7DFL
Cryo-EM structure of histamine H1 receptor Gq complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001664 | molecular_function | G protein-coupled receptor binding |
A | 0003924 | molecular_function | GTPase activity |
A | 0007165 | biological_process | signal transduction |
A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
A | 0019001 | molecular_function | guanyl nucleotide binding |
A | 0031683 | molecular_function | G-protein beta/gamma-subunit complex binding |
B | 0001750 | cellular_component | photoreceptor outer segment |
B | 0003924 | molecular_function | GTPase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005765 | cellular_component | lysosomal membrane |
B | 0005829 | cellular_component | cytosol |
B | 0005834 | cellular_component | heterotrimeric G-protein complex |
B | 0005886 | cellular_component | plasma membrane |
B | 0007165 | biological_process | signal transduction |
B | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
B | 0007191 | biological_process | adenylate cyclase-activating dopamine receptor signaling pathway |
B | 0007200 | biological_process | phospholipase C-activating G protein-coupled receptor signaling pathway |
B | 0007213 | biological_process | G protein-coupled acetylcholine receptor signaling pathway |
B | 0007265 | biological_process | Ras protein signal transduction |
B | 0008283 | biological_process | cell population proliferation |
B | 0016020 | cellular_component | membrane |
B | 0030159 | molecular_function | signaling receptor complex adaptor activity |
B | 0044877 | molecular_function | protein-containing complex binding |
B | 0045202 | cellular_component | synapse |
B | 0050909 | biological_process | sensory perception of taste |
B | 0051020 | molecular_function | GTPase binding |
B | 0060041 | biological_process | retina development in camera-type eye |
B | 0070062 | cellular_component | extracellular exosome |
B | 0071380 | biological_process | cellular response to prostaglandin E stimulus |
B | 0071870 | biological_process | cellular response to catecholamine stimulus |
B | 0097381 | cellular_component | photoreceptor disc membrane |
B | 1903561 | cellular_component | extracellular vesicle |
G | 0005834 | cellular_component | heterotrimeric G-protein complex |
G | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
G | 0031681 | molecular_function | G-protein beta-subunit binding |
R | 0004930 | molecular_function | G protein-coupled receptor activity |
R | 0004969 | molecular_function | histamine receptor activity |
R | 0005829 | cellular_component | cytosol |
R | 0005886 | cellular_component | plasma membrane |
R | 0006954 | biological_process | inflammatory response |
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 | 0007200 | biological_process | phospholipase C-activating G protein-coupled receptor signaling pathway |
R | 0007208 | biological_process | phospholipase C-activating serotonin receptor signaling pathway |
R | 0007268 | biological_process | chemical synaptic transmission |
R | 0007613 | biological_process | memory |
R | 0008542 | biological_process | visual learning |
R | 0016020 | cellular_component | membrane |
R | 0030425 | cellular_component | dendrite |
R | 0043114 | biological_process | regulation of vascular permeability |
R | 0045202 | cellular_component | synapse |
R | 0045907 | biological_process | positive regulation of vasoconstriction |
R | 0048167 | biological_process | regulation of synaptic plasticity |
R | 0071420 | biological_process | cellular response to histamine |
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. ASIfSVFILCIDRYRsV |
Chain | Residue | Details |
R | ALA113-VAL129 |
site_id | PS00678 |
Number of Residues | 15 |
Details | WD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS |
Chain | Residue | Details |
B | LEU70-SER84 | |
B | ILE157-ILE171 | |
B | LEU285-ALA299 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:P10824 |
Chain | Residue | Details |
A | CYS3 | |
R | MET90-ARG97 | |
R | TRP165-THR188 | |
R | CYS441-ASN446 |
site_id | SWS_FT_FI2 |
Number of Residues | 14 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P21279 |
Chain | Residue | Details |
A | SER50 | |
A | THR186 | |
A | ASN274 | |
A | LYS275 | |
A | ASP277 | |
A | ALA331 | |
A | GLY51 | |
A | LYS52 | |
A | SER53 | |
A | THR54 | |
A | SER156 | |
A | LEU180 | |
A | ARG181 | |
A | ARG183 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Deamidated glutamine; by Photorhabdus PAU_02230 => ECO:0000269|PubMed:24141704 |
Chain | Residue | Details |
A | GLN209 | |
R | ASP124-ALA144 | |
R | LYS212-GLN416 | |
R | LEU470-SER487 |
site_id | SWS_FT_FI4 |
Number of Residues | 24 |
Details | TRANSMEM: Helical; Name=2 => ECO:0000305|PubMed:33828102, ECO:0007744|PDB:7DFL |
Chain | Residue | Details |
R | TYR65-LEU89 |
site_id | SWS_FT_FI5 |
Number of Residues | 25 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000305|PubMed:33828102, ECO:0007744|PDB:7DFL |
Chain | Residue | Details |
R | PRO98-ILE123 |
site_id | SWS_FT_FI6 |
Number of Residues | 19 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000305|PubMed:33828102, ECO:0007744|PDB:7DFL |
Chain | Residue | Details |
R | SER145-GLY164 |
site_id | SWS_FT_FI7 |
Number of Residues | 22 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000305|PubMed:33828102, ECO:0007744|PDB:7DFL |
Chain | Residue | Details |
R | TRP189-ALA211 |
site_id | SWS_FT_FI8 |
Number of Residues | 23 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000305|PubMed:33828102, ECO:0007744|PDB:7DFL |
Chain | Residue | Details |
R | LEU417-PHE440 |
site_id | SWS_FT_FI9 |
Number of Residues | 22 |
Details | TRANSMEM: Helical; Name=7 => ECO:0000305|PubMed:33828102, ECO:0007744|PDB:7DFL |
Chain | Residue | Details |
R | GLU447-PRO469 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000305|PubMed:33828102 |
Chain | Residue | Details |
R | ASP107 | |
R | ASN198 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:33828102, ECO:0007744|PDB:7DFL |
Chain | Residue | Details |
R | THR112 | |
R | TYR431 |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:15328002 |
Chain | Residue | Details |
R | THR140 | |
R | THR142 |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
R | SER230 |
site_id | SWS_FT_FI14 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648 |
Chain | Residue | Details |
R | THR279 |
site_id | SWS_FT_FI15 |
Number of Residues | 3 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P70174 |
Chain | Residue | Details |
R | SER344 | |
R | SER347 | |
R | SER380 |
site_id | SWS_FT_FI16 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:15328002 |
Chain | Residue | Details |
R | SER396 | |
R | SER398 |
site_id | SWS_FT_FI17 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
R | ASN5 | |
R | ASN18 |