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9N1Y

BSEP E297G Apo Structure in GDN

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005768cellular_componentendosome
A0005886cellular_componentplasma membrane
A0006631biological_processfatty acid metabolic process
A0006699biological_processbile acid biosynthetic process
A0006805biological_processxenobiotic metabolic process
A0006855biological_processxenobiotic transmembrane transport
A0006869biological_processlipid transport
A0008206biological_processbile acid metabolic process
A0008559molecular_functionABC-type xenobiotic transporter activity
A0009986cellular_componentcell surface
A0015125molecular_functionbile acid transmembrane transporter activity
A0015126molecular_functioncanalicular bile acid transmembrane transporter activity
A0015432molecular_functionABC-type bile acid transporter activity
A0015721biological_processbile acid and bile salt transport
A0015722biological_processcanalicular bile acid transport
A0016020cellular_componentmembrane
A0016323cellular_componentbasolateral plasma membrane
A0016324cellular_componentapical plasma membrane
A0016567biological_processprotein ubiquitination
A0031998biological_processregulation of fatty acid beta-oxidation
A0042632biological_processcholesterol homeostasis
A0045177cellular_componentapical part of cell
A0046581cellular_componentintercellular canaliculus
A0046618biological_processxenobiotic export from cell
A0046691cellular_componentintracellular canaliculus
A0055037cellular_componentrecycling endosome
A0055038cellular_componentrecycling endosome membrane
A0055085biological_processtransmembrane transport
A0055088biological_processlipid homeostasis
A0055091biological_processphospholipid homeostasis
A0070062cellular_componentextracellular exosome
A0120189biological_processpositive regulation of bile acid secretion
A1904251biological_processregulation of bile acid metabolic process
Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. MSGGQKQRVAIARAL
ChainResidueDetails
AMET559-LEU573

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues240
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues105
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues223
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues323
DetailsDomain: {"description":"ABC transmembrane type-1 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues236
DetailsDomain: {"description":"ABC transporter 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues288
DetailsDomain: {"description":"ABC transmembrane type-1 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues3
DetailsRegion: {"description":"Mediates internalization from the plasma membrane","evidences":[{"source":"PubMed","id":"22262466","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9QY30","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"O70127","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"17082223","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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