8IQ4
Cryo-EM structure of Carboprost-bound prostaglandin-F2-alpha receptor-miniGq-Nb35 complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003924 | molecular_function | GTPase activity |
A | 0005525 | molecular_function | GTP binding |
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 | 0007165 | biological_process | signal transduction |
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 | 0004958 | molecular_function | prostaglandin F receptor activity |
R | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
R | 0016020 | cellular_component | membrane |
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. CPLlLGSVMAIERCIgV |
Chain | Residue | Details |
R | CYS121-VAL137 |
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 | MOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378 |
Chain | Residue | Details |
G | ALA2 | |
A | SER54 | |
A | THR204 | |
A | ASP223 | |
A | LEU302 | |
A | PHE376 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: Cysteine methyl ester => ECO:0000250|UniProtKB:P63212 |
Chain | Residue | Details |
G | CYS68 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | LIPID: S-geranylgeranyl cysteine => ECO:0000250|UniProtKB:P63212 |
Chain | Residue | Details |
G | CYS68 | |
R | GLU132-VAL152 | |
R | ILE225-GLN250 | |
R | ARG308-THR359 |
site_id | SWS_FT_FI4 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=2 => ECO:0000255 |
Chain | Residue | Details |
R | ALA70-PHE90 |
site_id | SWS_FT_FI5 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000255 |
Chain | Residue | Details |
R | ILE110-ILE131 |
site_id | SWS_FT_FI6 |
Number of Residues | 22 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000255 |
Chain | Residue | Details |
R | LYS153-ARG175 |
site_id | SWS_FT_FI7 |
Number of Residues | 25 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000255 |
Chain | Residue | Details |
R | ARG199-GLY224 |
site_id | SWS_FT_FI8 |
Number of Residues | 16 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000255 |
Chain | Residue | Details |
R | LEU251-VAL267 |
site_id | SWS_FT_FI9 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=7 => ECO:0000255 |
Chain | Residue | Details |
R | THR286-LEU307 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
R | ASN4 | |
R | ASN19 |