6ZG9
Structure of M1-StaR-T4L in complex with GSK1034702 at 2.5A
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 | 11 |
| Details | binding site for residue QK2 A 1201 |
| Chain | Residue |
| A | TYR82 |
| A | TYR408 |
| A | HOH1313 |
| A | TYR85 |
| A | TRP91 |
| A | LEU102 |
| A | ASP105 |
| A | SER109 |
| A | CYS178 |
| A | TRP378 |
| A | TYR404 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue EPE A 1202 |
| Chain | Residue |
| A | TYR179 |
| A | LEU183 |
| A | PRO186 |
| A | THR189 |
| A | SER388 |
| A | GLU397 |
| A | TYR404 |
| A | HOH1304 |
| A | HOH1307 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue OLA A 1203 |
| Chain | Residue |
| A | GLN57 |
| A | PHE65 |
| A | ILE73 |
| A | LEU143 |
| A | ILE146 |
| A | TRP150 |
| A | OLA1204 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue OLA A 1204 |
| Chain | Residue |
| A | LEU104 |
| A | VAL107 |
| A | LEU143 |
| A | ILE146 |
| A | GLY147 |
| A | PHE154 |
| A | CYS394 |
| A | OLA1203 |
| A | OLA1207 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue OLA A 1205 |
| Chain | Residue |
| A | GLU24 |
| A | GLU401 |
| A | TRP405 |
| A | OLA1208 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | binding site for residue OLA A 1206 |
| Chain | Residue |
| A | LEU93 |
| A | GLY94 |
| A | ALA95 |
| A | LEU96 |
| A | ALA97 |
| A | ALA175 |
| A | CYS205 |
| A | TYR208 |
| A | TRP209 |
| A | TYR212 |
| A | OLA1207 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue OLA A 1207 |
| Chain | Residue |
| A | HIS90 |
| A | TRP91 |
| A | ALA92 |
| A | LEU93 |
| A | ALA97 |
| A | LEU100 |
| A | OLA1204 |
| A | OLA1206 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue OLA A 1208 |
| Chain | Residue |
| A | LEU144 |
| A | THR398 |
| A | OLA1205 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 A 1209 |
| Chain | Residue |
| A | ARG129 |
| A | LEU131 |
| A | SER132 |
| A | ASP1072 |
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. AAVmNLLLISFDRYFsV |
| 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 | 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_FI6 |
| 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_FI7 |
| 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_FI8 |
| 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_FI9 |
| 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_FI10 |
| 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_FI11 |
| 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_FI12 |
| 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_FI13 |
| Number of Residues | 41 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| 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 | 15 |
| Details | Compositional bias: {"description":"Basic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| 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_FI17 |
| 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_FI18 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P12657","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| 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 | GLU1011 | proton shuttle (general acid/base) |
| A | ASP1020 | covalent catalysis |






