4L6R
Structure of the class B human glucagon G protein coupled receptor
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004888 | molecular_function | transmembrane signaling receptor activity |
A | 0004930 | molecular_function | G protein-coupled receptor activity |
A | 0004967 | molecular_function | glucagon receptor activity |
A | 0005506 | molecular_function | iron ion binding |
A | 0007166 | biological_process | cell surface receptor signaling pathway |
A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
A | 0009055 | molecular_function | electron transfer activity |
A | 0016020 | cellular_component | membrane |
A | 0020037 | molecular_function | heme binding |
A | 0022900 | biological_process | electron transport chain |
A | 0042597 | cellular_component | periplasmic space |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PEG A 1200 |
Chain | Residue |
A | ARG346 |
A | SER350 |
A | LEU399 |
A | LEU403 |
Functional Information from PROSITE/UniProt
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 |
A | GLN392-VAL407 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
A | TRP1007 | |
A | ILE1102 |
site_id | SWS_FT_FI2 |
Number of Residues | 24 |
Details | TRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451 |
Chain | Residue | Details |
A | MET137-ALA161 |
site_id | SWS_FT_FI3 |
Number of Residues | 47 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451 |
Chain | Residue | Details |
A | ILE162-ARG173 | |
A | HIS250-PHE263 | |
A | GLN327-SER350 |
site_id | SWS_FT_FI4 |
Number of Residues | 24 |
Details | TRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451 |
Chain | Residue | Details |
A | ASN174-LEU198 |
site_id | SWS_FT_FI5 |
Number of Residues | 54 |
Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451 |
Chain | Residue | Details |
A | ARG199-ARG225 | |
A | LYS286-PHE303 | |
A | ASP370-LYS381 |
site_id | SWS_FT_FI6 |
Number of Residues | 23 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451 |
Chain | Residue | Details |
A | VAL226-LEU249 |
site_id | SWS_FT_FI7 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451 |
Chain | Residue | Details |
A | PHE264-VAL285 |
site_id | SWS_FT_FI8 |
Number of Residues | 22 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451 |
Chain | Residue | Details |
A | TRP304-VAL326 |
site_id | SWS_FT_FI9 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451 |
Chain | Residue | Details |
A | THR351-THR369 |
site_id | SWS_FT_FI10 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451 |
Chain | Residue | Details |
A | LEU382-PHE402 |