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5W81

Phosphorylated, ATP-bound structure of zebrafish cystic fibrosis transmembrane conductance regulator (CFTR)

Functional Information from GO Data
ChainGOidnamespacecontents
A0002679biological_processrespiratory burst involved in defense response
A0005254molecular_functionchloride channel activity
A0005260molecular_functionintracellularly ATP-gated chloride channel activity
A0005524molecular_functionATP binding
A0005768cellular_componentendosome
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0006821biological_processchloride transport
A0007507biological_processheart development
A0008354biological_processgerm cell migration
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
A0030217biological_processT cell differentiation
A0031016biological_processpancreas development
A0031901cellular_componentearly endosome membrane
A0034220biological_processmonoatomic ion transmembrane transport
A0034707cellular_componentchloride channel complex
A0035162biological_processembryonic hemopoiesis
A0035377biological_processtransepithelial water transport
A0042626molecular_functionATPase-coupled transmembrane transporter activity
A0042742biological_processdefense response to bacterium
A0045087biological_processinnate immune response
A0050891biological_processmulticellular organismal-level water homeostasis
A0055038cellular_componentrecycling endosome membrane
A0055085biological_processtransmembrane transport
A0060063biological_processSpemann organizer formation at the embryonic shield
A0070121biological_processKupffer's vesicle development
A0090022biological_processregulation of neutrophil chemotaxis
A0097535biological_processlymphoid lineage cell migration into thymus
A0140359molecular_functionABC-type transporter activity
A1902476biological_processchloride transmembrane transport
A1904322biological_processcellular response to forskolin
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue ATP A 1501
ChainResidue
ATRP402
AASN1349
AMG1503
AMET459
AGLY460
AGLY462
ALYS463
ASER464
ASER465
AGLN492
ATYR1345

site_idAC2
Number of Residues15
Detailsbinding site for residue ATP A 1502
ChainResidue
ALEU545
AASN546
ASER548
AGLY550
AGLN551
ATYR1220
ATHR1247
AGLY1248
AGLY1250
ALYS1251
ASER1252
ASER1253
AGLN1292
AGLN1372
AMG1504

site_idAC3
Number of Residues3
Detailsbinding site for residue MG A 1503
ChainResidue
ASER464
AGLN492
AATP1501

site_idAC4
Number of Residues3
Detailsbinding site for residue MG A 1504
ChainResidue
ASER1252
AGLN1292
AATP1502

Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGQKARVALARAV
ChainResidueDetails
ALEU547-VAL561

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1101
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:27912062
ChainResidueDetails
AMET1-TYR78
AGLY150-SER195
AGLY246-LYS299
AASP364-SER856
AHIS947-PRO996
AARG1043-THR1103
AALA1160-LEU1485

site_idSWS_FT_FI2
Number of Residues20
DetailsTRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:27912062
ChainResidueDetails
AILE79-GLN99

site_idSWS_FT_FI3
Number of Residues109
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:27912062
ChainResidueDetails
APRO100-PHE123
ATRP217-SER224
AALA321-THR340
AGLY878-LEU924
AARG1020-PRO1021
AILE1125-GLY1138

site_idSWS_FT_FI4
Number of Residues25
DetailsTRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:27912062
ChainResidueDetails
ALEU124-LEU149

site_idSWS_FT_FI5
Number of Residues20
DetailsTRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:27912062
ChainResidueDetails
ALEU196-ILE216

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:27912062
ChainResidueDetails
APHE225-MET245

site_idSWS_FT_FI7
Number of Residues20
DetailsTRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:27912062
ChainResidueDetails
AILE300-VAL320

site_idSWS_FT_FI8
Number of Residues22
DetailsTRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:27912062
ChainResidueDetails
ALEU341-TYR363

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:27912062
ChainResidueDetails
ALEU857-ALA877

site_idSWS_FT_FI10
Number of Residues21
DetailsTRANSMEM: Discontinuously helical; Name=8 => ECO:0000269|PubMed:27912062
ChainResidueDetails
ATYR925-VAL946

site_idSWS_FT_FI11
Number of Residues22
DetailsTRANSMEM: Helical; Name=9 => ECO:0000269|PubMed:27912062
ChainResidueDetails
ALEU997-VAL1019

site_idSWS_FT_FI12
Number of Residues20
DetailsTRANSMEM: Helical; Name=10 => ECO:0000269|PubMed:27912062
ChainResidueDetails
ATYR1022-LEU1042

site_idSWS_FT_FI13
Number of Residues20
DetailsTRANSMEM: Helical; Name=11 => ECO:0000269|PubMed:27912062
ChainResidueDetails
ALEU1104-TRP1124

site_idSWS_FT_FI14
Number of Residues20
DetailsTRANSMEM: Helical; Name=12 => ECO:0000269|PubMed:27912062
ChainResidueDetails
AILE1139-ILE1159

site_idSWS_FT_FI15
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P13569
ChainResidueDetails
AGLN492
ATYR1220
ATRP402

site_idSWS_FT_FI16
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00434
ChainResidueDetails
AGLY1245
AGLY457

site_idSWS_FT_FI17
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AASN897
AASN903

221051

PDB entries from 2024-06-12

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