6IBB
Crystal structure of the rat isoform of the succinate receptor SUCNR1 (GPR91) in complex with a nanobody
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0002001 | biological_process | renin secretion into blood stream |
A | 0002281 | biological_process | macrophage activation involved in immune response |
A | 0004930 | molecular_function | G protein-coupled receptor activity |
A | 0005886 | cellular_component | plasma membrane |
A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
A | 0016020 | cellular_component | membrane |
A | 0038023 | molecular_function | signaling receptor activity |
A | 0042593 | biological_process | glucose homeostasis |
A | 0050729 | biological_process | positive regulation of inflammatory response |
A | 0050921 | biological_process | positive regulation of chemotaxis |
A | 0051592 | biological_process | response to calcium ion |
A | 0060177 | biological_process | regulation of angiotensin metabolic process |
A | 0097009 | biological_process | energy homeostasis |
C | 0002001 | biological_process | renin secretion into blood stream |
C | 0002281 | biological_process | macrophage activation involved in immune response |
C | 0004930 | molecular_function | G protein-coupled receptor activity |
C | 0005886 | cellular_component | plasma membrane |
C | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
C | 0016020 | cellular_component | membrane |
C | 0038023 | molecular_function | signaling receptor activity |
C | 0042593 | biological_process | glucose homeostasis |
C | 0050729 | biological_process | positive regulation of inflammatory response |
C | 0050921 | biological_process | positive regulation of chemotaxis |
C | 0051592 | biological_process | response to calcium ion |
C | 0060177 | biological_process | regulation of angiotensin metabolic process |
C | 0097009 | biological_process | energy homeostasis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | binding site for residue OLC A 401 |
Chain | Residue |
A | TYR20 |
A | HOH549 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue OLC A 402 |
Chain | Residue |
A | LEU185 |
A | THR188 |
A | ILE246 |
A | ASN249 |
A | HOH550 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue OLC A 403 |
Chain | Residue |
A | THR39 |
A | ALA284 |
A | ILE288 |
A | PHE291 |
A | ARG298 |
A | VAL32 |
A | GLY36 |
site_id | AC4 |
Number of Residues | 9 |
Details | binding site for residue OLC A 404 |
Chain | Residue |
A | ILE92 |
A | ARG95 |
A | TYR96 |
A | TRP143 |
A | LEU151 |
A | MET153 |
A | LEU154 |
A | OLC407 |
C | OLC406 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue OLC A 405 |
Chain | Residue |
A | MET34 |
A | PHE38 |
A | CYS70 |
A | TYR86 |
site_id | AC6 |
Number of Residues | 8 |
Details | binding site for residue OLC A 406 |
Chain | Residue |
A | TRP10 |
A | PRO243 |
A | MET247 |
A | CYS263 |
A | SER264 |
A | HOH520 |
C | OLC402 |
C | OLC407 |
site_id | AC7 |
Number of Residues | 8 |
Details | binding site for residue OLC A 407 |
Chain | Residue |
A | LYS49 |
A | ASN50 |
A | TRP51 |
A | ASN60 |
A | LYS132 |
A | TRP143 |
A | OLC404 |
A | HOH523 |
site_id | AC8 |
Number of Residues | 9 |
Details | binding site for residue OLC A 408 |
Chain | Residue |
A | THR155 |
A | PHE156 |
A | THR158 |
A | GLY175 |
A | ASN176 |
A | TYR179 |
A | ILE182 |
A | LEU190 |
C | LEU232 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue GOL A 409 |
Chain | Residue |
A | GLU14 |
A | SER173 |
A | LYS269 |
A | ILE273 |
A | ARG276 |
A | HOH533 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue H95 A 410 |
Chain | Residue |
A | LYS225 |
A | ARG228 |
A | PHE291 |
A | HIS296 |
A | PHE297 |
A | ARG298 |
site_id | AD2 |
Number of Residues | 9 |
Details | binding site for residue OLC C 401 |
