5CXV
Structure of the human M1 muscarinic acetylcholine receptor bound to antagonist Tiotropium
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 | 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 | 0016787 | molecular_function | hydrolase activity |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0016907 | molecular_function | G protein-coupled acetylcholine receptor activity |
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 | 0040012 | biological_process | regulation of locomotion |
A | 0042742 | biological_process | defense response to bacterium |
A | 0044659 | biological_process | viral release from host cell by cytolysis |
A | 0046541 | biological_process | saliva secretion |
A | 0050890 | biological_process | cognition |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 15 |
Details | binding site for residue 0HK A 501 |
Chain | Residue |
A | ASP105 |
A | TRP378 |
A | TYR381 |
A | ASN382 |
A | TYR404 |
A | CYS407 |
A | TYR408 |
A | TYR106 |
A | SER109 |
A | TRP157 |
A | THR189 |
A | THR192 |
A | ALA193 |
A | ALA196 |
A | PHE197 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue Y01 A 502 |
Chain | Residue |
A | TRP23 |
A | PHE50 |
A | LYS57 |
A | TYR62 |
A | LEU65 |
A | TRP150 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue EDO A 503 |
Chain | Residue |
A | GLN165 |
A | GLY169 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue PGE A 504 |
Chain | Residue |
A | ILE119 |
A | ARG123 |
A | GLU360 |
C | ASP1 |
C | TYR2 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue EDO A 505 |
Chain | Residue |
A | GLU1010 |
A | GOL506 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue GOL A 506 |
Chain | Residue |
A | GLY1029 |
A | LEU1031 |
A | ASP1069 |
A | PHE1103 |
A | EDO505 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue EDO A 507 |
Chain | Residue |
A | THR1141 |
A | PRO1142 |
A | ASN1143 |
A | ARG1144 |
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. ASVmNLLLISFDRYFsV |
Chain | Residue | Details |
A | ALA111-VAL127 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
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 | 1 |
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 | 2 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000303"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 25 |
Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"32646996","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WJC","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 33 |
Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"32646996","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WJC","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 21 |
Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"32646996","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WJC","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 36 |
Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"32646996","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WJC","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 25 |
Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"32646996","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WJC","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 21 |
Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"32646996","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WJC","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 23 |
Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"32646996","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WJC","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 23 |
Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"32646996","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WJC","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 22 |
Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"32646996","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WJC","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI14 |
Number of Residues | 9 |
Details | Compositional bias: {"description":"Low complexity","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI15 |
Number of Residues | 4 |
Details | Site: {"description":"Subtype-specific residue that binds to snake venom muscarinic toxin 7","evidences":[{"source":"PubMed","id":"32646996","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI16 |
Number of Residues | 1 |
Details | Site: {"description":"Binds to snake venom muscarinic toxin 7","evidences":[{"source":"PubMed","id":"32646996","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI17 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P12657","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI18 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 2 |
Details | M-CSA 921 |
Chain | Residue | Details |
A | GLU1010 | proton shuttle (general acid/base) |
A | ASP1019 | covalent catalysis |