6W2X
CryoEM Structure of Inactive GABAB Heterodimer
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004930 | molecular_function | G protein-coupled receptor activity |
A | 0004965 | molecular_function | G protein-coupled GABA receptor activity |
A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
A | 0016020 | cellular_component | membrane |
B | 0004888 | molecular_function | transmembrane signaling receptor activity |
B | 0004930 | molecular_function | G protein-coupled receptor activity |
B | 0004965 | molecular_function | G protein-coupled GABA receptor activity |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005886 | cellular_component | plasma membrane |
B | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
B | 0007193 | biological_process | adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway |
B | 0007194 | biological_process | negative regulation of adenylate cyclase activity |
B | 0007214 | biological_process | gamma-aminobutyric acid signaling pathway |
B | 0007268 | biological_process | chemical synaptic transmission |
B | 0016020 | cellular_component | membrane |
B | 0038039 | cellular_component | G protein-coupled receptor heterodimeric complex |
B | 0043005 | cellular_component | neuron projection |
B | 0045202 | cellular_component | synapse |
B | 0045211 | cellular_component | postsynaptic membrane |
B | 0046982 | molecular_function | protein heterodimerization activity |
B | 0051932 | biological_process | synaptic transmission, GABAergic |
B | 0150099 | biological_process | neuron-glial cell signaling |
B | 1902710 | cellular_component | GABA receptor complex |
B | 1902712 | cellular_component | G protein-coupled GABA receptor complex |
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. LNDSKyIGMSV |
Chain | Residue | Details |
B | LEU686-VAL696 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 490 |
Details | TOPO_DOM: Extracellular => ECO:0000255 |
Chain | Residue | Details |
B | TRP42-SER483 | |
B | VAL544-THR551 | |
B | ASP619-THR654 | |
B | THR713-GLN720 |
site_id | SWS_FT_FI2 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=1 => ECO:0000255 |
Chain | Residue | Details |
B | ILE484-ILE504 | |
A | HIS572-LEU593 | |
A | GLU673-ALA687 | |
A | PRO738-LYS844 |
site_id | SWS_FT_FI3 |
Number of Residues | 255 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
Chain | Residue | Details |
B | LYS505-LEU522 | |
B | ALA573-LEU597 | |
B | TRP676-TYR691 | |
B | PRO742-LEU941 |
site_id | SWS_FT_FI4 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=2 => ECO:0000255 |
Chain | Residue | Details |
B | ILE523-PHE543 | |
A | ASP615-THR651 | |
A | LEU709-ALA716 |
site_id | SWS_FT_FI5 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000255 |
Chain | Residue | Details |
B | LEU552-PHE572 |
site_id | SWS_FT_FI6 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000255 |
Chain | Residue | Details |
B | LEU598-VAL618 |
site_id | SWS_FT_FI7 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000255 |
Chain | Residue | Details |
B | ILE655-ALA675 |
site_id | SWS_FT_FI8 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000255 |
Chain | Residue | Details |
B | ILE692-LEU712 |
site_id | SWS_FT_FI9 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=7 => ECO:0000255 |
Chain | Residue | Details |
B | PHE721-VAL741 |
site_id | SWS_FT_FI10 |
Number of Residues | 8 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q80T41 |
Chain | Residue | Details |
B | SER776 | |
B | SER779 | |
B | SER884 | |
B | SER893 | |
B | SER913 | |
B | SER916 | |
B | SER920 | |
B | SER924 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q80T41 |
Chain | Residue | Details |
B | THR819 |
site_id | SWS_FT_FI12 |
Number of Residues | 3 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22660477 |
Chain | Residue | Details |
B | ASN90 | |
B | ASN389 | |
B | ASN453 |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
B | ASN298 | |
A | THR813 |
site_id | SWS_FT_FI14 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22660477, ECO:0000269|PubMed:24305054 |
Chain | Residue | Details |
B | ASN404 | |
A | ASN292 | |
A | ASN385 | |
A | ASN397 |
site_id | SWS_FT_FI15 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:24305054 |
Chain | Residue | Details |
A | ASN323 | |
A | ASN365 |