Chain | Residue |
A | ILE16 |
A | LEU17 |
A | TYR20 |
A | TYR21 |
C | LEU129 |
C | PHE134 |
C | ALA141 |
C | OLC402 |
C | OLC408 |
site_id | AD3 |
Number of Residues | 9 |
Details | binding site for residue OLC C 402 |
Chain | Residue |
A | SER238 |
A | VAL239 |
A | PRO243 |
A | THR275 |
A | OLC406 |
C | LEU140 |
C | VAL144 |
C | OLC401 |
C | OLC407 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue CLR C 403 |
Chain | Residue |
C | PHE111 |
C | LEU145 |
C | VAL198 |
C | OLC408 |
C | HOH529 |
site_id | AD5 |
Number of Residues | 9 |
Details | binding site for residue OLC C 404 |
Chain | Residue |
C | TYR44 |
C | LEU45 |
C | MET48 |
C | LYS49 |
C | TRP51 |
C | ASN60 |
C | LYS132 |
C | TRP143 |
C | OLC407 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue OLC C 405 |
Chain | Residue |
C | LYS205 |
C | OLC406 |
C | SER197 |
C | PHE201 |
C | TYR204 |
site_id | AD7 |
Number of Residues | 10 |
Details | binding site for residue OLC C 406 |
Chain | Residue |
A | LEU154 |
A | OLC404 |
C | LEU193 |
C | CYS200 |
C | TYR203 |
C | TYR204 |
C | SER238 |
C | THR242 |
C | OLC405 |
C | HOH547 |
site_id | AD8 |
Number of Residues | 6 |
Details | binding site for residue OLC C 407 |
Chain | Residue |
A | OLC406 |
C | TYR96 |
C | LEU140 |
C | TRP143 |
C | OLC402 |
C | OLC404 |
site_id | AD9 |
Number of Residues | 11 |
Details | binding site for residue OLC C 408 |
Chain | Residue |
C | SER53 |
C | TYR57 |
C | PHE111 |
C | ILE114 |
C | ASP115 |
C | LEU118 |
C | LEU129 |
C | PHE134 |
C | OLC401 |
C | CLR403 |
C | HOH502 |
site_id | AE1 |
Number of Residues | 9 |
Details | binding site for residue GOL C 409 |
Chain | Residue |
C | LYS18 |
C | VAL169 |
C | ASP170 |
C | SER173 |
C | LYS269 |
C | ILE273 |
C | ARG276 |
C | HOH514 |
C | HOH518 |
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. TSIlFLTFISIDRYLlM |
Chain | Residue | Details |
A | THR104-MET120 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 40 |
Details | TRANSMEM: Helical; Name=1 => ECO:0000255 |
Chain | Residue | Details |
A | ILE28-MET48 | |
C | ILE28-MET48 |
site_id | SWS_FT_FI2 |
Number of Residues | 120 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
Chain | Residue | Details |
A | LYS49-ASN55 | |
A | LYS121-GLU133 | |
A | TYR203-PRO226 | |
A | ARG298-LEU317 | |
C | LYS49-ASN55 | |
C | LYS121-GLU133 | |
C | TYR203-PRO226 | |
C | ARG298-LEU317 |
site_id | SWS_FT_FI3 |
Number of Residues | 40 |
Details | TRANSMEM: Helical; Name=2 => ECO:0000255 |
Chain | Residue | Details |
A | VAL56-ILE76 | |
C | VAL56-ILE76 |
site_id | SWS_FT_FI4 |
Number of Residues | 152 |
Details | TOPO_DOM: Extracellular => ECO:0000255 |
Chain | Residue | Details |
A | ARG77-HIS99 | |
A | THR155-LEU181 | |
A | ARG248-ARG276 | |
C | ARG77-HIS99 | |
C | THR155-LEU181 | |
C | ARG248-ARG276 |
site_id | SWS_FT_FI5 |
Number of Residues | 40 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000255 |
Chain | Residue | Details |
A | ALA100-MET120 | |
C | ALA100-MET120 |
site_id | SWS_FT_FI6 |
Number of Residues | 40 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000255 |
Chain | Residue | Details |
A | PHE134-LEU154 | |
C | PHE134-LEU154 |
site_id | SWS_FT_FI7 |
Number of Residues | 40 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000255 |
Chain | Residue | Details |
A | ILE182-PHE202 | |
C | ILE182-PHE202 |
site_id | SWS_FT_FI8 |
Number of Residues | 40 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000255 |
Chain | Residue | Details |
A | LEU227-MET247 | |
C | LEU227-MET247 |
site_id | SWS_FT_FI9 |
Number of Residues | 40 |
Details | TRANSMEM: Helical; Name=7 => ECO:0000255 |
Chain | Residue | Details |
A | PRO277-PHE297 | |
C | PRO277-PHE297 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN4 | |
C | ASN4 |