Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004930 | molecular_function | G protein-coupled receptor activity |
A | 0004993 | molecular_function | G protein-coupled serotonin receptor activity |
A | 0005506 | molecular_function | iron ion binding |
A | 0005886 | cellular_component | plasma membrane |
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PLM A 1201 |
Chain | Residue |
A | LEU62 |
A | CYS353 |
A | ILE395 |
A | THR396 |
A | CYS397 |
site_id | AC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE ERM A 1202 |
Chain | Residue |
A | LEU209 |
A | PHE217 |
A | MET218 |
A | ALA225 |
A | PHE340 |
A | ASN344 |
A | GLN359 |
A | HOH1302 |
A | ASP135 |
A | SER139 |
A | THR140 |
A | VAL208 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CLR A 1203 |
Chain | Residue |
A | ILE61 |
A | ILE69 |
A | GLY70 |
A | TYR394 |
A | TYR399 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE OLC A 1204 |
Chain | Residue |
A | SER150 |
A | MET233 |
A | THR240 |
A | LEU326 |
site_id | AC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE OLC A 1205 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PEG A 1206 |
Chain | Residue |
A | TYR87 |
A | TYR380 |
A | ASN384 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE OLC A 1207 |
Chain | Residue |
A | LEU77 |
A | HOH1305 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE OLC A 1208 |
Chain | Residue |
A | LYS193 |
A | ASP216 |
A | PHE217 |
A | OLA1212 |
A | OLA1212 |
site_id | AC9 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE TRS A 1209 |
site_id | BC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE OLA A 1211 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE OLA A 1212 |
Chain | Residue |
A | ILE174 |
A | OLC1208 |
A | OLC1208 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE DGA A 1213 |
Chain | Residue |
A | LEU239 |
A | HIS242 |
A | DGA1214 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE DGA A 1214 |
Chain | Residue |
A | HIS55 |
A | HIS242 |
A | DGA1213 |
A | HOH1306 |
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. ASIwHLCAISVDRYIaI |
Chain | Residue | Details |
A | ALA141-ILE157 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ALA57-VAL79 | |
Chain | Residue | Details |
A | SER80-ASN90 | |
A | ASP152-THR171 | |
Chain | Residue | Details |
A | TYR91-LEU113 | |
Chain | Residue | Details |
A | THR114-PRO129 | |
A | LYS193-ASP216 | |
A | THR346-MET360 | |
Chain | Residue | Details |
A | ALA130-VAL151 | |
Chain | Residue | Details |
A | ALA172-ILE192 | |
Chain | Residue | Details |
A | PHE217-LEU239 | |
Chain | Residue | Details |
A | VAL325-ILE345 | |
Chain | Residue | Details |
A | LEU361-LEU382 | |
Chain | Residue | Details |
A | ASP135 | |
A | THR140 | |
A | LEU209 | |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | SITE: Hydrophobic barrier that decreases the speed of ligand binding and dissociation => ECO:0000269|PubMed:28129538 |
Chain | Residue | Details |
A | LEU209 | |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000255 |
Chain | Residue | Details |
A | CYS397 | |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
A | TRP1007 | |
A | ILE1102 | |