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 | 22 |
Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 13 |
Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Binding site: {"description":"axial binding residue"} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 24 |
Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"23863937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27111510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28514451","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 47 |
Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"23863937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27111510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28514451","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 24 |
Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"23863937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27111510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28514451","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 23 |
Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"23863937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27111510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28514451","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 21 |
Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"23863937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27111510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28514451","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 28 |
Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"23863937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27111510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28514451","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 22 |
Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"23863937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27111510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28514451","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 18 |
Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"23863937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27111510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28514451","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"23863937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27111510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28514451","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 3 |
Details | Region: {"description":"Important for allosteric inhibitor binding","evidences":[{"source":"PubMed","id":"27111510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28514451","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |