_processpositive regulation of exocytosis
A0048240biological_processsperm capacitation
A0050891biological_processmulticellular organismal-level water homeostasis
A0051087molecular_functionprotein-folding chaperone binding
A0051454biological_processintracellular pH elevation
A0051649biological_processestablishment of localization in cell
A0055037cellular_componentrecycling endosome
A0055038cellular_componentrecycling endosome membrane
A0055085biological_processtransmembrane transport
A0060081biological_processmembrane hyperpolarization
A0070175biological_processpositive regulation of enamel mineralization
A0071320biological_processcellular response to cAMP
A0097186biological_processamelogenesis
A0106138molecular_functionSec61 translocon complex binding
A0140359molecular_functionABC-type transporter activity
A1902161biological_processpositive regulation of cyclic nucleotide-gated ion channel activity
A1902476biological_processchloride transmembrane transport
A1902943biological_processpositive regulation of voltage-gated chloride channel activity
A1904322biological_processcellular response to forskolin
Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGQRARISLARAV
ChainResidueDetails
ALEU548-VAL562

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues76
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
AMET1-PHE77

site_idSWS_FT_FI2
Number of Residues20
DetailsTRANSMEM: Helical; Name=1 => ECO:0000269|Ref.56
ChainResidueDetails
APHE78-GLN98

site_idSWS_FT_FI3
Number of Residues99
DetailsTOPO_DOM: Extracellular => ECO:0000269|Ref.56
ChainResidueDetails
APRO99-TYR122
AGLU217-SER222
ALEU320-THR339
ALEU881-TYR919
APRO1013-TYR1014
ASER1118-ILE1131

site_idSWS_FT_FI4
Number of Residues23
DetailsTRANSMEM: Helical; Name=2 => ECO:0000269|Ref.56
ChainResidueDetails
ALEU123-HIS146

site_idSWS_FT_FI5
Number of Residues1039
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|Ref.56
ChainResidueDetails
AHIS147-LEU195
AMET244-LYS298
AGLN359-LEU859
ALEU941-ILE991
ATHR1036-LEU1096

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=3 => ECO:0000269|Ref.56
ChainResidueDetails
AALA196-TRP216

site_idSWS_FT_FI7
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000269|Ref.56
ChainResidueDetails
AALA223-MET243

site_idSWS_FT_FI8
Number of Residues20
DetailsTRANSMEM: Helical; Name=5 => ECO:0000269|Ref.56
ChainResidueDetails
AALA299-PHE319

site_idSWS_FT_FI9
Number of Residues18
DetailsTRANSMEM: Helical; Name=6 => ECO:0000269|Ref.56
ChainResidueDetails
AILE340-VAL358

site_idSWS_FT_FI10
Number of Residues20
DetailsTRANSMEM: Helical; Name=7 => ECO:0000269|Ref.56
ChainResidueDetails
AILE860-VAL880

site_idSWS_FT_FI11
Number of Residues20
DetailsTRANSMEM: Discontinuously helical; Name=8 => ECO:0000269|Ref.56
ChainResidueDetails
AVAL920-THR940

site_idSWS_FT_FI12
Number of Residues20
DetailsTRANSMEM: Helical; Name=9 => ECO:0000269|Ref.56
ChainResidueDetails
APHE992-GLN1012

site_idSWS_FT_FI13
Number of Residues20
DetailsTRANSMEM: Helical; Name=10 => ECO:0000269|Ref.56
ChainResidueDetails
AILE1015-GLN1035

site_idSWS_FT_FI14
Number of Residues20
DetailsTRANSMEM: Helical; Name=11 => ECO:0000269|Ref.56
ChainResidueDetails
AARG1097-ILE1117

site_idSWS_FT_FI15
Number of Residues20
DetailsTRANSMEM: Helical; Name=12 => ECO:0000269|Ref.56
ChainResidueDetails
AILE1132-ASP1152

site_idSWS_FT_FI16
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15528182, ECO:0000269|PubMed:20150177, ECO:0007744|PDB:1XMI, ECO:0007744|PDB:1XMJ, ECO:0007744|PDB:2BBO, ECO:0007744|PDB:2BBS, ECO:0007744|PDB:2BBT, ECO:0007744|PDB:2PZE, ECO:0007744|PDB:2PZF, ECO:0007744|PDB:2PZG
ChainResidueDetails
ATRP401

site_idSWS_FT_FI17
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:20150177, ECO:0007744|PDB:2PZE, ECO:0007744|PDB:2PZF, ECO:0007744|PDB:2PZG
ChainResidueDetails
ASER434

site_idSWS_FT_FI18
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00434, ECO:0000269|PubMed:15528182, ECO:0007744|PDB:1XMI, ECO:0007744|PDB:1XMJ, ECO:0007744|PDB:2BBO, ECO:0007744|PDB:2BBS, ECO:0007744|PDB:2BBT
ChainResidueDetails
AGLY458

site_idSWS_FT_FI19
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15528182, ECO:0007744|PDB:1XMI, ECO:0007744|PDB:2BBO, ECO:0007744|PDB:2BBS
ChainResidueDetails
AGLN493

site_idSWS_FT_FI20
Number of Residues1
DetailsBINDING: BINDING => ECO:0007744|PDB:3GD7
ChainResidueDetails
ATHR1220

site_idSWS_FT_FI21
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00434, ECO:0007744|PDB:3GD7
ChainResidueDetails
AARG1245

site_idSWS_FT_FI22
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231
ChainResidueDetails
AGLY550

site_idSWS_FT_FI23
Number of Residues4
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:1377674, ECO:0000269|PubMed:22119790, ECO:0000269|PubMed:25330774, ECO:0000269|PubMed:9385646
ChainResidueDetails
AILE661
AILE701
ALEU738
ALEU796

site_idSWS_FT_FI24
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:25330774
ChainResidueDetails
ALEU671

site_idSWS_FT_FI25
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000269|PubMed:1377674, ECO:0000269|PubMed:22119790
ChainResidueDetails
APHE687

site_idSWS_FT_FI26
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:22119790, ECO:0000269|PubMed:25330774, ECO:0000269|PubMed:9385646
ChainResidueDetails
AILE713

site_idSWS_FT_FI27
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:22119790
ChainResidueDetails
APRO718

site_idSWS_FT_FI28
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:25330774, ECO:0000269|PubMed:9385646
ChainResidueDetails
AVAL754

site_idSWS_FT_FI29
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:1377674, ECO:0000269|PubMed:25330774, ECO:0000269|PubMed:9385646
ChainResidueDetails
AVAL769
AGLN814

site_idSWS_FT_FI30
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000269|PubMed:1377674
ChainResidueDetails
ATHR791

site_idSWS_FT_FI31
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:22119790
ChainResidueDetails
AASP1445
ALYS1457

site_idSWS_FT_FI32
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:22119790
ChainResidueDetails
AGLN525
ATHR1396

site_idSWS_FT_FI33
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:7518437, ECO:0000305|PubMed:20008117
ChainResidueDetails
ASER895
AASN901

site_idSWS_FT_FI34
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:22119790
ChainResidueDetails
AGLN689

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon