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 | 0043448 | biological_process | alkane catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 1201 |
| Chain | Residue |
| A | CYS1006 |
| A | CYS1009 |
| A | CYS1039 |
| A | CYS1042 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue OLC A 1202 |
| Chain | Residue |
| A | SER272 |
| A | VAL273 |
| A | MET276 |
| A | LEU277 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue OLC A 1203 |
| Chain | Residue |
| A | HOH1301 |
| A | ILE316 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue OLC A 1204 |
| Chain | Residue |
| A | VAL37 |
| A | VAL39 |
| A | ILE41 |
| A | THR44 |
| A | HIS103 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue OLC A 1205 |
| Chain | Residue |
| A | TYR202 |
| A | SER289 |
| A | LEU328 |
| A | ARG329 |
| A | SER332 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue OLC A 1206 |
| Chain | Residue |
| A | THR60 |
| A | VAL64 |
| A | THR323 |
| A | PHE324 |
| A | GLY327 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue OLC A 1207 |
| Chain | Residue |
| A | THR60 |
| A | VAL64 |
| A | OLC1208 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | binding site for residue OLC A 1208 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue OLC A 1210 |
| Chain | Residue |
| A | TRP180 |
| A | TYR202 |
| A | CYS209 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue OLC A 1211 |
| Chain | Residue |
| A | HIS33 |
| A | ASP38 |
| A | PHE42 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue OLC A 1212 |
| Chain | Residue |
| A | THR297 |
| A | LEU301 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue PEG A 1213 |
| Chain | Residue |
| A | ARG24 |
| A | GLU191 |
| A | ASP1036 |
Functional Information from PROSITE/UniProt
| site_id | PS00028 |
| Number of Residues | 23 |
| Details | ZINC_FINGER_C2H2_1 Zinc finger C2H2 type domain signature. Cts..CmefLevlfqgphHhhhhhH |
| Chain | Residue | Details |
| A | CYS336-HIS618 | |
| site_id | PS00202 |
| Number of Residues | 11 |
| Details | RUBREDOXIN Rubredoxin signature. IpDDWvCPlCG |
| Chain | Residue | Details |
| A | ILE1033-GLY1043 | |
| site_id | PS00237 |
| Number of Residues | 17 |
| Details | G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. VSMwCLACISVDRYLaI |
| Chain | Residue | Details |
| A | VAL127-ILE143 | |
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 | 20 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 38 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 21 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI11 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI12 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]} |
