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 | 0007194 | biological_process | negative regulation of adenylate cyclase activity |
| A | 0007596 | biological_process | blood coagulation |
| 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 | 0045028 | molecular_function | G protein-coupled purinergic nucleotide receptor activity |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE 6AT A 1201 |
| Chain | Residue |
| A | ARG93 |
| A | CYS175 |
| A | SER176 |
| A | LYS179 |
| A | HIS187 |
| A | VAL190 |
| A | ASN191 |
| A | CYS194 |
| A | ARG256 |
| A | TYR259 |
| A | GLN263 |
| A | CYS97 |
| A | LYS280 |
| A | SER101 |
| A | VAL102 |
| A | TYR105 |
| A | SER156 |
| A | ASN159 |
| A | LYS173 |
| A | LYS174 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE OLC A 1202 |
| Chain | Residue |
| A | THR275 |
| A | TYR278 |
| A | OLC1203 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE OLC A 1203 |
| Chain | Residue |
| A | ASP20 |
| A | ILE23 |
| A | PHE28 |
| A | TYR278 |
| A | SER282 |
| A | TRP285 |
| A | OLC1202 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 22 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 13 |
| Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue"} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical; Name=1"} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 10 |
| Details | Topological domain: {"description":"Cytoplasmic"} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=2"} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=3"} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 19 |
| Details | Transmembrane: {"description":"Helical; Name=4"} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 40 |
| Details | Topological domain: {"description":"Extracellular"} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 21 |
| Details | Transmembrane: {"description":"Helical; Name=5"} |
| site_id | SWS_FT_FI11 |
| Number of Residues | 25 |
| Details | Transmembrane: {"description":"Helical; Name=6"} |
| site_id | SWS_FT_FI12 |
| Number of Residues | 19 |
| Details | Transmembrane: {"description":"Helical; Name=7"} |
| site_id | SWS_FT_FI13 |
| Number of Residues | 17 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9EPX4","evidenceCode":"ECO:0000250"}]} |
