9LRC
Cryo-EM structure of the histamine H4 receptor-Gi protein complex (Receptor focused)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| R | 0004930 | molecular_function | G protein-coupled receptor activity |
| R | 0004969 | molecular_function | histamine receptor activity |
| R | 0005886 | cellular_component | plasma membrane |
| R | 0006091 | biological_process | generation of precursor metabolites and energy |
| R | 0007165 | biological_process | signal transduction |
| R | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| R | 0007187 | biological_process | G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger |
| R | 0007193 | biological_process | adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway |
| R | 0007197 | biological_process | adenylate cyclase-inhibiting G protein-coupled acetylcholine receptor signaling pathway |
| R | 0007268 | biological_process | chemical synaptic transmission |
| R | 0008218 | biological_process | bioluminescence |
| R | 0016020 | cellular_component | membrane |
| R | 0030425 | cellular_component | dendrite |
| R | 0030594 | molecular_function | neurotransmitter receptor activity |
| R | 0045202 | cellular_component | synapse |
Functional Information from PROSITE/UniProt
| site_id | PS00237 |
| Number of Residues | 17 |
| Details | G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASVyNIVLISYDRYLsV |
| Chain | Residue | Details |
| R | ALA100-VAL116 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 33 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 47 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
