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5C65

Structure of the human glucose transporter GLUT3 / SLC2A3

Functional Information from GO Data
ChainGOidnamespacecontents
A0005353molecular_functionfructose transmembrane transporter activity
A0005354molecular_functiongalactose transmembrane transporter activity
A0005515molecular_functionprotein binding
A0005536molecular_functionD-glucose binding
A0005886cellular_componentplasma membrane
A0005975biological_processcarbohydrate metabolic process
A0015755biological_processfructose transmembrane transport
A0015757biological_processgalactose transmembrane transport
A0016020cellular_componentmembrane
A0016235cellular_componentaggresome
A0019852biological_processL-ascorbic acid metabolic process
A0022857molecular_functiontransmembrane transporter activity
A0030667cellular_componentsecretory granule membrane
A0033300molecular_functiondehydroascorbic acid transmembrane transporter activity
A0035579cellular_componentspecific granule membrane
A0042995cellular_componentcell projection
A0043204cellular_componentperikaryon
A0046323biological_processD-glucose import
A0055056molecular_functionD-glucose transmembrane transporter activity
A0055085biological_processtransmembrane transport
A0070062cellular_componentextracellular exosome
A0070821cellular_componenttertiary granule membrane
A0070837biological_processdehydroascorbic acid transport
A0098708biological_processD-glucose import across plasma membrane
A0101003cellular_componentficolin-1-rich granule membrane
A0150104biological_processtransport across blood-brain barrier
A1904659biological_processD-glucose transmembrane transport
B0005353molecular_functionfructose transmembrane transporter activity
B0005354molecular_functiongalactose transmembrane transporter activity
B0005515molecular_functionprotein binding
B0005536molecular_functionD-glucose binding
B0005886cellular_componentplasma membrane
B0005975biological_processcarbohydrate metabolic process
B0015755biological_processfructose transmembrane transport
B0015757biological_processgalactose transmembrane transport
B0016020cellular_componentmembrane
B0016235cellular_componentaggresome
B0019852biological_processL-ascorbic acid metabolic process
B0022857molecular_functiontransmembrane transporter activity
B0030667cellular_componentsecretory granule membrane
B0033300molecular_functiondehydroascorbic acid transmembrane transporter activity
B0035579cellular_componentspecific granule membrane
B0042995cellular_componentcell projection
B0043204cellular_componentperikaryon
B0046323biological_processD-glucose import
B0055056molecular_functionD-glucose transmembrane transporter activity
B0055085biological_processtransmembrane transport
B0070062cellular_componentextracellular exosome
B0070821cellular_componenttertiary granule membrane
B0070837biological_processdehydroascorbic acid transport
B0098708biological_processD-glucose import across plasma membrane
B0101003cellular_componentficolin-1-rich granule membrane
B0150104biological_processtransport across blood-brain barrier
B1904659biological_processD-glucose transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue 37X A 501
ChainResidue
AARG91
APRO203
APHE204
A37X502
B37X502

site_idAC2
Number of Residues8
Detailsbinding site for residue 37X A 502
ChainResidue
A37X501
BPHE107
BSER116
BGLU118
APRO8
AALA9
APHE204
AARG228

site_idAC3
Number of Residues3
Detailsbinding site for residue 37X A 503
ChainResidue
APHE79
ASER80
A37X504

site_idAC4
Number of Residues3
Detailsbinding site for residue 37X A 504
ChainResidue
AILE96
A37X503
B37X501

site_idAC5
Number of Residues5
Detailsbinding site for residue 37X A 505
ChainResidue
AALA114
ASER116
BPRO8
BALA9
B37X501

site_idAC6
Number of Residues3
Detailsbinding site for residue 37X A 506
ChainResidue
ALEU46
AALA52
AILE121

site_idAC7
Number of Residues3
Detailsbinding site for residue Y01 A 507
ChainResidue
AILE274
ASER408
ATHR411

site_idAC8
Number of Residues7
Detailsbinding site for residue 37X B 501
ChainResidue
ALEU99
ALEU100
A37X504
A37X505
BARG91
BPRO203
BPHE204

site_idAC9
Number of Residues3
Detailsbinding site for residue 37X B 502
ChainResidue
A37X501
BLEU83
B37X503

site_idAD1
Number of Residues2
Detailsbinding site for residue 37X B 503
ChainResidue
BSER80
B37X502

site_idAD2
Number of Residues3
Detailsbinding site for residue Y01 B 504
ChainResidue
BPHE79
BVAL257
BSER408

Functional Information from PROSITE/UniProt
site_idPS00216
Number of Residues17
DetailsSUGAR_TRANSPORT_1 Sugar transport proteins signature 1. SLFLVERAGRRtlhmi.G
ChainResidueDetails
ASER322-GLY338

site_idPS00217
Number of Residues26
DetailsSUGAR_TRANSPORT_2 Sugar transport proteins signature 2. ViGLFcGLctgfvpmYigEisptalR
ChainResidueDetails
AVAL126-ARG151

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues42
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues75
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues120
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues46
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=8","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=9","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues50
DetailsTransmembrane: {"description":"Helical; Name=10","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=11","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=12","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues4
DetailsRegion: {"description":"Important for selectivity against fructose","evidences":[{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4ZW9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P32037","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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