8Z67
Cryo-EM structure of the hGPR68-Gs complex in pH6.8
Functional Information from GO Data
Chain | GOid | namespace | contents |
R | 0004930 | molecular_function | G protein-coupled receptor activity |
R | 0005886 | cellular_component | plasma membrane |
R | 0007165 | biological_process | signal transduction |
R | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
R | 0007189 | biological_process | adenylate cyclase-activating G protein-coupled receptor signaling pathway |
R | 0007200 | biological_process | phospholipase C-activating G protein-coupled receptor signaling pathway |
R | 0010447 | biological_process | response to acidic pH |
R | 0016020 | cellular_component | membrane |
R | 0016525 | biological_process | negative regulation of angiogenesis |
R | 0030155 | biological_process | regulation of cell adhesion |
R | 0035025 | biological_process | positive regulation of Rho protein signal transduction |
R | 0043114 | biological_process | regulation of vascular permeability |
R | 0050729 | biological_process | positive regulation of inflammatory response |
R | 0060055 | biological_process | angiogenesis involved in wound healing |
R | 0071468 | biological_process | cellular response to acidic pH |
R | 0072144 | biological_process | glomerular mesangial cell development |
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. ISIaFLCCISVDRYLaV |
Chain | Residue | Details |
R | ILE103-VAL119 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 71 |
Details | TOPO_DOM: Extracellular => ECO:0000255 |
Chain | Residue | Details |
R | MET1-HIS17 | |
R | PHE77-LYS91 | |
R | HIS155-ALA179 | |
R | SER246-ARG263 |
site_id | SWS_FT_FI2 |
Number of Residues | 24 |
Details | TRANSMEM: Helical; Name=1 => ECO:0000255 |
Chain | Residue | Details |
R | LEU18-ALA42 |
site_id | SWS_FT_FI3 |
Number of Residues | 128 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
Chain | Residue | Details |
R | TYR43-VAL54 | |
R | ASP114-LYS132 | |
R | ARG202-ARG224 | |
R | LEU285-GLN362 |
site_id | SWS_FT_FI4 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=2 => ECO:0000255 |
Chain | Residue | Details |
R | TYR55-TYR76 |
site_id | SWS_FT_FI5 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000255 |
Chain | Residue | Details |
R | LEU92-VAL113 |
site_id | SWS_FT_FI6 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000255 |
Chain | Residue | Details |
R | THR133-PHE154 |
site_id | SWS_FT_FI7 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000255 |
Chain | Residue | Details |
R | TRP180-TYR201 |
site_id | SWS_FT_FI8 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000255 |
Chain | Residue | Details |
R | LEU225-LEU245 |
site_id | SWS_FT_FI9 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=7 => ECO:0000255 |
Chain | Residue | Details |
R | VAL264-ILE284 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
R | ASN3 | |
R | ASN164 |