4YB9
Crystal structure of the Bovine Fructose transporter GLUT5 in an open inward-facing conformation
Functional Information from GO Data
Chain | GOid | namespace | contents |
D | 0003044 | biological_process | regulation of systemic arterial blood pressure mediated by a chemical signal |
D | 0005353 | molecular_function | fructose transmembrane transporter activity |
D | 0005886 | cellular_component | plasma membrane |
D | 0009750 | biological_process | response to fructose |
D | 0015755 | biological_process | fructose transmembrane transport |
D | 0016020 | cellular_component | membrane |
D | 0016324 | cellular_component | apical plasma membrane |
D | 0022857 | molecular_function | transmembrane transporter activity |
D | 0042383 | cellular_component | sarcolemma |
D | 0046323 | biological_process | D-glucose import |
D | 0055056 | molecular_function | D-glucose transmembrane transporter activity |
D | 0055085 | biological_process | transmembrane transport |
D | 0070061 | molecular_function | fructose binding |
D | 0070837 | biological_process | dehydroascorbic acid transport |
D | 0071332 | biological_process | cellular response to fructose stimulus |
D | 1990539 | biological_process | fructose import across plasma membrane |
Functional Information from PROSITE/UniProt
site_id | PS00216 |
Number of Residues | 17 |
Details | SUGAR_TRANSPORT_1 Sugar transport proteins signature 1. AIFVVELMGRRfllll.G |
Chain | Residue | Details |
D | ALA332-GLY348 |
site_id | PS00217 |
Number of Residues | 26 |
Details | SUGAR_TRANSPORT_2 Sugar transport proteins signature 2. LvGICaGLssnvvpmYlgElapknwR |
Chain | Residue | Details |
D | LEU134-ARG159 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"26416735","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 69 |
Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"26416735","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 22 |
Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"26416735","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 41 |
Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"26416735","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"26416735","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 22 |
Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"26416735","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"26416735","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"26416735","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"26416735","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=8","evidences":[{"source":"PubMed","id":"26416735","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=9","evidences":[{"source":"PubMed","id":"26416735","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 22 |
Details | Transmembrane: {"description":"Helical; Name=10","evidences":[{"source":"PubMed","id":"26416735","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=11","evidences":[{"source":"PubMed","id":"26416735","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI14 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=12","evidences":[{"source":"PubMed","id":"26416735","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI15 |
Number of Residues | 7 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P43427","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI16 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |