4DJH
Structure of the human kappa opioid receptor in complex with JDTic
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 |
B | 0003796 | molecular_function | lysozyme activity |
B | 0003824 | molecular_function | catalytic activity |
B | 0004930 | molecular_function | G protein-coupled receptor activity |
B | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
B | 0009253 | biological_process | peptidoglycan catabolic process |
B | 0016020 | cellular_component | membrane |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
B | 0016998 | biological_process | cell wall macromolecule catabolic process |
B | 0030430 | cellular_component | host cell cytoplasm |
B | 0031640 | biological_process | killing of cells of another organism |
B | 0042742 | biological_process | defense response to bacterium |
B | 0044659 | biological_process | viral release from host cell by cytolysis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE JDC A 1300 |
Chain | Residue |
A | THR111 |
A | ILE294 |
A | ILE316 |
A | TYR320 |
A | HOH1303 |
A | HOH1304 |
A | GLN115 |
A | VAL134 |
A | ASP138 |
A | TYR139 |
A | LYS227 |
A | VAL230 |
A | TRP287 |
A | ILE290 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CIT A 1301 |
Chain | Residue |
A | GLY1012 |
A | ARG1014 |
A | TYR1018 |
A | HOH1308 |
site_id | AC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE JDC B 1300 |
Chain | Residue |
B | THR111 |
B | GLN115 |
B | LEU135 |
B | ASP138 |
B | MET142 |
B | CYS210 |
B | LYS227 |
B | VAL230 |
B | TRP287 |
B | ILE294 |
B | ILE316 |
B | TYR320 |
B | HOH1307 |
B | HOH1313 |
B | HOH1314 |
B | HOH1316 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE OLC B 1302 |
Chain | Residue |
A | TRP221 |
B | TYR97 |
B | ASP155 |
B | ILE158 |
B | PHE169 |
B | LYS174 |
B | ILE178 |
B | CYS181 |
B | OLC1303 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE OLC B 1303 |
Chain | Residue |
A | GLY300 |
A | SER301 |
B | TYR157 |
B | HIS162 |
B | PRO163 |
B | VAL164 |
B | OLC1302 |
site_id | AC6 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE PEG B 1304 |
Chain | Residue |
B | LEU299 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PEG B 1305 |
Chain | Residue |
A | PRO1037 |
A | SER1038 |
A | LEU1039 |
B | THR92 |
B | THR94 |
B | ARG270 |
B | ILE272 |
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. TSIfTLTMMSVDRYIaV |
Chain | Residue | Details |
A | THR144-VAL160 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1892846","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000303"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 54 |
Details | Transmembrane: {"description":"Helical; Name=1"} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 54 |
Details | Topological domain: {"description":"Cytoplasmic"} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 46 |
Details | Transmembrane: {"description":"Helical; Name=2"} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 74 |
Details | Topological domain: {"description":"Extracellular"} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 42 |
Details | Transmembrane: {"description":"Helical; Name=3"} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 44 |
Details | Transmembrane: {"description":"Helical; Name=4"} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 48 |
Details | Transmembrane: {"description":"Helical; Name=5"} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 42 |
Details | Transmembrane: {"description":"Helical; Name=6"} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 42 |
Details | Transmembrane: {"description":"Helical; Name=7"} |
Chain | Residue | Details |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |