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 | 0007194 | biological_process | negative regulation of adenylate cyclase activity |
A | 0007596 | biological_process | blood coagulation |
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 | 0045028 | molecular_function | G protein-coupled purinergic nucleotide receptor activity |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE 6AD A 1201 |
Chain | Residue |
A | ARG93 |
A | LYS179 |
A | HIS187 |
A | VAL190 |
A | ASN191 |
A | CYS194 |
A | ARG256 |
A | TYR259 |
A | GLN263 |
A | LYS280 |
A | HOH1319 |
A | CYS97 |
A | HOH1322 |
A | HOH1331 |
A | HOH1336 |
A | HOH1348 |
A | SER101 |
A | VAL102 |
A | TYR105 |
A | SER156 |
A | ASN159 |
A | LYS174 |
A | CYS175 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE CLR A 1202 |
Chain | Residue |
A | SER55 |
A | ILE61 |
A | LYS64 |
A | ASN65 |
A | ILE68 |
A | TRP149 |
A | PHE153 |
A | PHE153 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE OLC A 1203 |
Chain | Residue |
A | GLN98 |
A | ILE161 |
A | ASN164 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE OLC A 1204 |
Chain | Residue |
A | ARG231 |
A | VAL236 |
A | THR275 |
A | TYR278 |
A | SER282 |
A | OLC1205 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE OLC A 1205 |
Chain | Residue |
A | ASP20 |
A | ILE23 |
A | LEU27 |
A | SER282 |
A | OLC1204 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PEG A 1206 |
Chain | Residue |
A | ASN1022 |
A | GLN1025 |
A | GLN1041 |
A | ARG1062 |
A | HOH1315 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 22 |
Details | TRANSMEM: Helical; Name=1 |
Chain | Residue | Details |
A | PHE28-PHE50 | |
site_id | SWS_FT_FI2 |
Number of Residues | 76 |
Details | TOPO_DOM: Cytoplasmic |
Chain | Residue | Details |
A | PHE51-ILE61 | |
A | THR119-LYS142 | |
A | PHE299-MET342 | |
site_id | SWS_FT_FI3 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=2 |
Chain | Residue | Details |
A | PHE62-LEU82 | |
site_id | SWS_FT_FI4 |
Number of Residues | 54 |
Details | TOPO_DOM: Extracellular |
Chain | Residue | Details |
A | SER83-CYS97 | |
A | THR163-VAL185 | |
A | THR260-TYR278 | |
site_id | SWS_FT_FI5 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=3 |
Chain | Residue | Details |
A | GLN98-ILE118 | |
site_id | SWS_FT_FI6 |
Number of Residues | 19 |
Details | TRANSMEM: Helical; Name=4 |
Chain | Residue | Details |
A | ILE143-LEU162 | |
site_id | SWS_FT_FI7 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=5 |
Chain | Residue | Details |
A | TRP186-VAL207 | |
site_id | SWS_FT_FI8 |
Number of Residues | 25 |
Details | TRANSMEM: Helical; Name=6 |
Chain | Residue | Details |
A | VAL234-TYR259 | |
site_id | SWS_FT_FI9 |
Number of Residues | 19 |
Details | TRANSMEM: Helical; Name=7 |
Chain | Residue | Details |
A | VAL279-TYR298 | |
site_id | SWS_FT_FI10 |
Number of Residues | 10 |
Details | BINDING: |
Chain | Residue | Details |
A | ARG93 | |
A | LYS280 | |
A | CYS97 | |
A | TYR105 | |
A | SER156 | |
A | CYS175 | |
A | HIS187 | |
A | ASN191 | |
A | ARG256 | |
A | GLN263 | |
Chain | Residue | Details |
A | SER55 | |
A | SER57 | |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN6 | |
A | ASN13 | |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
A | TRP1007 | |
A | ILE1102 | |