Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004930 | molecular_function | G protein-coupled receptor activity |
| A | 0004993 | molecular_function | G protein-coupled serotonin receptor activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005886 | cellular_component | plasma membrane |
| 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 | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | binding site for residue E2J A 1201 |
| Chain | Residue |
| A | TRP130 |
| A | PHE223 |
| A | PHE320 |
| A | PHE327 |
| A | PHE328 |
| A | ASN351 |
| A | VAL354 |
| A | TYR358 |
| A | HOH1301 |
| A | ASP134 |
| A | VAL135 |
| A | SER138 |
| A | THR139 |
| A | ILE142 |
| A | VAL215 |
| A | GLY218 |
| A | SER219 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue OLC A 1202 |
| Chain | Residue |
| A | TRP55 |
| A | LEU349 |
| A | PHE353 |
| A | OLC1203 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue OLC A 1203 |
| Chain | Residue |
| A | LEU333 |
| A | MET346 |
| A | OLC1202 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue OLC A 1204 |
| Chain | Residue |
| A | MET76 |
| A | TYR382 |
| A | ASN386 |
| A | TYR387 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue OLC A 1206 |
| Chain | Residue |
| A | THR228 |
| A | ILE229 |
| A | ILE232 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue OLC A 1207 |
| Chain | Residue |
| A | CYS146 |
| A | VAL221 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue PEG A 1208 |
| Chain | Residue |
| A | LEU370 |
| A | PHE371 |
| A | ARG376 |
| A | ARG376 |
| A | ARG377 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue OLA A 1210 |
| Chain | Residue |
| A | TYR90 |
| A | MET93 |
| A | ILE97 |
| A | ILE172 |
| A | TRP179 |
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. ASImHLCAISLDRYVaI |
| Chain | Residue | Details |
| A | ALA140-ILE156 | |
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","evidences":[{"source":"PubMed","id":"29398112","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6BQG","evidenceCode":"ECO:0000312"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"29398112","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6BQG","evidenceCode":"ECO:0000312"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 24 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"29398112","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6BQG","evidenceCode":"ECO:0000312"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 49 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"29398112","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6BQG","evidenceCode":"ECO:0000312"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"29398112","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6BQG","evidenceCode":"ECO:0000312"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 21 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"29398112","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6BQG","evidenceCode":"ECO:0000312"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"29398112","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6BQG","evidenceCode":"ECO:0000312"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 24 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"29398112","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6BQG","evidenceCode":"ECO:0000312"}]} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"29398112","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6BQG","evidenceCode":"ECO:0000312"}]} |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | Motif: {"description":"DRY motif; important for ligand-induced conformation changes","evidences":[{"source":"UniProtKB","id":"P41595","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | Motif: {"description":"NPxxY motif; important for ligand-induced conformation changes and signaling","evidences":[{"source":"UniProtKB","id":"P41595","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29398112","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6BQG","evidenceCode":"ECO:0000312"}]} |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]} |