4XES
Structure of active-like neurotensin receptor
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 | 0009253 | biological_process | peptidoglycan catabolic process |
A | 0016020 | cellular_component | membrane |
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 | 10 |
Details | binding site for residue CIT A 1201 |
Chain | Residue |
A | ARG299 |
A | SER1165 |
A | ARG1008 |
A | ILE1009 |
A | PHE1114 |
A | THR1115 |
A | ASN1116 |
A | SER1117 |
A | ASN1132 |
A | SER1163 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue PEG A 1202 |
Chain | Residue |
A | CYS172 |
A | LYS263 |
A | LEU1079 |
A | PEG1203 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue PEG A 1203 |
Chain | Residue |
A | LYS263 |
A | MET267 |
A | VAL1075 |
A | TYR1088 |
A | ARG1096 |
A | PEG1202 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue PEG A 1204 |
Chain | Residue |
A | LEU303 |
A | PHE1004 |
A | ASN1068 |
site_id | AC5 |
Number of Residues | 8 |
Details | binding site for residue PEG A 1206 |
Chain | Residue |
A | ARG1080 |
A | ASN1081 |
A | ALA1082 |
A | GLU1108 |
A | THR1109 |
A | TYR1139 |
A | PRO1143 |
A | ASN1144 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue GOL A 1207 |
Chain | Residue |
A | ARG1125 |
B | ARG8 |
site_id | AC7 |
Number of Residues | 1 |
Details | binding site for residue GOL A 1208 |
Chain | Residue |
A | TYR349 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue GOL A 1209 |
Chain | Residue |
A | LYS1083 |
A | THR1142 |
A | PRO1143 |
A | ASN1144 |
A | ARG1145 |
site_id | AC9 |
Number of Residues | 8 |
Details | binding site for residue EPE A 1210 |
Chain | Residue |
A | GLY1030 |
A | HIS1031 |
A | LEU1032 |
A | LYS1035 |
A | ASP1070 |
A | PHE1104 |
A | MET1106 |
A | ASP1159 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue EPE A 1211 |
Chain | Residue |
A | ASP56 |
A | VAL57 |
A | TRP130 |
A | HIS132 |
A | HIS133 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | SITE: Cleavage; by MME => ECO:0000250|UniProtKB:P30990 |
Chain | Residue | Details |
B | PRO10 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | SITE: Cleavage; by ACE and MME => ECO:0000250|UniProtKB:P30990 |
Chain | Residue | Details |
B | TYR11 | |
A | ALA166-ARG185 | |
A | ALA261-LEU308 |
site_id | SWS_FT_FI3 |
Number of Residues | 19 |
Details | TRANSMEM: Helical; Name=2 |
Chain | Residue | Details |
A | TYR104-VAL123 |
site_id | SWS_FT_FI4 |
Number of Residues | 64 |
Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:24453215 |
Chain | Residue | Details |
A | GLU124-ARG143 | |
A | THR207-LYS235 | |
A | PHE331-HIS348 |
site_id | SWS_FT_FI5 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=3 |
Chain | Residue | Details |
A | GLY144-VAL165 |
site_id | SWS_FT_FI6 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=4 |
Chain | Residue | Details |
A | THR186-PHE206 |
site_id | SWS_FT_FI7 |
Number of Residues | 24 |
Details | TRANSMEM: Helical; Name=5 |
Chain | Residue | Details |
A | VAL236-ILE260 |
site_id | SWS_FT_FI8 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=6 |
Chain | Residue | Details |
A | VAL309-MET330 |
site_id | SWS_FT_FI9 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=7 |
Chain | Residue | Details |
A | TYR349-TYR369 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:P30989 |
Chain | Residue | Details |
A | CYS978 | |
A | CYS980 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 |
Chain | Residue | Details |
A | GLU1011 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 |
Chain | Residue | Details |
A | ASP1020 |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8266098 |
Chain | Residue | Details |
A | LEU1032 | |
A | PHE1104 |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000303|PubMed:7831309 |
Chain | Residue | Details |
A | SER1117 | |
A | ASN1132 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 2 |
Details | M-CSA 921 |
Chain | Residue | Details |
A | GLU1011 | proton shuttle (general acid/base) |
A | ASP1020 | covalent catalysis |