Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0015293 | molecular_function | symporter activity |
| A | 0015519 | molecular_function | D-xylose:proton symporter activity |
| A | 0015753 | biological_process | D-xylose transmembrane transport |
| A | 0016020 | cellular_component | membrane |
| A | 0022857 | molecular_function | transmembrane transporter activity |
| A | 0055085 | biological_process | transmembrane transport |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0015293 | molecular_function | symporter activity |
| B | 0015519 | molecular_function | D-xylose:proton symporter activity |
| B | 0015753 | biological_process | D-xylose transmembrane transport |
| B | 0016020 | cellular_component | membrane |
| B | 0022857 | molecular_function | transmembrane transporter activity |
| B | 0055085 | biological_process | transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CD A 501 |
| Chain | Residue |
| A | GLU255 |
| A | HIS258 |
| B | GLU255 |
| B | HIS258 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE LU A 503 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE LU B 501 |
Functional Information from PROSITE/UniProt
| site_id | PS00216 |
| Number of Residues | 18 |
| Details | SUGAR_TRANSPORT_1 Sugar transport proteins signature 1. AIMTVDKFGRKplqiigA |
| Chain | Residue | Details |
| A | ALA332-ALA349 | |
| site_id | PS00217 |
| Number of Residues | 26 |
| Details | SUGAR_TRANSPORT_2 Sugar transport proteins signature 2. IgGIGvGLasmlspmYiaElapahiR |
| Chain | Residue | Details |
| A | ILE135-ARG160 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 44 |
| Details | Transmembrane: {"description":"Helical; Name=1"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 134 |
| Details | Topological domain: {"description":"Periplasmic"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=2"} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 46 |
| Details | Topological domain: {"description":"Cytoplasmic"} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=3"} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 42 |
| Details | Transmembrane: {"description":"Helical; Name=4"} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=5"} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=6"} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 44 |
| Details | Transmembrane: {"description":"Helical; Name=7"} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 42 |
| Details | Transmembrane: {"description":"Helical; Name=8"} |
| site_id | SWS_FT_FI11 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=9"} |
| site_id | SWS_FT_FI12 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=10"} |
| site_id | SWS_FT_FI13 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=11"} |
| site_id | SWS_FT_FI14 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=12"} |
| site_id | SWS_FT_FI15 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23075985","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4GBY","evidenceCode":"ECO:0007744"}]} |
