Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004930 | molecular_function | G protein-coupled receptor activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0016020 | cellular_component | membrane |
| B | 0004930 | molecular_function | G protein-coupled receptor activity |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 155 |
| Chain | Residue |
| A | ASP95 |
| A | VAL96 |
| A | GLU98 |
| A | ASN114 |
| A | THR115 |
| A | SER118 |
| A | HOH2018 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 156 |
| Chain | Residue |
| A | GLU46 |
| A | ASN63 |
| A | THR64 |
| A | SER67 |
| A | HOH2014 |
| A | ASP43 |
| A | ILE44 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 155 |
| Chain | Residue |
| B | ASP95 |
| B | VAL96 |
| B | GLU98 |
| B | ASN114 |
| B | THR115 |
| B | SER118 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA B 156 |
| Chain | Residue |
| B | ASP43 |
| B | ILE44 |
| B | GLU46 |
| B | ASN63 |
| B | THR64 |
| B | SER67 |
| B | HOH2002 |
Functional Information from PROSITE/UniProt
| site_id | PS00010 |
| Number of Residues | 12 |
| Details | ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CwNtegsYdCvC |
| Chain | Residue | Details |
| A | CYS61-CYS72 | |
| A | CYS112-CYS123 | |
| site_id | PS01187 |
| Number of Residues | 28 |
| Details | EGF_CA Calcium-binding EGF-like domain signature. DiNECatlskvs.......Cgkfsd..CwNtegsYdC |
| Chain | Residue | Details |
| A | ASP43-CYS70 | |
| A | ASP95-CYS121 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN17 | |
| A | ASN87 | |
| B | ASN17 | |
| B | ASN87 | |
