4XT3
Structure of a viral GPCR bound to human chemokine CX3CL1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004930 | molecular_function | G protein-coupled receptor activity |
| A | 0004950 | molecular_function | chemokine receptor activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0006935 | biological_process | chemotaxis |
| A | 0006955 | biological_process | immune response |
| A | 0007165 | biological_process | signal transduction |
| A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| A | 0007204 | biological_process | positive regulation of cytosolic calcium ion concentration |
| A | 0016020 | cellular_component | membrane |
| A | 0016493 | molecular_function | C-C chemokine receptor activity |
| A | 0019087 | biological_process | symbiont-mediated transformation of host cell |
| A | 0019722 | biological_process | calcium-mediated signaling |
| A | 0019957 | molecular_function | C-C chemokine binding |
| A | 0020002 | cellular_component | host cell plasma membrane |
| A | 0052031 | biological_process | symbiont-mediated perturbation of host defense response |
| A | 0060326 | biological_process | cell chemotaxis |
| A | 0070098 | biological_process | chemokine-mediated signaling pathway |
| B | 0005576 | cellular_component | extracellular region |
| B | 0006955 | biological_process | immune response |
| B | 0008009 | molecular_function | chemokine activity |
Functional Information from PROSITE/UniProt
| site_id | PS00237 |
| Number of Residues | 17 |
| Details | G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASLcFITEIALDRYYaI |
| Chain | Residue | Details |
| A | ALA117-ILE133 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 55 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 39 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
