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7NIV

Nanodisc reconstituted human ABCB4 in complex with 4B1-Fab and QA2-Fab (phosphatidylcholine-bound, occluded conformation)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005548molecular_functionphospholipid transporter activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
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 PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGQKQRIAIARAL
ChainResidueDetails
ALEU533-LEU547
ALEU1175-LEU1189

site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YICNVNH
ChainResidueDetails
CTYR214-HIS220
ETYR207-HIS213
DTYR193-HIS199
BTYR193-HIS199

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues247
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues218
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues57
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues288
DetailsDomain: {"description":"ABC transmembrane type-1 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"31873305","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6S7P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues13
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"31873305","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6S7P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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