Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7SPS

Crystal structure of human glucose transporter GLUT3 bound with exofacial inhibitor SA47

Functional Information from GO Data
ChainGOidnamespacecontents
A0005353molecular_functionfructose transmembrane transporter activity
A0005354molecular_functiongalactose transmembrane transporter activity
A0005355molecular_functionglucose transmembrane transporter activity
A0005515molecular_functionprotein binding
A0005536molecular_functionglucose 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_processglucose import
A0055056molecular_functionD-glucose transmembrane transporter activity
A0055085biological_processtransmembrane transport
A0070062cellular_componentextracellular exosome
A0070821cellular_componenttertiary granule membrane
A0070837biological_processdehydroascorbic acid transport
A0071702biological_processorganic substance transport
A0098708biological_processglucose import across plasma membrane
A0101003cellular_componentficolin-1-rich granule membrane
A0150104biological_processtransport across blood-brain barrier
A1904659biological_processglucose transmembrane transport
B0005353molecular_functionfructose transmembrane transporter activity
B0005354molecular_functiongalactose transmembrane transporter activity
B0005355molecular_functionglucose transmembrane transporter activity
B0005515molecular_functionprotein binding
B0005536molecular_functionglucose 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_processglucose import
B0055056molecular_functionD-glucose transmembrane transporter activity
B0055085biological_processtransmembrane transport
B0070062cellular_componentextracellular exosome
B0070821cellular_componenttertiary granule membrane
B0070837biological_processdehydroascorbic acid transport
B0071702biological_processorganic substance transport
B0098708biological_processglucose import across plasma membrane
B0101003cellular_componentficolin-1-rich granule membrane
B0150104biological_processtransport across blood-brain barrier
B1904659biological_processglucose transmembrane transport
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 Residues292
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
AMET1-LEU10
AASN86-ARG90
AGLY143-ALA153
ACYS205-PRO269
AVAL326-ARG331
AALA390-PRO399
APRO451-VAL496
BMET1-LEU10
BASN86-ARG90
BGLY143-ALA153
BCYS205-PRO269
BVAL326-ARG331
BALA390-PRO399
BPRO451-VAL496

site_idSWS_FT_FI2
Number of Residues42
DetailsTRANSMEM: Helical; Name=1 => ECO:0000255, ECO:0000269|PubMed:26176916
ChainResidueDetails
AILE11-ASN32
BILE11-ASN32

site_idSWS_FT_FI3
Number of Residues152
DetailsTOPO_DOM: Extracellular => ECO:0000305
ChainResidueDetails
AALA33-SER64
ALYS112-GLU118
AGLU175-LEU183
ATYR291-PRO304
ALEU353-SER363
APRO421-ALA429
BALA33-SER64
BLYS112-GLU118
BGLU175-LEU183
BTYR291-PRO304
BLEU353-SER363
BPRO421-ALA429

site_idSWS_FT_FI4
Number of Residues40
DetailsTRANSMEM: Helical; Name=2 => ECO:0000255, ECO:0000269|PubMed:26176916
ChainResidueDetails
ALEU65-VAL85
BLEU65-VAL85

site_idSWS_FT_FI5
Number of Residues40
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255, ECO:0000269|PubMed:26176916
ChainResidueDetails
AARG91-CYS111
BARG91-CYS111

site_idSWS_FT_FI6
Number of Residues46
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255, ECO:0000269|PubMed:26176916
ChainResidueDetails
AMET119-ILE142
BMET119-ILE142

site_idSWS_FT_FI7
Number of Residues40
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255, ECO:0000269|PubMed:26176916
ChainResidueDetails
APHE154-LEU174
BPHE154-LEU174

site_idSWS_FT_FI8
Number of Residues40
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255, ECO:0000269|PubMed:26176916
ChainResidueDetails
ATRP184-PHE204
BTRP184-PHE204

site_idSWS_FT_FI9
Number of Residues40
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255, ECO:0000269|PubMed:26176916
ChainResidueDetails
AILE270-TYR290
BILE270-TYR290

site_idSWS_FT_FI10
Number of Residues40
DetailsTRANSMEM: Helical; Name=8 => ECO:0000255, ECO:0000269|PubMed:26176916
ChainResidueDetails
AILE305-LEU325
BILE305-LEU325

site_idSWS_FT_FI11
Number of Residues40
DetailsTRANSMEM: Helical; Name=9 => ECO:0000255, ECO:0000269|PubMed:26176916
ChainResidueDetails
AARG332-SER352
BARG332-SER352

site_idSWS_FT_FI12
Number of Residues50
DetailsTRANSMEM: Helical; Name=10 => ECO:0000255, ECO:0000269|PubMed:26176916
ChainResidueDetails
APHE364-VAL389
BPHE364-VAL389

site_idSWS_FT_FI13
Number of Residues40
DetailsTRANSMEM: Helical; Name=11 => ECO:0000255, ECO:0000269|PubMed:26176916
ChainResidueDetails
AALA400-PHE420
BALA400-PHE420

site_idSWS_FT_FI14
Number of Residues40
DetailsTRANSMEM: Helical; Name=12 => ECO:0000255, ECO:0000269|PubMed:26176916
ChainResidueDetails
ATYR430-VAL450
BTYR430-VAL450

site_idSWS_FT_FI15
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:26176916, ECO:0007744|PDB:4ZW9
ChainResidueDetails
AGLN159
BGLU378
BTRP386
AGLN280
AASN286
AASN315
AGLU378
ATRP386
BGLN159
BGLN280
BASN286
BASN315

site_idSWS_FT_FI16
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P32037
ChainResidueDetails
ATHR232
BTHR232

site_idSWS_FT_FI17
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P32037
ChainResidueDetails
ASER475
BSER475

site_idSWS_FT_FI18
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q07647
ChainResidueDetails
ASER485
BSER485

site_idSWS_FT_FI19
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q07647
ChainResidueDetails
ATHR492
BTHR492

site_idSWS_FT_FI20
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
ATHR43
BTHR43

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon