7F61
Crystal structure of human histamine receptor H3R in complex with antagonist PF03654746
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004930 | molecular_function | G protein-coupled receptor activity |
A | 0004969 | molecular_function | histamine receptor activity |
A | 0004993 | molecular_function | G protein-coupled serotonin receptor activity |
A | 0005886 | cellular_component | plasma membrane |
A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
A | 0007187 | biological_process | G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger |
A | 0007197 | biological_process | adenylate cyclase-inhibiting G protein-coupled acetylcholine receptor signaling pathway |
A | 0007268 | biological_process | chemical synaptic transmission |
A | 0007269 | biological_process | neurotransmitter secretion |
A | 0016020 | cellular_component | membrane |
A | 0016907 | molecular_function | G protein-coupled acetylcholine receptor activity |
A | 0030425 | cellular_component | dendrite |
A | 0045202 | cellular_component | synapse |
A | 0098664 | biological_process | G protein-coupled serotonin receptor signaling pathway |
A | 0098793 | cellular_component | presynapse |
B | 0005506 | molecular_function | iron ion binding |
B | 0009055 | molecular_function | electron transfer activity |
B | 0020037 | molecular_function | heme binding |
B | 0022900 | biological_process | electron transport chain |
B | 0042597 | cellular_component | periplasmic space |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
B | TRP7 | |
B | ILE102 |
site_id | SWS_FT_FI2 |
Number of Residues | 176 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
Chain | Residue | Details |
A | ALA61-ASN70 | |
A | TYR130-MET156 | |
A | ASN218-SER359 |
site_id | SWS_FT_FI3 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=2 => ECO:0000255 |
Chain | Residue | Details |
A | PHE71-TYR91 |
site_id | SWS_FT_FI4 |
Number of Residues | 48 |
Details | TOPO_DOM: Extracellular => ECO:0000255 |
Chain | Residue | Details |
A | VAL92-LYS108 | |
A | SER178-TRP196 | |
A | ARG381-GLU395 |
site_id | SWS_FT_FI5 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000255 |
Chain | Residue | Details |
A | LEU109-SER129 |
site_id | SWS_FT_FI6 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000255 |
Chain | Residue | Details |
A | LEU157-LEU177 |
site_id | SWS_FT_FI7 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000255 |
Chain | Residue | Details |
A | TYR197-PHE217 |
site_id | SWS_FT_FI8 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000255 |
Chain | Residue | Details |
A | LEU360-ILE380 |
site_id | SWS_FT_FI9 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=7 => ECO:0000255 |
Chain | Residue | Details |
A | THR396-HIS416 |