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6S7P

Nucleotide bound ABCB4

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005548molecular_functionphospholipid transporter activity
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005925cellular_componentfocal adhesion
A0006629biological_processlipid metabolic process
A0006869biological_processlipid transport
A0016020cellular_componentmembrane
A0016324cellular_componentapical plasma membrane
A0016887molecular_functionATP hydrolysis activity
A0030136cellular_componentclathrin-coated vesicle
A0031410cellular_componentcytoplasmic vesicle
A0032376biological_processpositive regulation of cholesterol transport
A0032782biological_processbile acid secretion
A0042626molecular_functionATPase-coupled transmembrane transporter activity
A0045121cellular_componentmembrane raft
A0045332biological_processphospholipid translocation
A0046581cellular_componentintercellular canaliculus
A0055085biological_processtransmembrane transport
A0055088biological_processlipid homeostasis
A0061092biological_processpositive regulation of phospholipid translocation
A0070062cellular_componentextracellular exosome
A0090554molecular_functionphosphatidylcholine floppase activity
A0099038molecular_functionceramide floppase activity
A0099040biological_processceramide translocation
A0140326molecular_functionATPase-coupled intramembrane lipid transporter activity
A0140359molecular_functionABC-type transporter activity
A1901557biological_processresponse to fenofibrate
A1903413biological_processcellular response to bile acid
A2001140biological_processpositive regulation of phospholipid transport
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue ATP A 1301
ChainResidue
ATYR403
ATHR437
AGLN477
AASP557
APHE1156
ATHR1173
AGLN1174
ASER1176
AGLY1177
AGLN1179
ASER405
AARG406
AILE411
AGLY432
ACYS433
AGLY434
ALYS435
ASER436

site_idAC2
Number of Residues17
Detailsbinding site for residue ATP A 1302
ChainResidue
AALA531
ASER534
AGLY535
AGLY536
AGLN537
ATYR1043
ATHR1045
AARG1046
ASER1071
AGLY1072
ACYS1073
AGLY1074
ALYS1075
ASER1076
ATHR1077
AGLN1117
AMG1303

site_idAC3
Number of Residues3
Detailsbinding site for residue MG A 1303
ChainResidue
ASER1076
AGLN1117
AATP1302

site_idAC4
Number of Residues1
Detailsbinding site for residue CLR A 1304
ChainResidue
ASER755

site_idAC5
Number of Residues3
Detailsbinding site for residue CLR A 1305
ChainResidue
ASER121
APHE950
AARG957

site_idAC6
Number of Residues1
Detailsbinding site for residue CLR A 1306
ChainResidue
AALA720

site_idAC7
Number of Residues1
Detailsbinding site for residue CLR A 1307
ChainResidue
APHE137

site_idAC8
Number of Residues3
Detailsbinding site for residue CLR A 1309
ChainResidue
AGLN52
ALEU59
APHE137

site_idAC9
Number of Residues3
Detailsbinding site for residue CLR A 1310
ChainResidue
AVAL863
AARG957
ATYR961

site_idAD1
Number of Residues4
Detailsbinding site for residue CLR A 1311
ChainResidue
AALA66
ALEU73
AILE76
AALA130

Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGQKQRIAIARAL
ChainResidueDetails
ALEU533-LEU547
ALEU1175-LEU1189

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues623
DetailsTOPO_DOM: Cytoplasmic => ECO:0000250
ChainResidueDetails
AMET1-ASP50
ALEU140-ILE188
ASER239-SER296
AASP355-PHE711
AGLY777-ARG831
AGLU874-LYS933

site_idSWS_FT_FI2
Number of Residues247
DetailsTRANSMEM: Helical => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
ATRP51-LEU73
ATRP854-VAL873
AALA934-PHE956
AVAL973-ALA994
ATYR119-THR139
AGLY189-PHE210
ALEU218-LEU238
AALA297-TYR318
AALA333-ILE354
AVAL712-PHE732
ALEU756-PHE776
ALEU832-TYR852

site_idSWS_FT_FI3
Number of Residues101
DetailsTOPO_DOM: Extracellular => ECO:0000250
ChainResidueDetails
AMET74-TYR118
AILE211-THR217
AGLY319-ASN332
ASER733-SER755
AGLY853
AARG957-ASP972

site_idSWS_FT_FI4
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:31873305, ECO:0007744|PDB:6S7P
ChainResidueDetails
AARG406
AGLN477
AGLY536
AARG1046
ACYS1124

site_idSWS_FT_FI5
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00434, ECO:0000269|PubMed:31873305, ECO:0007744|PDB:6S7P
ChainResidueDetails
AGLY432
ASER1071
AALA1184

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P21440
ChainResidueDetails
ASER27

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:24723470
ChainResidueDetails
ATHR34

site_idSWS_FT_FI8
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN91
AASN97

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PDB entries from 2024-07-24

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