6A94
Crystal structure of 5-HT2AR in complex with zotepine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004930 | molecular_function | G protein-coupled receptor activity |
| A | 0004993 | molecular_function | G protein-coupled serotonin receptor activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0016020 | cellular_component | membrane |
| A | 0020037 | molecular_function | heme binding |
| A | 0022900 | biological_process | electron transport chain |
| B | 0004930 | molecular_function | G protein-coupled receptor activity |
| B | 0004993 | molecular_function | G protein-coupled serotonin receptor activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0016020 | cellular_component | membrane |
| B | 0020037 | molecular_function | heme binding |
| B | 0022900 | biological_process | electron transport chain |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | binding site for residue ZOT A 3001 |
| Chain | Residue |
| A | ASP155 |
| A | ASN343 |
| A | SER159 |
| A | LEU229 |
| A | VAL235 |
| A | GLY238 |
| A | SER242 |
| A | TRP336 |
| A | PHE339 |
| A | PHE340 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue CLR A 3002 |
| Chain | Residue |
| A | TYR111 |
| A | MET114 |
| A | ILE118 |
| A | LEU122 |
| A | TYR153 |
| A | PHE193 |
| A | ILE196 |
| A | TRP200 |
| A | VAL204 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue 1PE A 3003 |
| Chain | Residue |
| A | LEU261 |
| A | GLN262 |
| A | ALA265 |
| A | ILE315 |
| A | SER316 |
| A | GLN319 |
| A | GLU1004 |
| A | ASN1080 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 3004 |
| Chain | Residue |
| A | HIS182 |
| A | HIS183 |
| A | GLU264 |
| A | GLU318 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | binding site for residue ZOT B 3001 |
| Chain | Residue |
| B | ASP155 |
| B | VAL156 |
| B | SER159 |
| B | THR160 |
| B | LEU229 |
| B | VAL235 |
| B | GLY238 |
| B | SER242 |
| B | PHE339 |
| B | PHE340 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue PLM B 3002 |
| Chain | Residue |
| B | ILE395 |
| B | GLN396 |
| B | CYS397 |
| B | CLR3003 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue CLR B 3003 |
| Chain | Residue |
| B | ILE86 |
| B | TYR394 |
| B | TYR399 |
| B | PLM3002 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue A6L B 3004 |
| Chain | Residue |
| A | THR253 |
| A | LEU256 |
| B | TYR399 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 46 |
| Details | TRANSMEM: Helical; Name=1 => ECO:0000250 |
| Chain | Residue | Details |
| A | TRP76-VAL99 | |
| B | TRP76-VAL99 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 58 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000250 |
| Chain | Residue | Details |
| A | SER100-ASN110 | |
| A | ASP172-LYS191 | |
| B | SER100-ASN110 | |
| B | ASP172-LYS191 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 42 |
| Details | TRANSMEM: Helical; Name=2 => ECO:0000250 |
| Chain | Residue | Details |
| A | TYR111-MET132 | |
| B | TYR111-MET132 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 94 |
| Details | TOPO_DOM: Extracellular => ECO:0000250 |
| Chain | Residue | Details |
| A | LEU133-CYS148 | |
| A | GLN216-ASN233 | |
| A | VAL347-LEU362 | |
| B | LEU133-CYS148 | |
| B | GLN216-ASN233 | |
| B | VAL347-LEU362 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 44 |
| Details | TRANSMEM: Helical; Name=3 => ECO:0000250 |
| Chain | Residue | Details |
| A | ALA149-LEU171 | |
| B | ALA149-LEU171 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 46 |
| Details | TRANSMEM: Helical; Name=4 => ECO:0000250 |
| Chain | Residue | Details |
| A | ALA192-LEU215 | |
| B | ALA192-LEU215 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 40 |
| Details | TRANSMEM: Helical; Name=5 => ECO:0000250 |
| Chain | Residue | Details |
| A | PHE234-TYR254 | |
| B | PHE234-TYR254 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 42 |
| Details | TRANSMEM: Helical; Name=6 => ECO:0000250 |
| Chain | Residue | Details |
| A | LEU325-ALA346 | |
| B | LEU325-ALA346 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 42 |
| Details | TRANSMEM: Helical; Name=7 => ECO:0000250 |
| Chain | Residue | Details |
| A | ASN363-ASN384 | |
| B | ASN363-ASN384 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P41595 |
| Chain | Residue | Details |
| A | LEU229 | |
| B | ASP155 | |
| B | THR160 | |
| B | LEU229 | |
| A | ASP155 | |
| A | THR160 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | SITE: Hydrophobic barrier that decreases the speed of ligand binding and dissociation => ECO:0000269|PubMed:28129538 |
| Chain | Residue | Details |
| A | LEU229 | |
| B | LEU229 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | BINDING: axial binding residue |
| Chain | Residue | Details |
| A | TRP1007 | |
| A | ILE1102 | |
| B | TRP1007 | |
| B | ILE1102 |
