5C65
Structure of the human glucose transporter GLUT3 / SLC2A3
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005353 | molecular_function | fructose transmembrane transporter activity |
| A | 0005354 | molecular_function | galactose transmembrane transporter activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005536 | molecular_function | D-glucose binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0015755 | biological_process | fructose transmembrane transport |
| A | 0015757 | biological_process | galactose transmembrane transport |
| A | 0016020 | cellular_component | membrane |
| A | 0019852 | biological_process | L-ascorbic acid metabolic process |
| A | 0022857 | molecular_function | transmembrane transporter activity |
| A | 0030667 | cellular_component | secretory granule membrane |
| A | 0033300 | molecular_function | dehydroascorbic acid transmembrane transporter activity |
| A | 0035579 | cellular_component | specific granule membrane |
| A | 0042995 | cellular_component | cell projection |
| A | 0043204 | cellular_component | perikaryon |
| A | 0055056 | molecular_function | D-glucose transmembrane transporter activity |
| A | 0055085 | biological_process | transmembrane transport |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0070821 | cellular_component | tertiary granule membrane |
| A | 0070837 | biological_process | dehydroascorbic acid transport |
| A | 0098708 | biological_process | D-glucose import across plasma membrane |
| A | 0101003 | cellular_component | ficolin-1-rich granule membrane |
| A | 0150104 | biological_process | transport across blood-brain barrier |
| A | 1904659 | biological_process | D-glucose transmembrane transport |
| B | 0005353 | molecular_function | fructose transmembrane transporter activity |
| B | 0005354 | molecular_function | galactose transmembrane transporter activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005536 | molecular_function | D-glucose binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0015755 | biological_process | fructose transmembrane transport |
| B | 0015757 | biological_process | galactose transmembrane transport |
| B | 0016020 | cellular_component | membrane |
| B | 0019852 | biological_process | L-ascorbic acid metabolic process |
| B | 0022857 | molecular_function | transmembrane transporter activity |
| B | 0030667 | cellular_component | secretory granule membrane |
| B | 0033300 | molecular_function | dehydroascorbic acid transmembrane transporter activity |
| B | 0035579 | cellular_component | specific granule membrane |
| B | 0042995 | cellular_component | cell projection |
| B | 0043204 | cellular_component | perikaryon |
| B | 0055056 | molecular_function | D-glucose transmembrane transporter activity |
| B | 0055085 | biological_process | transmembrane transport |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0070821 | cellular_component | tertiary granule membrane |
| B | 0070837 | biological_process | dehydroascorbic acid transport |
| B | 0098708 | biological_process | D-glucose import across plasma membrane |
| B | 0101003 | cellular_component | ficolin-1-rich granule membrane |
| B | 0150104 | biological_process | transport across blood-brain barrier |
| B | 1904659 | biological_process | D-glucose transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue 37X A 501 |
| Chain | Residue |
| A | ARG91 |
| A | PRO203 |
| A | PHE204 |
| A | 37X502 |
| B | 37X502 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue 37X A 502 |
| Chain | Residue |
| A | 37X501 |
| B | PHE107 |
| B | SER116 |
| B | GLU118 |
| A | PRO8 |
| A | ALA9 |
| A | PHE204 |
| A | ARG228 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue 37X A 503 |
| Chain | Residue |
| A | PHE79 |
| A | SER80 |
| A | 37X504 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue 37X A 504 |
| Chain | Residue |
| A | ILE96 |
| A | 37X503 |
| B | 37X501 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue 37X A 505 |
| Chain | Residue |
| A | ALA114 |
| A | SER116 |
| B | PRO8 |
| B | ALA9 |
| B | 37X501 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue 37X A 506 |
| Chain | Residue |
| A | LEU46 |
| A | ALA52 |
| A | ILE121 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue Y01 A 507 |
| Chain | Residue |
| A | ILE274 |
| A | SER408 |
| A | THR411 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue 37X B 501 |
| Chain | Residue |
| A | LEU99 |
| A | LEU100 |
| A | 37X504 |
| A | 37X505 |
| B | ARG91 |
| B | PRO203 |
| B | PHE204 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue 37X B 502 |
| Chain | Residue |
| A | 37X501 |
| B | LEU83 |
| B | 37X503 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue 37X B 503 |
| Chain | Residue |
| B | SER80 |
| B | 37X502 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue Y01 B 504 |
| Chain | Residue |
| B | PHE79 |
| B | VAL257 |
| B | SER408 |
Functional Information from PROSITE/UniProt
| site_id | PS00216 |
| Number of Residues | 17 |
| Details | SUGAR_TRANSPORT_1 Sugar transport proteins signature 1. SLFLVERAGRRtlhmi.G |
| Chain | Residue | Details |
| A | SER322-GLY338 |
| site_id | PS00217 |
| Number of Residues | 26 |
| Details | SUGAR_TRANSPORT_2 Sugar transport proteins signature 2. ViGLFcGLctgfvpmYigEisptalR |
| Chain | Residue | Details |
| A | VAL126-ARG151 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 42 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 75 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 120 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 46 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=8","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=9","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 50 |
| Details | Transmembrane: {"description":"Helical; Name=10","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=11","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=12","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 4 |
| Details | Region: {"description":"Important for selectivity against fructose","evidences":[{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4ZW9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P32037","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
