5EE7
Crystal structure of the human glucagon receptor (GCGR) in complex with the antagonist MK-0893
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003796 | molecular_function | lysozyme activity |
A | 0004888 | molecular_function | transmembrane signaling receptor activity |
A | 0004930 | molecular_function | G protein-coupled receptor activity |
A | 0007166 | biological_process | cell surface receptor signaling pathway |
A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
A | 0009253 | biological_process | peptidoglycan catabolic process |
A | 0016020 | cellular_component | membrane |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0016998 | biological_process | cell wall macromolecule catabolic process |
A | 0030430 | cellular_component | host cell cytoplasm |
A | 0031640 | biological_process | killing of cells of another organism |
A | 0042742 | biological_process | defense response to bacterium |
A | 0044659 | biological_process | viral release from host cell by cytolysis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 18 |
Details | binding site for residue 5MV A 1201 |
Chain | Residue |
A | GLY269 |
A | SER350 |
A | THR353 |
A | LEU399 |
A | ASN404 |
A | LYS405 |
A | OLA1211 |
A | OLA1212 |
A | OLA1214 |
A | HOH1313 |
A | ILE270 |
A | GLY273 |
A | ALA274 |
A | LEU277 |
A | LEU329 |
A | PHE345 |
A | ARG346 |
A | LYS349 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue OLA A 1202 |
Chain | Residue |
A | LEU268 |
A | OLA1214 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue OLA A 1203 |
Chain | Residue |
A | PHE289 |
A | ALA380 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue OLA A 1204 |
Chain | Residue |
A | HIS361 |
A | ASP385 |
A | LEU388 |
A | PHE391 |
site_id | AC5 |
Number of Residues | 8 |
Details | binding site for residue OLA A 1205 |
Chain | Residue |
A | THR146 |
A | SER150 |
A | PHE320 |
A | VAL323 |
A | ARG324 |
A | GLN327 |
A | OLA1206 |
A | OLA1209 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue OLA A 1206 |
Chain | Residue |
A | ARG324 |
A | OLA1205 |
A | HOH1309 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue OLA A 1207 |
Chain | Residue |
A | SER189 |
A | VAL326 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue OLA A 1208 |
Chain | Residue |
A | CYS171 |
A | THR172 |
A | ASN179 |
A | PHE264 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue OLA A 1209 |
Chain | Residue |
A | HIS250 |
A | ILE317 |
A | ARG324 |
A | OLA1205 |
site_id | AD1 |
Number of Residues | 3 |
Details | binding site for residue OLA A 1210 |
Chain | Residue |
A | ASP218 |
A | ARG225 |
A | LYS1058 |
site_id | AD2 |
Number of Residues | 2 |
Details | binding site for residue OLA A 1211 |
Chain | Residue |
A | 5MV1201 |
A | OLA1212 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue OLA A 1212 |
Chain | Residue |
A | PHE345 |
A | 5MV1201 |
A | OLA1211 |
A | OLA1213 |
site_id | AD4 |
Number of Residues | 3 |
Details | binding site for residue OLA A 1213 |
Chain | Residue |
A | LEU352 |
A | OLA1212 |
A | OLA1215 |
site_id | AD5 |
Number of Residues | 4 |
Details | binding site for residue OLA A 1214 |
Chain | Residue |
A | SER265 |
A | 5MV1201 |
A | OLA1202 |
A | HOH1301 |
site_id | AD6 |
Number of Residues | 3 |
Details | binding site for residue OLA A 1215 |
Chain | Residue |
A | LEU333 |
A | ARG334 |
A | OLA1213 |
site_id | AD7 |
Number of Residues | 13 |
Details | binding site for residue PE5 A 1216 |
Chain | Residue |
A | TYR145 |
A | TYR149 |
A | LYS187 |
A | ILE194 |
A | ARG199 |
A | ILE235 |
A | ASN238 |
A | TYR239 |
A | THR296 |
A | MET301 |
A | HIS361 |
A | PHE365 |
A | GLN392 |
site_id | AD8 |
Number of Residues | 7 |
Details | binding site for residue TLA A 1217 |
Chain | Residue |
A | ILE315 |
A | ASN318 |
A | PHE319 |
A | ILE355 |
A | PRO356 |
A | GLY359 |
A | VAL360 |
Functional Information from PROSITE/UniProt
site_id | PS00650 |
Number of Residues | 16 |
Details | G_PROTEIN_RECEP_F2_2 G-protein coupled receptors family 2 signature 2. QGLLVaVLYCFlNkeV |
Chain | Residue | Details |
A | GLN392-VAL407 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 24 |
Details | TRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451 |
Chain | Residue | Details |
A | GLY137-ALA161 |
site_id | SWS_FT_FI2 |
Number of Residues | 34 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451 |
Chain | Residue | Details |
A | ILE162-ALA173 | |
A | GLN327-SER350 |
site_id | SWS_FT_FI3 |
Number of Residues | 24 |
Details | TRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451 |
Chain | Residue | Details |
A | ASN174-LEU198 |
site_id | SWS_FT_FI4 |
Number of Residues | 54 |
Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451 |
Chain | Residue | Details |
A | ARG199-ARG225 | |
A | LYS286-PHE303 | |
A | ASP370-LYS381 |
site_id | SWS_FT_FI5 |
Number of Residues | 23 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451 |
Chain | Residue | Details |
A | VAL226-LEU249 |
site_id | SWS_FT_FI6 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451 |
Chain | Residue | Details |
A | PHE264-VAL285 |
site_id | SWS_FT_FI7 |
Number of Residues | 22 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451 |
Chain | Residue | Details |
A | TRP304-VAL326 |
site_id | SWS_FT_FI8 |
Number of Residues | 18 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451 |
Chain | Residue | Details |
A | THR351-THR369 |
site_id | SWS_FT_FI9 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451 |
Chain | Residue | Details |
A | LEU382-PHE402 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 |
Chain | Residue | Details |
A | GLU1009 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 |
Chain | Residue | Details |
A | ASP1018 |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8266098 |
Chain | Residue | Details |
A | LEU1030 | |
A | PHE1102 |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000303|PubMed:7831309 |
Chain | Residue | Details |
A | SER1115 | |
A | ASN1130 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 2 |
Details | M-CSA 921 |
Chain | Residue | Details |
A | GLU1009 | proton shuttle (general acid/base) |
A | ASP1018 | covalent catalysis |