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 | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| A | 0016020 | cellular_component | membrane |
| A | 0016998 | biological_process | cell wall macromolecule catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | binding site for residue D2U A 1201 |
| Chain | Residue |
| A | ASP147 |
| A | VAL185 |
| A | THR188 |
| A | PHE240 |
| A | TYR281 |
| A | TRP336 |
| A | LEU339 |
| A | ARG343 |
| A | ALA375 |
| A | ASN378 |
| A | SER379 |
| A | HIS150 |
| A | HOH1311 |
| A | ASN158 |
| A | LYS161 |
| A | VAL177 |
| A | PRO178 |
| A | GLN181 |
| A | LYS182 |
| A | SER184 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 A 1202 |
| Chain | Residue |
| A | ILE1003 |
| A | TYR1038 |
| A | ALA1043 |
| A | ARG1046 |
| A | ILE1050 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 A 1203 |
| Chain | Residue |
| A | CYS131 |
| A | ARG392 |
| A | ASN395 |
| A | HOH1313 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 A 1204 |
| Chain | Residue |
| A | ASN312 |
| A | ASP313 |
| A | ASP1010 |
| A | ARG1095 |
| A | ARG1098 |
| A | HOH1301 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | binding site for residue PO4 A 1205 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue OLC A 1206 |
| Chain | Residue |
| A | GLU98 |
| A | LYS101 |
| A | TYR102 |
| A | LEU163 |
| A | LEU232 |
| A | THR263 |
| A | PHE265 |
| A | TYR269 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue OLC A 1207 |
| Chain | Residue |
| A | TRP275 |
| A | SER279 |
| A | OLC1208 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue OLC A 1208 |
| Chain | Residue |
| A | TYR102 |
| A | ALA264 |
| A | PHE268 |
| A | OLC1207 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue OLC A 1209 |
| Chain | Residue |
| A | ILE117 |
| A | LEU145 |
| A | TRP226 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue OLC A 1210 |
| Chain | Residue |
| A | LYS323 |
| A | VAL331 |
| A | ALA381 |
| A | LEU388 |
| A | VAL389 |
| A | LYS391 |
| A | OLC1211 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue OLC A 1211 |
| Chain | Residue |
| A | ALA290 |
| A | PHE326 |
| A | LEU330 |
| A | VAL331 |
| A | LEU334 |
| A | OLC1210 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue OLC A 1212 |
| Chain | Residue |
| A | ILE96 |
| A | MET374 |
| A | LEU377 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue OLC A 1213 |
| Chain | Residue |
| A | PHE112 |
| A | LEU149 |
| A | VAL159 |
| A | ALA183 |
| A | VAL230 |
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. ITVlSLCALSIDRYRaV |
| Chain | Residue | Details |
| A | ILE187-VAL203 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000303"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 25 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 49 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 21 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 24 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 24 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 25 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI11 |
| Number of Residues | 26 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P28088","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"9261180","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | |
| Details | M-CSA 921 |
