5YQZ
Structure of the glucagon receptor in complex with a glucagon analogue
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| P | 0005179 | molecular_function | hormone activity |
| P | 0005576 | cellular_component | extracellular region |
| R | 0003796 | molecular_function | lysozyme activity |
| R | 0003824 | molecular_function | catalytic activity |
| R | 0004888 | molecular_function | transmembrane signaling receptor activity |
| R | 0004930 | molecular_function | G protein-coupled receptor activity |
| R | 0007166 | biological_process | cell surface receptor signaling pathway |
| R | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| R | 0008152 | biological_process | metabolic process |
| R | 0009253 | biological_process | peptidoglycan catabolic process |
| R | 0016020 | cellular_component | membrane |
| R | 0016787 | molecular_function | hydrolase activity |
| R | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| R | 0016998 | biological_process | cell wall macromolecule catabolic process |
| R | 0030430 | cellular_component | host cell cytoplasm |
| R | 0031640 | biological_process | killing of cells of another organism |
| R | 0042742 | biological_process | defense response to bacterium |
| R | 0044659 | biological_process | viral release from host cell by cytolysis |
Functional Information from PROSITE/UniProt
| site_id | PS00649 |
| Number of Residues | 25 |
| Details | G_PROTEIN_RECEP_F2_1 G-protein coupled receptors family 2 signature 1. CnrtFDkys.CWpdTpanttanisCP |
| Chain | Residue | Details |
| R | CYS58-PRO82 |
| site_id | PS00650 |
| Number of Residues | 16 |
| Details | G_PROTEIN_RECEP_F2_2 G-protein coupled receptors family 2 signature 2. QGLLVaVLYCFlNkeV |
| Chain | Residue | Details |
| R | GLN392-VAL407 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P55095 |
| Chain | Residue | Details |
| P | SER2 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 34 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451 |
| Chain | Residue | Details |
| R | ILE162-ALA173 | |
| R | GLN327-SER350 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | TRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451 |
| Chain | Residue | Details |
| R | ASN174-LEU198 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 54 |
| Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451 |
| Chain | Residue | Details |
| R | ARG199-ARG225 | |
| R | LYS286-PHE303 | |
| R | ASP370-LYS381 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 23 |
| Details | TRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451 |
| Chain | Residue | Details |
| R | VAL226-LEU249 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 21 |
| Details | TRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451 |
| Chain | Residue | Details |
| R | PHE264-VAL285 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 22 |
| Details | TRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451 |
| Chain | Residue | Details |
| R | TRP304-VAL326 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 18 |
| Details | TRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451 |
| Chain | Residue | Details |
| R | THR351-THR369 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 20 |
| Details | TRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451 |
| Chain | Residue | Details |
| R | LEU382-PHE402 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:28514451 |
| Chain | Residue | Details |
| R | ASN46 | |
| R | ASN59 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22908259, ECO:0000269|PubMed:28514451, ECO:0007744|PDB:4ERS |
| Chain | Residue | Details |
| R | ASN74 | |
| R | ASN78 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| 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 |
| R | GLU1010 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 |
| Chain | Residue | Details |
| R | ASP1019 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:8266098 |
| Chain | Residue | Details |
| R | LEU1031 | |
| R | PHE1103 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000303|PubMed:7831309 |
| Chain | Residue | Details |
| R | SER1116 | |
| R | ASN1131 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 921 |
| Chain | Residue | Details |
| R | GLU1010 | proton shuttle (general acid/base) |
| R | ASP1019 | covalent catalysis |
