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8VVC

Cryo-EM structure of human ABC transporter (hABCC1) with nucleotide-binding domain 2

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005524molecular_functionATP binding
A0005886cellular_componentplasma membrane
A0006691biological_processleukotriene metabolic process
A0006805biological_processxenobiotic metabolic process
A0006869biological_processlipid transport
A0008559molecular_functionABC-type xenobiotic transporter activity
A0009410biological_processresponse to xenobiotic stimulus
A0009925cellular_componentbasal plasma membrane
A0015420molecular_functionABC-type vitamin B12 transporter activity
A0015431molecular_functionABC-type glutathione S-conjugate transporter activity
A0015562molecular_functionefflux transmembrane transporter activity
A0015889biological_processcobalamin transport
A0016020cellular_componentmembrane
A0016323cellular_componentbasolateral plasma membrane
A0016324cellular_componentapical plasma membrane
A0016328cellular_componentlateral plasma membrane
A0016787molecular_functionhydrolase activity
A0016887molecular_functionATP hydrolysis activity
A0022857molecular_functiontransmembrane transporter activity
A0030054cellular_componentcell junction
A0030148biological_processsphingolipid biosynthetic process
A0034040molecular_functionATPase-coupled lipid transmembrane transporter activity
A0034599biological_processcellular response to oxidative stress
A0034634molecular_functionglutathione transmembrane transporter activity
A0034775biological_processglutathione transmembrane transport
A0042167biological_processheme catabolic process
A0042626molecular_functionATPase-coupled transmembrane transporter activity
A0042908biological_processxenobiotic transport
A0042910molecular_functionxenobiotic transmembrane transporter activity
A0045332biological_processphospholipid translocation
A0046624molecular_functionsphingolipid transporter activity
A0046942biological_processcarboxylic acid transport
A0046943molecular_functioncarboxylic acid transmembrane transporter activity
A0050729biological_processpositive regulation of inflammatory response
A0055085biological_processtransmembrane transport
A0060326biological_processcell chemotaxis
A0070062cellular_componentextracellular exosome
A0070633biological_processtransepithelial transport
A0070729biological_processcyclic nucleotide transport
A0071716biological_processleukotriene transport
A0099039biological_processsphingolipid translocation
A0140115biological_processexport across plasma membrane
A0140359molecular_functionABC-type transporter activity
A0150104biological_processtransport across blood-brain barrier
A1904646biological_processcellular response to amyloid-beta
A1905039biological_processcarboxylic acid transmembrane transport
A1990962biological_processxenobiotic transport across blood-brain barrier
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues26
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGCGKSSLLSaLlaemdkvegh........VAIK
ChainResidueDetails
AVAL680-LYS705

site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGQKQRVSLARAV
ChainResidueDetails
ALEU768-VAL782
ALEU1430-LEU1444

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues139
DetailsTopological domain: {"description":"Extracellular"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=1"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues541
DetailsTopological domain: {"description":"Cytoplasmic"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=2"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=3"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=4"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=5"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=6"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=7"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=8"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=9"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=10"}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=11"}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=13"}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=14"}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=15"}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=16"}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=17"}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues283
DetailsDomain: {"description":"ABC transmembrane type-1 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues224
DetailsDomain: {"description":"ABC transporter 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues281
DetailsDomain: {"description":"ABC transmembrane type-1 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues234
DetailsDomain: {"description":"ABC transporter 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues9
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI24
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI25
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"O35379","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI26
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"9295302","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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