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6HIJ

Cryo-EM structure of the human ABCG2-MZ29-Fab complex with cholesterol and PE lipids docked

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005886cellular_componentplasma membrane
A0006869biological_processlipid transport
A0008559molecular_functionABC-type xenobiotic transporter activity
A0015143molecular_functionurate transmembrane transporter activity
A0015225molecular_functionbiotin transmembrane transporter activity
A0015562molecular_functionefflux transmembrane transporter activity
A0015711biological_processorganic anion transport
A0015747biological_processurate transport
A0015878biological_processbiotin transport
A0016020cellular_componentmembrane
A0016324cellular_componentapical plasma membrane
A0016887molecular_functionATP hydrolysis activity
A0022857molecular_functiontransmembrane transporter activity
A0030148biological_processsphingolipid biosynthetic process
A0031526cellular_componentbrush border membrane
A0031966cellular_componentmitochondrial membrane
A0032217molecular_functionriboflavin transmembrane transporter activity
A0032218biological_processriboflavin transport
A0042626molecular_functionATPase-coupled transmembrane transporter activity
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0042910molecular_functionxenobiotic transmembrane transporter activity
A0045121cellular_componentmembrane raft
A0046415biological_processurate metabolic process
A0046624molecular_functionsphingolipid transporter activity
A0046983molecular_functionprotein dimerization activity
A0055085biological_processtransmembrane transport
A0070633biological_processtransepithelial transport
A0097744biological_processrenal urate salt excretion
A0098591cellular_componentexternal side of apical plasma membrane
A0140115biological_processexport across plasma membrane
A0140359molecular_functionABC-type transporter activity
A0150104biological_processtransport across blood-brain barrier
A1990748biological_processcellular detoxification
A1990961biological_processxenobiotic detoxification by transmembrane export across the plasma membrane
A1990962biological_processxenobiotic transport across blood-brain barrier
B0000166molecular_functionnucleotide binding
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005886cellular_componentplasma membrane
B0006869biological_processlipid transport
B0008559molecular_functionABC-type xenobiotic transporter activity
B0015143molecular_functionurate transmembrane transporter activity
B0015225molecular_functionbiotin transmembrane transporter activity
B0015562molecular_functionefflux transmembrane transporter activity
B0015711biological_processorganic anion transport
B0015747biological_processurate transport
B0015878biological_processbiotin transport
B0016020cellular_componentmembrane
B0016324cellular_componentapical plasma membrane
B0016887molecular_functionATP hydrolysis activity
B0022857molecular_functiontransmembrane transporter activity
B0030148biological_processsphingolipid biosynthetic process
B0031526cellular_componentbrush border membrane
B0031966cellular_componentmitochondrial membrane
B0032217molecular_functionriboflavin transmembrane transporter activity
B0032218biological_processriboflavin transport
B0042626molecular_functionATPase-coupled transmembrane transporter activity
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0042910molecular_functionxenobiotic transmembrane transporter activity
B0045121cellular_componentmembrane raft
B0046415biological_processurate metabolic process
B0046624molecular_functionsphingolipid transporter activity
B0046983molecular_functionprotein dimerization activity
B0055085biological_processtransmembrane transport
B0070633biological_processtransepithelial transport
B0097744biological_processrenal urate salt excretion
B0098591cellular_componentexternal side of apical plasma membrane
B0140115biological_processexport across plasma membrane
B0140359molecular_functionABC-type transporter activity
B0150104biological_processtransport across blood-brain barrier
B1990748biological_processcellular detoxification
B1990961biological_processxenobiotic detoxification by transmembrane export across the plasma membrane
B1990962biological_processxenobiotic transport across blood-brain barrier
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue PEE A 701
ChainResidue
AGLN393
AILE396
AVAL401
AVAL404
BPHE547
BCLR702

site_idAC2
Number of Residues3
Detailsbinding site for residue CLR A 702
ChainResidue
APHE571
ATYR576
ACYS635

site_idAC3
Number of Residues7
Detailsbinding site for residue CLR A 703
ChainResidue
APHE547
AMET548
APHE551
ALEU568
APHE640
ALYS647
BPEE709

site_idAC4
Number of Residues4
Detailsbinding site for residue CLR A 704
ChainResidue
ASER467
ATHR642
ATYR645
APEE709

site_idAC5
Number of Residues3
Detailsbinding site for residue CLR A 705
ChainResidue
AMET510
AMET514
ATRP627

site_idAC6
Number of Residues5
Detailsbinding site for residue CLR A 706
ChainResidue
AARG378
ASER381
ALEU475
AMET483
ALEU484

site_idAC7
Number of Residues1
Detailsbinding site for residue PEE A 707
ChainResidue
APEE708

site_idAC8
Number of Residues3
Detailsbinding site for residue PEE A 708
ChainResidue
ATRP624
ATRP627
APEE707

site_idAC9
Number of Residues2
Detailsbinding site for residue PEE A 709
ChainResidue
AARG465
ACLR704

site_idAD1
Number of Residues15
Detailsbinding site for residue BWQ A 710
ChainResidue
AALA397
AVAL401
ALEU405
APHE431
APHE432
ATHR435
AASN436
APHE439
BLEU539
BTHR542
BILE543
BVAL546
BMET549
BLEU555
BBWQ710

site_idAD2
Number of Residues3
Detailsbinding site for residue CLR B 701
ChainResidue
BPHE571
BTYR576
BCYS635

site_idAD3
Number of Residues7
Detailsbinding site for residue CLR B 702
ChainResidue
APEE701
BPHE547
BMET548
BPHE551
BLEU568
BPHE640
BLYS647

site_idAD4
Number of Residues3
Detailsbinding site for residue CLR B 703
ChainResidue
BSER467
BTYR645
BPEE708

site_idAD5
Number of Residues3
Detailsbinding site for residue CLR B 704
ChainResidue
BMET510
BMET514
BTRP627

site_idAD6
Number of Residues1
Detailsbinding site for residue PEE B 707
ChainResidue
BTRP624

site_idAD7
Number of Residues3
Detailsbinding site for residue PEE B 708
ChainResidue
BPHE373
BARG465
BCLR703

site_idAD8
Number of Residues4
Detailsbinding site for residue PEE B 709
ChainResidue
APHE547
ACLR703
BGLN393
BILE396

site_idAD9
Number of Residues16
Detailsbinding site for residue BWQ B 710
ChainResidue
ALEU539
ATHR542
AILE543
AVAL546
AMET549
ALEU555
ABWQ710
BALA397
BVAL401
BLEU405
BPHE431
BPHE432
BTHR435
BASN436
BPHE439
BSER440

site_idAE1
Number of Residues9
Detailsbinding site for Di-peptide CLR B 705 and LEU B 484
ChainResidue
BSER381
BLEU475
BPRO480
BARG482
BMET483
BPRO485
BSER486
BILE487
BILE488

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

site_idSWS_FT_FI2
Number of Residues182
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues68
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues524
DetailsDomain: {"description":"ABC transmembrane type-2"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"30405239","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6HBU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6HZM","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"30405239","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6HBU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6HZM","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsSite: {"description":"Not glycosylated","evidences":[{"source":"PubMed","id":"15807535","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15807535","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28554189","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5NJ3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5NJG","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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