6THA
Crystal structure of human sugar transporter GLUT1 (SLC2A1) in the inward conformation
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000139 | cellular_component | Golgi membrane |
A | 0001666 | biological_process | response to hypoxia |
A | 0001674 | cellular_component | female germ cell nucleus |
A | 0001917 | cellular_component | photoreceptor inner segment |
A | 0001939 | cellular_component | female pronucleus |
A | 0005324 | molecular_function | long-chain fatty acid transmembrane transporter activity |
A | 0005355 | molecular_function | glucose transmembrane transporter activity |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0005901 | cellular_component | caveola |
A | 0005911 | cellular_component | cell-cell junction |
A | 0007417 | biological_process | central nervous system development |
A | 0007565 | biological_process | female pregnancy |
A | 0014704 | cellular_component | intercalated disc |
A | 0015911 | biological_process | long-chain fatty acid import across plasma membrane |
A | 0016020 | cellular_component | membrane |
A | 0016323 | cellular_component | basolateral plasma membrane |
A | 0016324 | cellular_component | apical plasma membrane |
A | 0019852 | biological_process | L-ascorbic acid metabolic process |
A | 0019900 | molecular_function | kinase binding |
A | 0021987 | biological_process | cerebral cortex development |
A | 0022857 | molecular_function | transmembrane transporter activity |
A | 0030018 | cellular_component | Z disc |
A | 0030496 | cellular_component | midbody |
A | 0030864 | cellular_component | cortical actin cytoskeleton |
A | 0031982 | cellular_component | vesicle |
A | 0032868 | biological_process | response to insulin |
A | 0033300 | molecular_function | dehydroascorbic acid transmembrane transporter activity |
A | 0042149 | biological_process | cellular response to glucose starvation |
A | 0042383 | cellular_component | sarcolemma |
A | 0042470 | cellular_component | melanosome |
A | 0042802 | molecular_function | identical protein binding |
A | 0042908 | biological_process | xenobiotic transport |
A | 0042910 | molecular_function | xenobiotic transmembrane transporter activity |
A | 0045121 | cellular_component | membrane raft |
A | 0045202 | cellular_component | synapse |
A | 0045494 | biological_process | photoreceptor cell maintenance |
A | 0046323 | biological_process | glucose import |
A | 0055056 | molecular_function | D-glucose transmembrane transporter activity |
A | 0055085 | biological_process | transmembrane transport |
A | 0065003 | biological_process | protein-containing complex assembly |
A | 0070062 | cellular_component | extracellular exosome |
A | 0070837 | biological_process | dehydroascorbic acid transport |
A | 0071260 | biological_process | cellular response to mechanical stimulus |
A | 0071474 | biological_process | cellular hyperosmotic response |
A | 0072562 | cellular_component | blood microparticle |
A | 0098708 | biological_process | glucose import across plasma membrane |
A | 0098793 | cellular_component | presynapse |
A | 0150104 | biological_process | transport across blood-brain barrier |
A | 1904016 | biological_process | response to Thyroglobulin triiodothyronine |
A | 1904659 | biological_process | glucose transmembrane transport |
A | 1990350 | cellular_component | glucose transporter complex |
Functional Information from PROSITE/UniProt
site_id | PS00216 |
Number of Residues | 17 |
Details | SUGAR_TRANSPORT_1 Sugar transport proteins signature 1. SLFVVERAGRRtlhli.G |
Chain | Residue | Details |
A | SER324-GLY340 |
site_id | PS00217 |
Number of Residues | 26 |
Details | SUGAR_TRANSPORT_2 Sugar transport proteins signature 2. IiGVYcGLttgfvpmYvgEvsptalR |
Chain | Residue | Details |
A | ILE128-ARG153 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 144 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:24847886 |
Chain | Residue | Details |
A | MET1-ARG11 | |
A | ASN88-PHE90 | |
A | GLY145-ALA155 | |
A | CYS207-PRO271 | |
A | GLU329-ARG334 | |
A | PHE389-PRO401 | |
A | LYS451-VAL492 |
site_id | SWS_FT_FI2 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=1 |
Chain | Residue | Details |
A | LEU12-ILE33 |
site_id | SWS_FT_FI3 |
Number of Residues | 74 |
Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:24847886 |
Chain | Residue | Details |
A | ASN34-SER66 | |
A | SER113-GLU120 | |
A | ASP177-LEU185 | |
A | SER294-PRO306 | |
A | ALA356-SER365 | |
A | GLN423-CYS429 |
site_id | SWS_FT_FI4 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=2 |
Chain | Residue | Details |
A | LEU67-VAL87 |
site_id | SWS_FT_FI5 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=3 |
Chain | Residue | Details |
A | GLY91-PHE112 |
site_id | SWS_FT_FI6 |
Number of Residues | 23 |
Details | TRANSMEM: Helical; Name=4 |
Chain | Residue | Details |
A | MET121-VAL144 |
site_id | SWS_FT_FI7 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=5 |
Chain | Residue | Details |
A | LEU156-LEU176 |
site_id | SWS_FT_FI8 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=6 |
Chain | Residue | Details |
A | TRP186-PHE206 |
site_id | SWS_FT_FI9 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=7 |
Chain | Residue | Details |
A | ILE272-TYR293 |
site_id | SWS_FT_FI10 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=8 |
Chain | Residue | Details |
A | VAL307-VAL328 |
site_id | SWS_FT_FI11 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=9 |
Chain | Residue | Details |
A | THR335-LEU355 |
site_id | SWS_FT_FI12 |
Number of Residues | 22 |
Details | TRANSMEM: Helical; Name=10 |
Chain | Residue | Details |
A | TYR366-TRP388 |
site_id | SWS_FT_FI13 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=11 |
Chain | Residue | Details |
A | ALA402-PHE422 |
site_id | SWS_FT_FI14 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=12 |
Chain | Residue | Details |
A | GLY430-PHE450 |
site_id | SWS_FT_FI15 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27078104, ECO:0007744|PDB:5EQI |
Chain | Residue | Details |
A | THR137 | |
A | GLN282 | |
A | TRP388 |
site_id | SWS_FT_FI16 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000305|PubMed:24847886, ECO:0007744|PDB:4PYP |
Chain | Residue | Details |
A | ASN288 | |
A | ASN317 | |
A | GLU380 |
site_id | SWS_FT_FI17 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27078104 |
Chain | Residue | Details |
A | ASN411 |
site_id | SWS_FT_FI18 |
Number of Residues | 1 |
Details | SITE: Not glycosylated => ECO:0000269|PubMed:3839598 |
Chain | Residue | Details |
A | ASN411 |
site_id | SWS_FT_FI19 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22814378 |
Chain | Residue | Details |
A | MET1 |
site_id | SWS_FT_FI20 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by PKC/PRKCB => ECO:0000269|PubMed:25982116 |
Chain | Residue | Details |
A | SER226 |
site_id | SWS_FT_FI21 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER465 |
site_id | SWS_FT_FI22 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231 |
Chain | Residue | Details |
A | THR478 |
site_id | SWS_FT_FI23 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER490 |
site_id | SWS_FT_FI24 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:3839598 |
Chain | Residue | Details |
A | ASN45 |