6FFI
Crystal Structure of mGluR5 in complex with MMPEP at 2.2 A
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 | 7 |
Details | binding site for residue OLA A 4001 |
Chain | Residue |
A | ASN897 |
A | VAL901 |
A | LEU904 |
A | LEU912 |
A | CYS942 |
A | TRP945 |
A | PHE953 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue OLA A 4002 |
Chain | Residue |
A | VAL570 |
A | OLA4004 |
A | SER568 |
A | PRO569 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue OLA A 4003 |
Chain | Residue |
A | TYR645 |
A | ILE649 |
A | PHE872 |
A | ILE873 |
A | OLA4005 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue OLA A 4004 |
Chain | Residue |
A | PRO569 |
A | CYS588 |
A | ILE636 |
A | OLA4002 |
A | HOH4130 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue OLA A 4005 |
Chain | Residue |
A | TYR645 |
A | OLA4003 |
site_id | AC6 |
Number of Residues | 9 |
Details | binding site for residue MES A 4006 |
Chain | Residue |
A | TYR816 |
A | TYR890 |
A | ASN956 |
A | TYR957 |
A | LYS958 |
A | ILE959 |
A | HOH4105 |
A | HOH4176 |
A | HOH4182 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue OLA A 4007 |
Chain | Residue |
A | ARG574 |
A | ILE581 |
site_id | AC8 |
Number of Residues | 1 |
Details | binding site for residue OLA A 4008 |
Chain | Residue |
A | THR598 |
site_id | AC9 |
Number of Residues | 10 |
Details | binding site for residue D8B A 4009 |
Chain | Residue |
A | GLY624 |
A | SER654 |
A | PRO655 |
A | SER658 |
A | TYR659 |
A | ILE944 |
A | TRP945 |
A | PHE948 |
A | SER965 |
A | SER969 |
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 | PHE928-MET938 |
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 | 9 |
Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"25042998","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 22 |
Details | Transmembrane: {"description":"Helical; Name=3"} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=4"} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 21 |
Details | Transmembrane: {"description":"Helical; Name=5"} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 22 |
Details | Transmembrane: {"description":"Helical; Name=6"} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 21 |
Details | Transmembrane: {"description":"Helical; Name=7"} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
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 | LEU692 | proton shuttle (general acid/base) |
A | TYR701 | covalent catalysis |