Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004930 | molecular_function | G protein-coupled receptor activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0016020 | cellular_component | membrane |
| A | 0020037 | molecular_function | heme binding |
| A | 0022900 | biological_process | electron transport chain |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0070915 | molecular_function | lysophosphatidic acid receptor activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue ON3 A 2000 |
| Chain | Residue |
| A | VAL52 |
| A | GLU293 |
| A | LYS294 |
| A | PHE296 |
| A | LEU297 |
| A | THR109 |
| A | GLN125 |
| A | ILE128 |
| A | ASP129 |
| A | TRP210 |
| A | TRP271 |
| A | GLY274 |
| A | LEU278 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue 1WV A 2001 |
| Chain | Residue |
| A | LEU51 |
| A | LEU122 |
| A | THR130 |
| A | GLY179 |
| A | SER183 |
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. ASVaNLLAIAIERHItV |
| Chain | Residue | Details |
| A | ALA134-VAL150 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Transmembrane: {"description":"Helical; Name=1"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 25 |
| Details | Topological domain: {"description":"Cytoplasmic"} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 23 |
| Details | Transmembrane: {"description":"Helical; Name=2"} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 45 |
| Details | Topological domain: {"description":"Extracellular"} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical; Name=3"} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=4"} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=5"} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 24 |
| Details | Transmembrane: {"description":"Helical; Name=6"} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=7"} |
| site_id | SWS_FT_FI11 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26091040","evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
