5CGC
Structure of the human class C GPCR metabotropic glutamate receptor 5 transmembrane domain in complex with the negative allosteric modulator 3-chloro-4-fluoro-5-[6-(1H-pyrazol-1-yl)pyrimidin-4-yl]benzonitrile
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 | 6 |
| Details | binding site for residue OLA A 4001 |
| Chain | Residue |
| A | ASN737 |
| A | LEU744 |
| A | GLY748 |
| A | CYS782 |
| A | TRP785 |
| A | PHE793 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue OLA A 4002 |
| Chain | Residue |
| A | OLA4004 |
| A | SER568 |
| A | PRO569 |
| A | VAL570 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue OLA A 4003 |
| Chain | Residue |
| A | TYR645 |
| A | ILE649 |
| A | PHE712 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue OLA A 4004 |
| Chain | Residue |
| A | PHE633 |
| A | ILE636 |
| A | OLA4002 |
| A | HOH4106 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue MES A 4005 |
| Chain | Residue |
| A | TYR730 |
| A | ASN796 |
| A | TYR797 |
| A | LYS798 |
| A | ILE799 |
| A | TYR1139 |
| A | LYS1147 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | binding site for residue 51D A 4006 |
| Chain | Residue |
| A | GLY624 |
| A | ILE625 |
| A | GLY628 |
| A | ILE651 |
| A | SER654 |
| A | PRO655 |
| A | SER658 |
| A | LEU744 |
| A | TRP785 |
| A | SER805 |
| A | VAL806 |
| A | SER809 |
| A | ALA810 |
| A | HOH4126 |
Functional Information from PROSITE/UniProt
| site_id | PS00981 |
| Number of Residues | 11 |
| Details | G_PROTEIN_RECEP_F3_3 G-protein coupled receptors family 3 signature 3. FNEAKyIAFTM |
| Chain | Residue | Details |
| A | PHE768-MET778 |
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 | 22 |
| Details | Transmembrane: {"description":"Helical; Name=1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 21 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"25042998","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical; Name=2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 9 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"25042998","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical; Name=3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=4"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 21 |
| Details | Transmembrane: {"description":"Helical; Name=5"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical; Name=6"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 21 |
| Details | Transmembrane: {"description":"Helical; Name=7"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","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 |
