5DSG
Structure of the M4 muscarinic acetylcholine receptor (M4-mT4L) bound to tiotropium
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 | 0009253 | biological_process | peptidoglycan catabolic process |
A | 0016020 | cellular_component | membrane |
A | 0016907 | molecular_function | G protein-coupled acetylcholine receptor activity |
A | 0016998 | biological_process | cell wall macromolecule catabolic process |
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 | 0009253 | biological_process | peptidoglycan catabolic process |
B | 0016020 | cellular_component | membrane |
B | 0016907 | molecular_function | G protein-coupled acetylcholine receptor activity |
B | 0016998 | biological_process | cell wall macromolecule catabolic process |
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 | 44 |
Details | TRANSMEM: Helical; Name=1 => ECO:0000250 |
Chain | Residue | Details |
A | MET32-MET54 | |
B | MET32-MET54 |
site_id | SWS_FT_FI2 |
Number of Residues | 64 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000250 |
Chain | Residue | Details |
A | LEU55-ASN68 | |
A | ASP129-MET148 | |
B | LEU55-ASN68 | |
B | ASP129-MET148 |
site_id | SWS_FT_FI3 |
Number of Residues | 40 |
Details | TRANSMEM: Helical; Name=2 => ECO:0000250 |
Chain | Residue | Details |
A | TYR69-TYR89 | |
B | TYR69-TYR89 |
site_id | SWS_FT_FI4 |
Number of Residues | 100 |
Details | TOPO_DOM: Extracellular => ECO:0000250 |
Chain | Residue | Details |
A | THR90-ASP106 | |
A | GLN172-PRO193 | |
A | ASN423-SER436 | |
B | THR90-ASP106 | |
B | GLN172-PRO193 | |
B | ASN423-SER436 |
site_id | SWS_FT_FI5 |
Number of Residues | 42 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000250 |
Chain | Residue | Details |
A | LEU107-PHE128 | |
B | LEU107-PHE128 |
site_id | SWS_FT_FI6 |
Number of Residues | 44 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000250 |
Chain | Residue | Details |
A | ALA149-TRP171 | |
B | ALA149-TRP171 |
site_id | SWS_FT_FI7 |
Number of Residues | 44 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000250 |
Chain | Residue | Details |
A | ALA194-ILE216 | |
B | ALA194-ILE216 |
site_id | SWS_FT_FI8 |
Number of Residues | 40 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000250 |
Chain | Residue | Details |
A | ILE402-VAL422 | |
B | ILE402-VAL422 |
site_id | SWS_FT_FI9 |
Number of Residues | 38 |
Details | TRANSMEM: Helical; Name=7 => ECO:0000250 |
Chain | Residue | Details |
A | ILE437-CYS456 | |
B | ILE437-CYS456 |
site_id | SWS_FT_FI10 |
Number of Residues | 6 |
Details | MOD_RES: Phosphothreonine => ECO:0000255 |
Chain | Residue | Details |
A | THR459 | |
A | THR463 | |
A | THR477 | |
B | THR459 | |
B | THR463 | |
B | THR477 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
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 |
B | GLU1011 | |
A | GLU1011 |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8266098 |
Chain | Residue | Details |
A | PHE1061 | |
B | PHE1061 |
site_id | SWS_FT_FI13 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000303|PubMed:7831309 |
Chain | Residue | Details |
A | SER1074 | |
A | ASN1089 | |
B | SER1074 | |
B | ASN1089 |