Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003796 | molecular_function | lysozyme activity |
| A | 0004930 | molecular_function | G protein-coupled receptor activity |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| A | 0016020 | cellular_component | membrane |
| A | 0016907 | molecular_function | G protein-coupled acetylcholine receptor activity |
| A | 0040012 | biological_process | regulation of locomotion |
| B | 0003796 | molecular_function | lysozyme activity |
| B | 0004930 | molecular_function | G protein-coupled receptor activity |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| B | 0016020 | cellular_component | membrane |
| B | 0016907 | molecular_function | G protein-coupled acetylcholine receptor activity |
| B | 0040012 | biological_process | regulation of locomotion |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue 0HK A 1201 |
| Chain | Residue |
| A | ASP112 |
| A | TRP413 |
| A | TYR416 |
| A | ASN417 |
| A | TYR439 |
| A | CYS442 |
| A | TYR443 |
| A | TYR113 |
| A | SER116 |
| A | ASN117 |
| A | TRP164 |
| A | THR196 |
| A | THR199 |
| A | ALA203 |
| A | PHE204 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue OLA A 1202 |
| Chain | Residue |
| A | LEU100 |
| A | OLA1203 |
| A | OLA1209 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue OLA A 1203 |
| Chain | Residue |
| A | ALA83 |
| A | LEU88 |
| A | PRO99 |
| A | OLA1202 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue EDT A 1204 |
| Chain | Residue |
| A | GLY20 |
| A | PRO21 |
| A | SER23 |
| A | GLY176 |
| B | SER219 |
| B | SER222 |
| B | ARG223 |
| B | SER224 |
| B | ARG225 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue P6G A 1205 |
| Chain | Residue |
| A | TYR89 |
| A | LEU109 |
| A | TYR113 |
| A | CYS185 |
| A | PHE186 |
| A | ILE187 |
| A | LEU190 |
| A | TRP435 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue OLC A 1206 |
| Chain | Residue |
| A | LYS58 |
| A | TYR69 |
| A | PHE72 |
| A | SER73 |
| A | LEU111 |
| A | TRP157 |
| B | OLC1202 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue OLC A 1207 |
| Chain | Residue |
| A | PHE128 |
| A | TYR131 |
| A | LYS136 |
| A | ILE210 |
| B | LEU107 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | binding site for residue OLC A 1208 |
| Chain | Residue |
| A | ARG26 |
| A | ASN117 |
| A | LEU163 |
| A | TRP164 |
| A | TRP171 |
| A | PHE189 |
| A | SER191 |
| A | ASN192 |
| A | ALA202 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue OLA A 1209 |
| Chain | Residue |
| A | VAL104 |
| A | OLA1202 |
| A | HOH1307 |
| B | PHE128 |
| B | TYR131 |
| site_id | AD1 |
| Number of Residues | 16 |
| Details | binding site for residue 0HK B 1201 |
| Chain | Residue |
| B | ASP112 |
| B | TYR113 |
| B | SER116 |
| B | ASN117 |
| B | TRP164 |
| B | THR196 |
| B | THR199 |
| B | ALA200 |
| B | ALA203 |
| B | PHE204 |
| B | TRP413 |
| B | TYR416 |
| B | ASN417 |
| B | TYR439 |
| B | CYS442 |
| B | TYR443 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue OLC B 1202 |
| Chain | Residue |
| A | TYR69 |
| A | GLY150 |
| A | ALA154 |
| A | TRP157 |
| A | OLC1206 |
| B | PHE197 |
| B | THR424 |
| site_id | AD3 |
| Number of Residues | 9 |
| Details | binding site for residue OLA B 1203 |
| Chain | Residue |
| A | PHE197 |
| A | ILE201 |
| A | TYR205 |
| A | LEU206 |
| A | THR424 |
| B | GLY150 |
| B | ALA154 |
| B | TRP157 |
| B | OLA1204 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue OLA B 1204 |
| Chain | Residue |
| B | VAL114 |
| B | TRP157 |
| B | OLA1203 |
| B | PHE72 |
| B | SER73 |
| site_id | AD5 |
| Number of Residues | 7 |
| Details | binding site for residue P6G B 1205 |
| Chain | Residue |
| B | TYR89 |
| B | TYR113 |
| B | PHE186 |
| B | ILE187 |
| B | TYR416 |
| B | TRP435 |
| B | TYR439 |
| site_id | AD6 |
| Number of Residues | 8 |
| Details | binding site for residue OLC B 1206 |
| Chain | Residue |
| B | ASN117 |
| B | LEU163 |
| B | TRP164 |
| B | TRP171 |
| B | PHE189 |
| B | SER191 |
| B | ASN192 |
| B | ALA203 |
| site_id | AD7 |
| Number of Residues | 7 |
| Details | binding site for residue PG6 B 1207 |
| Chain | Residue |
| B | GLY1070 |
| B | ASN1073 |
| B | SER1074 |
| B | ASN1089 |
| B | SER1093 |
| B | ARG1094 |
| B | TRP1095 |
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. ASVmNLLIISFDRYFcV |
| Chain | Residue | Details |
| A | ALA118-VAL134 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000303"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 44 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 64 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 100 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 42 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 44 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 44 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI11 |
| Number of Residues | 38 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | |
| Details | M-CSA 921 |
| site_id | MCSA2 |
| Number of Residues | |
| Details | M-CSA 921 |
