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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9MXL

Complex of the phosphorylated human cystic fibrosis transmembrane conductance regulator (CFTR) with (R)-BPO-27 and ATP/Mg

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
B0000166molecular_functionnucleotide binding
B0005254molecular_functionchloride channel activity
B0005260molecular_functionintracellularly ATP-gated chloride channel activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005765cellular_componentlysosomal membrane
B0005769cellular_componentearly endosome
B0005789cellular_componentendoplasmic reticulum membrane
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0006821biological_processchloride transport
B0006833biological_processwater transport
B0009986cellular_componentcell surface
B0010008cellular_componentendosome membrane
B0015106molecular_functionbicarbonate transmembrane transporter activity
B0015108molecular_functionchloride transmembrane transporter activity
B0015701biological_processbicarbonate transport
B0016020cellular_componentmembrane
B0016323cellular_componentbasolateral plasma membrane
B0016324cellular_componentapical plasma membrane
B0016853molecular_functionisomerase activity
B0016887molecular_functionATP hydrolysis activity
B0017081molecular_functionchloride channel regulator activity
B0019869molecular_functionchloride channel inhibitor activity
B0019899molecular_functionenzyme binding
B0030165molecular_functionPDZ domain binding
B0030660cellular_componentGolgi-associated vesicle membrane
B0030669cellular_componentclathrin-coated endocytic vesicle membrane
B0031901cellular_componentearly endosome membrane
B0032991cellular_componentprotein-containing complex
B0034220biological_processmonoatomic ion transmembrane transport
B0034707cellular_componentchloride channel complex
B0034976biological_processresponse to endoplasmic reticulum stress
B0035377biological_processtransepithelial water transport
B0042626molecular_functionATPase-coupled transmembrane transporter activity
B0042802molecular_functionidentical protein binding
B0048240biological_processsperm capacitation
B0050891biological_processmulticellular organismal-level water homeostasis
B0051087molecular_functionprotein-folding chaperone binding
B0051454biological_processintracellular pH elevation
B0055037cellular_componentrecycling endosome
B0055038cellular_componentrecycling endosome membrane
B0055085biological_processtransmembrane transport
B0060081biological_processmembrane hyperpolarization
B0070175biological_processpositive regulation of enamel mineralization
B0071320biological_processcellular response to cAMP
B0071889molecular_function14-3-3 protein binding
B0097186biological_processamelogenesis
B0106138molecular_functionSec61 translocon complex binding
B0140359molecular_functionABC-type transporter activity
B1902476biological_processchloride transmembrane transport
B1904322biological_processcellular response to forskolin
Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGQRARISLARAV
ChainResidueDetails
BLEU548-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","evidences":[{"source":"PubMed","id":"22119790","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues2
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"22119790","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

248942

PDB entries from 2026-02-11

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