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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8RQ3

Cryo-em structure of the rat Multidrug resistance-associated protein 2 (rMrp2) in an autoinhibited state (nucleotide-free)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005886cellular_componentplasma membrane
A0006749biological_processglutathione metabolic process
A0006855biological_processxenobiotic transmembrane transport
A0006869biological_processlipid transport
A0006979biological_processresponse to oxidative stress
A0007507biological_processheart development
A0007565biological_processfemale pregnancy
A0008206biological_processbile acid metabolic process
A0008559molecular_functionABC-type xenobiotic transporter activity
A0009410biological_processresponse to xenobiotic stimulus
A0009636biological_processresponse to toxic substance
A0009986cellular_componentcell surface
A0010467biological_processgene expression
A0010629biological_processnegative regulation of gene expression
A0015127molecular_functionbilirubin transmembrane transporter activity
A0015431molecular_functionABC-type glutathione S-conjugate transporter activity
A0015694biological_processmercury ion transport
A0015711biological_processorganic anion transport
A0015718biological_processmonocarboxylic acid transport
A0015721biological_processbile acid and bile salt transport
A0015722biological_processcanalicular bile acid transport
A0015723biological_processbilirubin transport
A0015732biological_processprostaglandin transport
A0015779biological_processglucuronoside transport
A0016020cellular_componentmembrane
A0016071biological_processmRNA metabolic process
A0016324cellular_componentapical plasma membrane
A0016887molecular_functionATP hydrolysis activity
A0016999biological_processantibiotic metabolic process
A0019534molecular_functiontoxin transmembrane transporter activity
A0019904molecular_functionprotein domain specific binding
A0022857molecular_functiontransmembrane transporter activity
A0030001biological_processmetal ion transport
A0030644biological_processintracellular chloride ion homeostasis
A0031526cellular_componentbrush border membrane
A0031982cellular_componentvesicle
A0032355biological_processresponse to estradiol
A0032496biological_processresponse to lipopolysaccharide
A0032868biological_processresponse to insulin
A0033762biological_processresponse to glucagon
A0034635biological_processglutathione transport
A0042167biological_processheme catabolic process
A0042178biological_processxenobiotic catabolic process
A0042440biological_processpigment metabolic process
A0042626molecular_functionATPase-coupled transmembrane transporter activity
A0042908biological_processxenobiotic transport
A0042910molecular_functionxenobiotic transmembrane transporter activity
A0043491biological_processphosphatidylinositol 3-kinase/protein kinase B signal transduction
A0043627biological_processresponse to estrogen
A0046581cellular_componentintercellular canaliculus
A0046618biological_processxenobiotic export from cell
A0046685biological_processresponse to arsenic-containing substance
A0046689biological_processresponse to mercury ion
A0046691cellular_componentintracellular canaliculus
A0048545biological_processresponse to steroid hormone
A0050787biological_processdetoxification of mercury ion
A0055007biological_processcardiac muscle cell differentiation
A0055085biological_processtransmembrane transport
A0060416biological_processresponse to growth hormone
A0070327biological_processthyroid hormone transport
A0070633biological_processtransepithelial transport
A0071222biological_processcellular response to lipopolysaccharide
A0071347biological_processcellular response to interleukin-1
A0071354biological_processcellular response to interleukin-6
A0071356biological_processcellular response to tumor necrosis factor
A0071466biological_processcellular response to xenobiotic stimulus
A0071549biological_processcellular response to dexamethasone stimulus
A0071716biological_processleukotriene transport
A0072014biological_processproximal tubule development
A0072718biological_processresponse to cisplatin
A0097327biological_processresponse to antineoplastic agent
A0140359molecular_functionABC-type transporter activity
A1901086biological_processbenzylpenicillin metabolic process
A1901652biological_processresponse to peptide
A1904567biological_processresponse to wortmannin
A1990961biological_processxenobiotic detoxification by transmembrane export across the plasma membrane
A1990962biological_processxenobiotic transport across blood-brain barrier
Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGQKQRVSLARAA
ChainResidueDetails
ALEU757-ALA771
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues135
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues258
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=8","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=9","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=10","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=11","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=12","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=13","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=14","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=15","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=16","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=17","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues283
DetailsDomain: {"description":"ABC transmembrane type-1 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues224
DetailsDomain: {"description":"ABC transporter 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues285
DetailsDomain: {"description":"ABC transmembrane type-1 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues234
DetailsDomain: {"description":"ABC transporter 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues22
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues9
DetailsCompositional bias: {"description":"Low complexity","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q92887","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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