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 | 0046872 | molecular_function | metal ion binding |
| B | 0004930 | molecular_function | G protein-coupled receptor activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0016020 | cellular_component | membrane |
| B | 0020037 | molecular_function | heme binding |
| B | 0022900 | biological_process | electron transport chain |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE FM9 A 1901 |
| Chain | Residue |
| A | VAL664 |
| A | TYR805 |
| A | LYS811 |
| A | THR815 |
| A | ALA818 |
| A | SER822 |
| A | SER668 |
| A | PRO756 |
| A | LEU757 |
| A | ASN760 |
| A | THR794 |
| A | ILE797 |
| A | TRP798 |
| A | PHE801 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CLR A 1902 |
| Chain | Residue |
| A | ILE597 |
| A | PHE646 |
| A | CLR1904 |
| B | TRP588 |
| B | PHE646 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CLR A 1903 |
| Chain | Residue |
| A | ILE597 |
| A | ALA598 |
| A | LEU602 |
| B | PRO1056 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CLR A 1904 |
| Chain | Residue |
| A | TRP588 |
| A | PHE639 |
| A | PHE646 |
| A | CLR1902 |
| A | CLR1905 |
| B | TRP588 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CLR A 1905 |
| Chain | Residue |
| A | ALA650 |
| A | THR653 |
| A | CLR1904 |
| B | CLR1905 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE OLA A 1906 |
| Chain | Residue |
| A | TYR810 |
| A | PHE817 |
| B | SER702 |
| B | PO41903 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE OLC A 1907 |
| Chain | Residue |
| A | GLY758 |
| A | PHE806 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE OLC A 1908 |
| Chain | Residue |
| A | SER589 |
| A | ILE591 |
| site_id | AC9 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE FM9 B 1901 |
| Chain | Residue |
| B | LEU648 |
| B | GLN660 |
| B | VAL664 |
| B | LEU757 |
| B | ASN760 |
| B | THR794 |
| B | ILE797 |
| B | TRP798 |
| B | PHE801 |
| B | TYR805 |
| B | LYS811 |
| B | ILE812 |
| B | THR815 |
| B | ALA818 |
| B | SER822 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 1902 |
| Chain | Residue |
| B | ASN809 |
| B | TYR810 |
| B | LYS811 |
| B | ILE812 |
| B | ILE813 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 B 1903 |
| Chain | Residue |
| A | TYR810 |
| A | OLA1906 |
| B | PRO698 |
| B | SER702 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE OLC B 1904 |
| Chain | Residue |
| A | TYR836 |
| B | ASN750 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CLR B 1905 |
| Chain | Residue |
| A | CLR1905 |
| B | TRP588 |
| B | ILE594 |
| B | ILE597 |
| B | ALA598 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CLR B 1906 |
| Chain | Residue |
| B | THR653 |
| B | THR655 |
Functional Information from PROSITE/UniProt
| site_id | PS00981 |
| Number of Residues | 11 |
| Details | G_PROTEIN_RECEP_F3_3 G-protein coupled receptors family 3 signature 3. FNEAKyIAFTM |
| Chain | Residue | Details |
| A | PHE781-MET791 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 44 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 26 |
| 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 | 4 |
| Details | Binding site: {"description":"axial binding residue"} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 44 |
| Details | Transmembrane: {"description":"Helical; Name=1"} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 50 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"24603153","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=2"} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 72 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"24603153","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 42 |
| Details | Transmembrane: {"description":"Helical; Name=3"} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 46 |
| Details | Transmembrane: {"description":"Helical; Name=4"} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 42 |
| Details | Transmembrane: {"description":"Helical; Name=5"} |
| site_id | SWS_FT_FI11 |
| Number of Residues | 42 |
| Details | Transmembrane: {"description":"Helical; Name=6"} |
| site_id | SWS_FT_FI12 |
| Number of Residues | 48 |
| Details | Transmembrane: {"description":"Helical; Name=7"} |
