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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9DW8

Dephosphorylated (E1371Q)CFTR in complex with PKA-C

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
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
A0006833biological_processwater 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
A0016323cellular_componentbasolateral plasma membrane
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
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
A0065008biological_processregulation of biological quality
A0070175biological_processpositive regulation of enamel mineralization
A0071320biological_processcellular response to cAMP
A0071889molecular_function14-3-3 protein binding
A0097186biological_processamelogenesis
A0098660biological_processinorganic ion transmembrane transport
A0106138molecular_functionSec61 translocon complex binding
A0140359molecular_functionABC-type transporter activity
A1902476biological_processchloride transmembrane transport
A1902943biological_processpositive regulation of voltage-gated chloride channel activity
A1904322biological_processcellular response to forskolin
G0000166molecular_functionnucleotide binding
G0000287molecular_functionmagnesium ion binding
G0001669cellular_componentacrosomal vesicle
G0001707biological_processmesoderm formation
G0001843biological_processneural tube closure
G0004672molecular_functionprotein kinase activity
G0004674molecular_functionprotein serine/threonine kinase activity
G0004691molecular_functioncAMP-dependent protein kinase activity
G0004712molecular_functionprotein serine/threonine/tyrosine kinase activity
G0005515molecular_functionprotein binding
G0005524molecular_functionATP binding
G0005634cellular_componentnucleus
G0005737cellular_componentcytoplasm
G0005739cellular_componentmitochondrion
G0005813cellular_componentcentrosome
G0005829cellular_componentcytosol
G0005886cellular_componentplasma membrane
G0005930cellular_componentaxoneme
G0005952cellular_componentcAMP-dependent protein kinase complex
G0006397biological_processmRNA processing
G0006468biological_processprotein phosphorylation
G0006611biological_processprotein export from nucleus
G0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
G0007193biological_processadenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
G0016020cellular_componentmembrane
G0016301molecular_functionkinase activity
G0016607cellular_componentnuclear speck
G0016740molecular_functiontransferase activity
G0018105biological_processpeptidyl-serine phosphorylation
G0019901molecular_functionprotein kinase binding
G0019904molecular_functionprotein domain specific binding
G0030007biological_processintracellular potassium ion homeostasis
G0030145molecular_functionmanganese ion binding
G0031594cellular_componentneuromuscular junction
G0031625molecular_functionubiquitin protein ligase binding
G0032024biological_processpositive regulation of insulin secretion
G0034237molecular_functionprotein kinase A regulatory subunit binding
G0034605biological_processcellular response to heat
G0036126cellular_componentsperm flagellum
G0044853cellular_componentplasma membrane raft
G0045542biological_processpositive regulation of cholesterol biosynthetic process
G0045667biological_processregulation of osteoblast differentiation
G0045722biological_processpositive regulation of gluconeogenesis
G0045879biological_processnegative regulation of smoothened signaling pathway
G0046827biological_processpositive regulation of protein export from nucleus
G0048240biological_processsperm capacitation
G0048471cellular_componentperinuclear region of cytoplasm
G0050766biological_processpositive regulation of phagocytosis
G0050804biological_processmodulation of chemical synaptic transmission
G0051726biological_processregulation of cell cycle
G0061136biological_processregulation of proteasomal protein catabolic process
G0070417biological_processcellular response to cold
G0070613biological_processregulation of protein processing
G0071333biological_processcellular response to glucose stimulus
G0071374biological_processcellular response to parathyroid hormone stimulus
G0071377biological_processcellular response to glucagon stimulus
G0097546cellular_componentciliary base
G0098794cellular_componentpostsynapse
G0098978cellular_componentglutamatergic synapse
G0099170biological_processpostsynaptic modulation of chemical synaptic transmission
G0106310molecular_functionprotein serine kinase activity
G1904262biological_processnegative regulation of TORC1 signaling
G1904539biological_processnegative regulation of glycolytic process through fructose-6-phosphate
G1990044biological_processprotein localization to lipid droplet
G2000810biological_processregulation of bicellular tight junction assembly
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGSFGRVMlVkhmetgnh..........YAMK
ChainResidueDetails
GLEU50-LYS73
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LiYrDLKpeNLLI
ChainResidueDetails
GLEU163-ILE175
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
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues61
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues212
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues20
DetailsTransmembrane: {"description":"Discontinuously helical; Name=8","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=9","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=10","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=11","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=12","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Structure of human cystic fibrosis transmembrane conductance regulator (CFTR).","authors":["Liu F.","Zhang Z.","Chen J."]}}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues284
DetailsDomain: {"description":"ABC transmembrane type-1 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues233
DetailsDomain: {"description":"ABC transporter 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15528182","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20150177","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XMI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XMJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BBO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BBS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BBT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PZE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PZF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PZG","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15528182","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XMI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XMJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BBO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BBS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BBT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15528182","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XMI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BBO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BBS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PDB","id":"3GD7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"},{"source":"PDB","id":"3GD7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PKA","evidences":[{"source":"PubMed","id":"1377674","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25330774","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9385646","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22119790","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues2
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"22119790","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"6286662","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues9
DetailsBinding site: {}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P17612","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI31
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P05132","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI32
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by PDPK1","evidences":[{"source":"PubMed","id":"6262777","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 757
ChainResidueDetails

238895

PDB entries from 2025-07-16

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