Functional Information from GO Data
| Chain | GOid | namespace | contents |
| B | 0004875 | molecular_function | complement receptor activity |
| B | 0004930 | molecular_function | G protein-coupled receptor activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0006935 | biological_process | chemotaxis |
| 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 | 10 |
| Details | binding site for residue 9P2 B 501 |
| Chain | Residue |
| B | ILE210 |
| B | THR303 |
| B | LEU211 |
| B | ALA214 |
| B | THR215 |
| B | ALA242 |
| B | VAL245 |
| B | LEU295 |
| B | TRP299 |
| B | PRO300 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | binding site for PMX53 chain L |
| Chain | Residue |
| B | LEU178 |
| B | SER181 |
| B | PRO199 |
| B | ARG261 |
| B | VAL262 |
| B | ARG264 |
| B | CYS274 |
| B | GLY275 |
| B | VAL276 |
| B | SER279 |
| B | TYR344 |
| B | THR347 |
| B | GLY348 |
| B | ASP368 |
| B | VAL372 |
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. ASIlLLATISADRFLlV |
| Chain | Residue | Details |
| B | ALA208-VAL224 | |
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 | 26 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"29300009","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"29300009","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 23 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"29300009","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 57 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"29300009","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 21 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"29300009","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"29300009","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 25 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"29300009","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"29300009","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"29300009","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"7642584","evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"10636859","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7642584","evidenceCode":"ECO:0000269"}]} |
