4Z9G
Crystal structure of human corticotropin-releasing factor receptor 1 (CRF1R) in complex with the antagonist CP-376395 in a hexagonal setting with translational non-crystallographic symmetry
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003796 | molecular_function | lysozyme activity |
| A | 0003824 | molecular_function | catalytic 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 | 0008152 | biological_process | metabolic process |
| A | 0009253 | biological_process | peptidoglycan catabolic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016787 | molecular_function | hydrolase activity |
| 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 |
| B | 0003796 | molecular_function | lysozyme activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004888 | molecular_function | transmembrane signaling receptor activity |
| B | 0004930 | molecular_function | G protein-coupled receptor activity |
| B | 0007166 | biological_process | cell surface receptor signaling pathway |
| B | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| B | 0008152 | biological_process | metabolic process |
| B | 0009253 | biological_process | peptidoglycan catabolic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0016998 | biological_process | cell wall macromolecule catabolic process |
| B | 0030430 | cellular_component | host cell cytoplasm |
| B | 0031640 | biological_process | killing of cells of another organism |
| B | 0042742 | biological_process | defense response to bacterium |
| B | 0044659 | biological_process | viral release from host cell by cytolysis |
| C | 0003796 | molecular_function | lysozyme activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004888 | molecular_function | transmembrane signaling receptor activity |
| C | 0004930 | molecular_function | G protein-coupled receptor activity |
| C | 0007166 | biological_process | cell surface receptor signaling pathway |
| C | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| C | 0008152 | biological_process | metabolic process |
| C | 0009253 | biological_process | peptidoglycan catabolic process |
| C | 0016020 | cellular_component | membrane |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| C | 0016998 | biological_process | cell wall macromolecule catabolic process |
| C | 0030430 | cellular_component | host cell cytoplasm |
| C | 0031640 | biological_process | killing of cells of another organism |
| C | 0042742 | biological_process | defense response to bacterium |
| C | 0044659 | biological_process | viral release from host cell by cytolysis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue OLA A 1201 |
| Chain | Residue |
| A | ARG227 |
| A | TRP229 |
| A | CYS233 |
| A | LYS314 |
| A | PHE358 |
| A | PHE365 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue OLA A 1202 |
| Chain | Residue |
| A | VAL136 |
| A | LEU140 |
| A | ASN157 |
| A | ILE232 |
| A | CYS364 |
| A | CYS128 |
| A | VAL132 |
| A | ALA133 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue OLA A 1203 |
| Chain | Residue |
| A | ASN157 |
| A | ALA160 |
| A | ILE163 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue 1Q5 A 1204 |
| Chain | Residue |
| A | PHE203 |
| A | GLY210 |
| A | LEU280 |
| A | ASN283 |
| A | LEU287 |
| A | THR316 |
| A | LEU320 |
| A | LEU323 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 1205 |
| Chain | Residue |
| A | THR1142 |
| A | PRO1143 |
| A | ASN1144 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 1206 |
| Chain | Residue |
| A | SER1038 |
| A | SER1040 |
| C | SER1036 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue OLA B 1201 |
| Chain | Residue |
| B | ILE232 |
| B | TRP236 |
| B | OLA1202 |
| C | CYS364 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue OLA B 1202 |
| Chain | Residue |
| B | LEU135 |
| B | PHE138 |
| B | ILE153 |
| B | OLA1201 |
| C | LEU140 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue OLA B 1203 |
| Chain | Residue |
| B | PHE365 |
| C | TRP229 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue 1Q5 B 1204 |
| Chain | Residue |
| B | PHE203 |
| B | MET206 |
| B | GLY210 |
| B | LEU280 |
| B | ASN283 |
| B | THR316 |
| B | LEU320 |
| B | LEU323 |
| site_id | AD2 |
| Number of Residues | 10 |
| Details | binding site for residue OLA C 1201 |
| Chain | Residue |
| B | VAL132 |
| B | ALA133 |
| B | VAL136 |
| B | LEU140 |
| B | CYS364 |
| C | LEU164 |
| C | ALA228 |
| C | ILE232 |
| C | TRP236 |
| C | OLA1202 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue OLA C 1202 |
| Chain | Residue |
| B | VAL136 |
| C | LEU135 |
| C | PHE138 |
| C | ILE153 |
| C | ASN157 |
| C | OLA1201 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue OLA C 1203 |
| Chain | Residue |
| C | HIS199 |
| C | GLN273 |
| C | LEU280 |
| C | TYR327 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue OLA C 1204 |
| Chain | Residue |
| B | TRP229 |
| B | CYS233 |
| C | VAL318 |
| C | PHE358 |
| C | VAL361 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue 1Q5 C 1205 |
| Chain | Residue |
| C | PHE203 |
| C | MET206 |
| C | GLY210 |
| C | ASN283 |
| C | THR316 |
| C | LEU323 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 C 1206 |
| Chain | Residue |
| A | SER1036 |
| B | SER1038 |
| B | LEU1039 |
| B | SER1040 |
| C | SER1038 |
| C | SER1040 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 90 |
| Details | TRANSMEM: Helical; Name=1 |
| Chain | Residue | Details |
| A | SER112-LEU142 | |
| B | SER112-LEU142 | |
| C | SER112-LEU142 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 135 |
| Details | TOPO_DOM: Cytoplasmic |
| Chain | Residue | Details |
| A | ARG143-PRO178 | |
| A | THR296-THR306 | |
| B | ARG143-PRO178 | |
| B | THR296-THR306 | |
| C | ARG143-PRO178 | |
| C | THR296-THR306 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 72 |
| Details | TRANSMEM: Helical; Name=2 |
| Chain | Residue | Details |
| A | GLU179-PHE203 | |
| B | GLU179-PHE203 | |
| C | GLU179-PHE203 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 105 |
| Details | TOPO_DOM: Extracellular |
| Chain | Residue | Details |
| A | PHE204-VAL218 | |
| A | ASP254-ASP269 | |
| A | VAL332-GLU338 | |
| B | PHE204-VAL218 | |
| B | ASP254-ASP269 | |
| B | VAL332-GLU338 | |
| C | PHE204-VAL218 | |
| C | ASP254-ASP269 | |
| C | VAL332-GLU338 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 84 |
| Details | TRANSMEM: Helical; Name=3 |
| Chain | Residue | Details |
| A | LEU219-GLY1028 | |
| B | LEU219-GLY1028 | |
| C | LEU219-GLY1028 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 81 |
| Details | TRANSMEM: Helical; Name=4 |
| Chain | Residue | Details |
| A | LEU226-TYR253 | |
| B | LEU226-TYR253 | |
| C | LEU226-TYR253 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 75 |
| Details | TRANSMEM: Helical; Name=5 |
| Chain | Residue | Details |
| A | TYR270-MET295 | |
| B | TYR270-MET295 | |
| C | TYR270-MET295 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 72 |
| Details | TRANSMEM: Helical; Name=6 |
| Chain | Residue | Details |
| A | ILE307-PHE331 | |
| B | ILE307-PHE331 | |
| C | ILE307-PHE331 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 87 |
| Details | TRANSMEM: Helical; Name=7 |
| Chain | Residue | Details |
| A | VAL339-SER368 | |
| B | VAL339-SER368 | |
| C | VAL339-SER368 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:14657255 |
| Chain | Residue | Details |
| A | SER301 | |
| B | SER301 | |
| C | SER301 |
