Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004930 | molecular_function | G protein-coupled receptor activity |
| A | 0004960 | molecular_function | thromboxane 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 | 0043448 | biological_process | alkane catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue A90 A 9001 |
| Chain | Residue |
| A | GLY77 |
| A | TRP258 |
| A | LEU291 |
| A | LEU294 |
| A | ARG295 |
| A | THR298 |
| A | GLN301 |
| A | LEU78 |
| A | THR81 |
| A | VAL85 |
| A | HIS89 |
| A | MET112 |
| A | SER181 |
| A | TRP182 |
| A | PHE184 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 9002 |
| Chain | Residue |
| A | CYS2006 |
| A | CYS2009 |
| A | CYS2039 |
| A | CYS2042 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue CLR A 9003 |
| Chain | Residue |
| A | ARG103 |
| A | PHE107 |
| A | VAL110 |
| A | TRP150 |
| A | GLY154 |
| A | TRP157 |
| A | LEU161 |
| A | LEU168 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 9004 |
| Chain | Residue |
| A | GLU94 |
| A | TRP95 |
| A | HIS96 |
| A | GLN1103 |
| A | ASP2036 |
Functional Information from PROSITE/UniProt
| site_id | PS00202 |
| Number of Residues | 11 |
| Details | RUBREDOXIN Rubredoxin signature. IpDDWvCPlCG |
| Chain | Residue | Details |
| A | ILE2033-GLY2043 | |
| site_id | PS00237 |
| Number of Residues | 17 |
| Details | G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. SPLlLGAAMASERYLgI |
| Chain | Residue | Details |
| A | SER118-ILE134 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 53 |
| Details | Domain: {"description":"Rubredoxin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00241","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00241","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10216292","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-formylmethionine","evidences":[{"source":"PubMed","id":"1637309","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 22 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| site_id | SWS_FT_FI5 |
| 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_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue"} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 56 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 21 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI11 |
| Number of Residues | 20 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI12 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI13 |
| Number of Residues | 25 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI14 |
| Number of Residues | 23 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI15 |
| Number of Residues | 21 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI16 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine"} |
