Structure of PDB 8eig Chain A

Receptor sequence
>8eigA (length=1141) Species: 9606 (Homo sapiens) [Search protein sequence]
RSPLEKASVVSKLFFSWTRPILRKGYRQRLELSDIYQIPSVDSADNLSEK
LEREWDRELASKKNPKLINALRRCFFWRFMFYGIFLYLGEVTKAVQPLLL
GRIIASYDPDNKEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQM
RIAMFSLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVW
IAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQAGLGRMMMKYRDQRA
GKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYV
RYFNSSAFFFSGFFVVFLSVLPYALIKGIILRKIFTTISFCIVLRMAVTR
QFPWAVQTWYDSLGAINKIQDFLQKQEYKTLEYNLTTTEVVMENVTAFWE
GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG
RISFCSQFSWIMPGTIKENIIGVSYDEYRYRSVIKACQLEEDISKFAEKD
NIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIF
ESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQNLW
NTYLRYITVHKSLIFVLIWCLVIFLAEVAASLVVLWLLGNTPSYAVIITS
TSSYYVFYIYVGVADTLLAMGFFRGLPLVHTLITVSKILHHKMLHSVLQA
PMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVA
VLQPYIFVATVPVIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSL
KGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVI
FFIAVTFISILTTGEGEGRVGIILTLAMNIMSTLQWAVNSSIDVDSLMRS
VSRVFKFIDMPTEGIWPSGGQMTVKDLTAKYTEGGNAILENISFSISPGQ
RVGLLGRTGSGKSTLLSAFLRLLNTEGEIQIDGVSWDSITLQQWRKAFGV
IPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFV
LVDGGCVLSHGHKQLMCLARSVLSKAKILLLDQPSAHLDPVTYQIIRRTL
KQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQK
3D structure
PDB8eig Molecular structures reveal synergistic rescue of Delta 508 CFTR by Trikafta modulators.
ChainA
Resolution3.6 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 5.6.1.6: channel-conductance-controlling ATPase.
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 ATP A D173 W401 G461 G463 K464 T465 D171 W399 G425 G427 K428 T429
BS02 ATP A T547 S549 G551 Y1219 T1246 G1247 K1250 S1251 T510 S512 G514 Y931 T958 G959 K962 S963
BS03 WJX A R21 L24 R1102 M1105 R19 L22 R843 M846
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

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

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