Structure of PDB 8eig Chain A Binding Site BS03

Receptor Information
>8eig Chain A (length=1141) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RSPLEKASVVSKLFFSWTRPILRKGYRQRLELSDIYQIPSVDSADNLSEK
LEREWDRELASKKNPKLINALRRCFFWRFMFYGIFLYLGEVTKAVQPLLL
GRIIASYDPDNKEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQM
RIAMFSLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVW
IAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQAGLGRMMMKYRDQRA
GKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYV
RYFNSSAFFFSGFFVVFLSVLPYALIKGIILRKIFTTISFCIVLRMAVTR
QFPWAVQTWYDSLGAINKIQDFLQKQEYKTLEYNLTTTEVVMENVTAFWE
GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG
RISFCSQFSWIMPGTIKENIIGVSYDEYRYRSVIKACQLEEDISKFAEKD
NIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIF
ESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQNLW
NTYLRYITVHKSLIFVLIWCLVIFLAEVAASLVVLWLLGNTPSYAVIITS
TSSYYVFYIYVGVADTLLAMGFFRGLPLVHTLITVSKILHHKMLHSVLQA
PMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVA
VLQPYIFVATVPVIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSL
KGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVI
FFIAVTFISILTTGEGEGRVGIILTLAMNIMSTLQWAVNSSIDVDSLMRS
VSRVFKFIDMPTEGIWPSGGQMTVKDLTAKYTEGGNAILENISFSISPGQ
RVGLLGRTGSGKSTLLSAFLRLLNTEGEIQIDGVSWDSITLQQWRKAFGV
IPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFV
LVDGGCVLSHGHKQLMCLARSVLSKAKILLLDQPSAHLDPVTYQIIRRTL
KQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQK
Ligand information
Ligand IDWJX
InChIInChI=1S/C26H34F3N7O4S/c1-16-12-25(5,6)35(13-16)22-18(23(37)33-41(38,39)19-14-34(7)31-17(19)2)8-9-20(30-22)36-11-10-21(32-36)40-15-24(3,4)26(27,28)29/h8-11,14,16H,12-13,15H2,1-7H3,(H,33,37)/t16-/m0/s1
InChIKeyMVRHVFSOIWFBTE-INIZCTEOSA-N
SMILES
SoftwareSMILES
CACTVS 3.385C[CH]1CN(c2nc(ccc2C(=O)N[S](=O)(=O)c3cn(C)nc3C)n4ccc(OCC(C)(C)C(F)(F)F)n4)C(C)(C)C1
CACTVS 3.385C[C@@H]1CN(c2nc(ccc2C(=O)N[S](=O)(=O)c3cn(C)nc3C)n4ccc(OCC(C)(C)C(F)(F)F)n4)C(C)(C)C1
OpenEye OEToolkits 2.0.7Cc1c(cn(n1)C)S(=O)(=O)NC(=O)c2ccc(nc2N3C[C@H](CC3(C)C)C)n4ccc(n4)OCC(C)(C)C(F)(F)F
OpenEye OEToolkits 2.0.7Cc1c(cn(n1)C)S(=O)(=O)NC(=O)c2ccc(nc2N3CC(CC3(C)C)C)n4ccc(n4)OCC(C)(C)C(F)(F)F
ACDLabs 12.01O=S(=O)(NC(=O)c1ccc(nc1N1CC(C)CC1(C)C)n1ccc(OCC(C)(C)C(F)(F)F)n1)c1cn(C)nc1C
FormulaC26 H34 F3 N7 O4 S
Name(6P)-N-(1,3-dimethyl-1H-pyrazole-4-sulfonyl)-6-[3-(3,3,3-trifluoro-2,2-dimethylpropoxy)-1H-pyrazol-1-yl]-2-[(4S)-2,2,4-trimethylpyrrolidin-1-yl]pyridine-3-carboxamide;
Elexacaftor
ChEMBLCHEMBL4298128
DrugBankDB15444
ZINC
PDB chain8eig Chain A Residue 1506 [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]
PDB8eig Molecular structures reveal synergistic rescue of Delta 508 CFTR by Trikafta modulators.
Resolution3.6 Å
Binding residue
(original residue number in PDB)		R21 L24 R1102 M1105
Binding residue
(residue number reindexed from 1)		R19 L22 R843 M846
Annotation score1
Enzymatic activity
Enzyme Commision number 5.6.1.6: channel-conductance-controlling ATPase.
Gene Ontology
Molecular Function
GO:0005254 chloride channel activity
GO:0005260 intracellularly ATP-gated chloride channel activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0015106 bicarbonate transmembrane transporter activity
GO:0015108 chloride transmembrane transporter activity
GO:0016853 isomerase activity
GO:0016887 ATP hydrolysis activity
GO:0017081 chloride channel regulator activity
GO:0019869 chloride channel inhibitor activity
GO:0019899 enzyme binding
GO:0030165 PDZ domain binding
GO:0042626 ATPase-coupled transmembrane transporter activity
GO:0043225 ATPase-coupled inorganic anion transmembrane transporter activity
GO:0051087 protein-folding chaperone binding
GO:0071889 14-3-3 protein binding
GO:0106138 Sec61 translocon complex binding
GO:0140359 ABC-type transporter activity
Biological Process
GO:0006695 cholesterol biosynthetic process
GO:0006811 monoatomic ion transport
GO:0006821 chloride transport
GO:0006904 vesicle docking involved in exocytosis
GO:0015701 bicarbonate transport
GO:0030301 cholesterol transport
GO:0034220 monoatomic ion transmembrane transport
GO:0034976 response to endoplasmic reticulum stress
GO:0035377 transepithelial water transport
GO:0035774 positive regulation of insulin secretion involved in cellular response to glucose stimulus
GO:0045921 positive regulation of exocytosis
GO:0048240 sperm capacitation
GO:0050891 multicellular organismal-level water homeostasis
GO:0051454 intracellular pH elevation
GO:0051649 establishment of localization in cell
GO:0055085 transmembrane transport
GO:0060081 membrane hyperpolarization
GO:0070175 positive regulation of enamel mineralization
GO:0071320 cellular response to cAMP
GO:0097186 amelogenesis
GO:1902161 positive regulation of cyclic nucleotide-gated ion channel activity
GO:1902476 chloride transmembrane transport
GO:1902943 positive regulation of voltage-gated chloride channel activity
GO:1904322 cellular response to forskolin
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005765 lysosomal membrane
GO:0005768 endosome
GO:0005769 early endosome
GO:0005783 endoplasmic reticulum
GO:0005789 endoplasmic reticulum membrane
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0009986 cell surface
GO:0010008 endosome membrane
GO:0016020 membrane
GO:0016324 apical plasma membrane
GO:0030660 Golgi-associated vesicle membrane
GO:0030669 clathrin-coated endocytic vesicle membrane
GO:0031901 early endosome membrane
GO:0032991 protein-containing complex
GO:0034707 chloride channel complex
GO:0055037 recycling endosome
GO:0055038 recycling endosome membrane

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:8eig, PDBe:8eig, PDBj:8eig
PDBsum8eig
PubMed36264792
UniProtP13569|CFTR_HUMAN Cystic fibrosis transmembrane conductance regulator (Gene Name=CFTR)

[Back to BioLiP]