5ZTY
Crystal structure of human G protein coupled receptor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003796 | molecular_function | lysozyme activity |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004930 | molecular_function | G protein-coupled receptor activity |
| A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| A | 0009253 | biological_process | peptidoglycan catabolic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0016998 | biological_process | cell wall macromolecule catabolic process |
| A | 0030430 | cellular_component | host cell cytoplasm |
| A | 0031640 | biological_process | killing of cells of another organism |
| A | 0042742 | biological_process | defense response to bacterium |
| A | 0044659 | biological_process | viral release from host cell by cytolysis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue 9JU A 1201 |
| Chain | Residue |
| A | PHE87 |
| A | SER90 |
| A | THR114 |
| A | PHE117 |
| A | PHE183 |
| A | ILE186 |
| A | LEU262 |
| A | MET265 |
| A | SER285 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue OLA A 1202 |
| Chain | Residue |
| A | LEU151 |
| A | TRP158 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue OLC A 1203 |
| Chain | Residue |
| A | THR146 |
| A | GLY148 |
| A | LYS245 |
| A | GLY248 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue OLC A 1204 |
| Chain | Residue |
| A | PHE259 |
| A | ALA263 |
| A | ALA266 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue OLC A 1205 |
| Chain | Residue |
| A | LEU255 |
| A | PHE259 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue PEG A 1206 |
| Chain | Residue |
| A | GLY1029 |
| A | LEU1031 |
| A | PHE1103 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue PEG A 1207 |
| Chain | Residue |
| A | TYR132 |
| A | TYR207 |
| A | THR208 |
| A | HIS211 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue EPE A 1208 |
| Chain | Residue |
| A | LYS1042 |
| A | ASN1054 |
| A | ARG1075 |
| A | ARG1079 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | binding site for residue PG4 A 1210 |
| Chain | Residue |
| A | LYS1015 |
| A | ARG1051 |
| A | GLU1061 |
| A | LYS1064 |
| A | ASP1071 |
| A | ALA1092 |
| A | ARG1095 |
| A | ALA1096 |
| A | ILE1099 |
| A | SO41213 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 1211 |
| Chain | Residue |
| A | THR1141 |
| A | PRO1142 |
| A | ASN1143 |
| A | ARG1144 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 1212 |
| Chain | Residue |
| A | PHE1113 |
| A | THR1114 |
| A | ASN1115 |
| A | SER1116 |
| A | ASN1131 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 1213 |
| Chain | Residue |
| A | ARG1013 |
| A | LEU1014 |
| A | LYS1015 |
| A | LYS1064 |
| A | PG41210 |
| A | HOH1311 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 1214 |
| Chain | Residue |
| A | ARG1007 |
| A | LYS1059 |
| A | HOH1304 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 1215 |
| Chain | Residue |
| A | ARG1007 |
| A | LEU1012 |
| A | ARG1013 |
| A | HOH1319 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI2 |
| Number of Residues | 25 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 30 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 37 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 24 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 25 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 21 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
